|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
1.96e-124 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 354.01 E-value: 1.96e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSS-HVELRNITKSY----GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP 75
Cdd:COG1116 1 MSAAApALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 76 DRGMVFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPE 155
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRG--VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 156 ILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGPrSTIIADIEV 223
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP-GRIVEEIDV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-223 |
1.33e-112 |
|
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: 322.50 E-value: 1.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAA----EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMVFQ 82
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQG--VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 163 FGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMShGPRSTIIADIEV 223
Cdd:cd03293 159 FSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS-ARPGRIVAEVEV 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-213 |
1.36e-91 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 270.97 E-value: 1.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 5 SHVELRNITKSYGAA----EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMV 80
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRG--VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 161 EPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGP 213
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-223 |
6.27e-90 |
|
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: 265.48 E-value: 6.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMVFQHHALLPWMTAKGNIEFGLKSARP 105
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVDRVLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 106 QLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEAN 185
Cdd:TIGR01184 85 DLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEH 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1721987636 186 RRTVIMVTHDVDEAILLSDRILVMSHGPRSTIIADIEV 223
Cdd:TIGR01184 165 RVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-212 |
2.54e-89 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 268.12 E-value: 2.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 3 NSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GM 79
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnvGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRG--VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-212 |
7.11e-87 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 257.06 E-value: 7.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQH 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRG--VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-212 |
1.14e-81 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 248.52 E-value: 1.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA--PGPDR--GMVFQ 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnlPPRERrvGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIEFGLKSARPqlSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPP--SKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 163 FGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-212 |
2.56e-73 |
|
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: 223.27 E-value: 2.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQH 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpvNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKK--LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-212 |
5.49e-73 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 226.49 E-value: 5.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 5 SHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP-DRG--MVF 81
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPkDRNiaMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRK--VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 162 PFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDG 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-213 |
1.06e-71 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 219.96 E-value: 1.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMVFQHHALL 87
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 88 PWMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALD 167
Cdd:PRK11248 83 PWRNVQDNVAFGLQLA--GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721987636 168 ALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGP 213
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGP 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-212 |
1.15e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 213.75 E-value: 1.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY--GAAEVIA--PTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----- 77
Cdd:COG1136 5 LELRNLTKSYgtGEGEVTAlrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERElarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ----GMVFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:COG1136 85 rrhiGFVFQFFNLLPELTALENVALPLLLAG--VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 154 PEILLLDEPFGALDALTRRE-LQLqLRNVWEANRRTVIMVTHDvDEAILLSDRILVMSHG 212
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHD-PELAARADRVIRLRDG 220
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-212 |
9.15e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 216.89 E-value: 9.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGA---------------AEVIAPT---------SVHIDEGQ-FVsILGPSGCGKSTILSMIAGLAFPSTG 61
Cdd:COG4175 4 IEVRNLYKIFGKrperalklldqgkskDEILEKTgqtvgvndaSFDVEEGEiFV-IMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 62 EVFAAGHAVTAPGPDR---------GMVFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRR 132
Cdd:COG4175 83 EVLIDGEDITKLSKKElrelrrkkmSMVFQHFALLPHRTVLENVAFGLEIQG--VPKAERRERAREALELVGLAGWEDSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 133 PARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-212 |
1.23e-68 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 213.80 E-value: 1.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD---RGM--VF 81
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrRRIgyVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEfglksARPQL---SRAERSEIADQFLQQVGLAHA--ASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:COG1125 83 QQIGLFPHMTVAENIA-----TVPRLlgwDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 157 LLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-220 |
6.16e-68 |
|
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: 209.84 E-value: 6.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR--------G 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrrriG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPWMTAKGNIEFGLKsARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILL 158
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLR-EHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 159 LDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG---KIIAE 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-212 |
1.72e-67 |
|
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: 208.73 E-value: 1.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP-DR--GMVFQH 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqERnvGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKsARPQLSRAERSEI---ADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:cd03296 83 YALFRHMTVFDNVAFGLR-VKPRSERPPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 161 EPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-212 |
3.52e-67 |
|
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: 207.34 E-value: 3.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPT----SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----- 77
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQAlkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ----GMVFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAG--VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 154 PEILLLDEPFGALDALTRRE-LQLqLRNVWEANRRTVIMVTHDVDEAiLLSDRILVMSHG 212
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEvMEL-LRELNKEAGTTIVVVTHDPELA-EYADRIIELRDG 216
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-220 |
5.12e-67 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 211.43 E-value: 5.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 3 NSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP---DRGM 79
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPqkrDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRG--MGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG--------------PRSTIIAD 220
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGvieqvgtpqeiyrhPATPFVAD 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-212 |
5.57e-67 |
|
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: 207.54 E-value: 5.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAE-VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMV 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrkiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIefglkSARPQL---SRAERSEIADQFLQQVGL--AHAASRRPARLSGGMQQRVGLARAFAVDPE 155
Cdd:cd03295 81 IQQIGLFPHMTVEENI-----ALVPKLlkwPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 156 ILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNG 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-212 |
1.63e-66 |
|
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: 205.18 E-value: 1.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP-DR--GMVFQH 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkDRdiAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKSAR-PQLSRAERSEIADQFLQqvgLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKvPKDEIDERVREVAELLQ---IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 163 FGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-212 |
7.90e-66 |
|
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: 202.42 E-value: 7.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-------GM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrriGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPWMTAKGNIEFGlksarpqlsraerseiadqflqqvglahaasrrparLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-212 |
9.35e-66 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 208.01 E-value: 9.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVT-APGPDR--GMVFQH 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrLHARDRkvGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLkSARPQLSRAERSEI---ADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:PRK10851 83 YALFRHMTVFDNIAFGL-TVLPRRERPNAAAIkakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 161 EPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-212 |
1.16e-64 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 201.57 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVT-APGPDR--GMVFQH 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATrVHARDRkiGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKSARPqlSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKH--PKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNG 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-212 |
2.92e-64 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 204.80 E-value: 2.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVT-APGPDRGM 79
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 --VFQHHALLPWMTAKGNIEFGLK-SARPQLSRAERSEIAdqfLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:PRK09452 89 ntVFQSYALFPHMTVFENVAFGLRmQKTPAAEITPRVMEA---LRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 157 LLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-212 |
1.75e-63 |
|
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: 199.41 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYG---------------AAEVIAPT---------SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGE 62
Cdd:cd03294 1 IKIKGLYKIFGknpqkafkllakgksKEEILKKTgqtvgvndvSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 63 VFAAGHAVTAPGPDR---------GMVFQHHALLPWMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRP 133
Cdd:cd03294 81 VLIDGQDIAAMSRKElrelrrkkiSMVFQSFALLPHRTVLENVAFGLEVQ--GVPRAEREERAAEALELVGLEGWEHKYP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 134 ARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDG 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-224 |
1.82e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 198.36 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD-R---GMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRrriGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIEFgLKSARPqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:COG1131 81 EPALYPDLTVRENLRF-FARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 163 FGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHGprsTIIADIEVA 224
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERLCDRVAIIDKG---RIVADGTPD 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-212 |
1.97e-59 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 188.73 E-value: 1.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 9 LRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMVFQHHALLP 88
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 89 WMTAKGNIEFGLKSA-RPQlsraerseiADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALD 167
Cdd:PRK11247 95 WKKVIDNVGLGLKGQwRDA---------ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1721987636 168 ALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-212 |
4.55e-59 |
|
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: 187.16 E-value: 4.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIApTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQH 83
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRK--VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-212 |
4.75e-59 |
|
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: 186.94 E-value: 4.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR--------G 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPWMTAKGNIEFGLKSARpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILL 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHT-RLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 159 LDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-212 |
6.20e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.43 E-value: 6.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-------GM 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPWMTAKGNIEFGLKSARpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 160 DEPFGALD-ALTR------RELqlqlrnvweANR-RTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG1126 161 DEPTSALDpELVGevldvmRDL---------AKEgMTMVVVTHEMGFAREVADRVVFMDGG 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-220 |
6.33e-58 |
|
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: 184.07 E-value: 6.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHhallPW-----MTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPE 155
Cdd:COG1122 81 FQN----PDdqlfaPTVEEDVAFGPENLG--LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 156 ILLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDG---RIVAD 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-212 |
2.94e-57 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 186.08 E-value: 2.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG---PDR 77
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQHHALLPWMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEIL 157
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKML--GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 158 LLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
14-212 |
3.46e-57 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 186.21 E-value: 3.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 14 KSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---------GMVFQHH 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrkkiGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 ALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFG 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLG--WPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1721987636 165 ALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAG 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-225 |
5.20e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 181.88 E-value: 5.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAptSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQHH 84
Cdd:COG3840 3 RLDDLTYRYGDFPLRF--DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 ALLPWMTAKGNIEFGLKSARpQLSRAERSEIAdQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFG 164
Cdd:COG3840 81 NLFPHLTVAQNIGLGLRPGL-KLTAEQRAQVE-QALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 165 ALDALTRRE-LQLqLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIADIEVAT 225
Cdd:COG3840 159 ALDPALRQEmLDL-VDELCRERGLTVLMVTHDPEDAARIADRVLLVADG---RIAADGPTAA 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-212 |
8.27e-57 |
|
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: 189.34 E-value: 8.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPT-----SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---- 77
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRavddvSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ----GMVFQH--HALLPWMTAKGNIEFGLKsARPQLSRAERSEIADQFLQQVGL-AHAASRRPARLSGGMQQRVGLARAF 150
Cdd:COG1123 341 rrrvQMVFQDpySSLNPRMTVGDIIAEPLR-LHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 151 AVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDG 481
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-212 |
1.27e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 181.41 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-------- 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrrri 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQHHALLPWMTAKGNIEFG-------LKSARPQLSRAERsEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAF 150
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstWRSLLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 151 AVDPEILLLDEPFGALD-ALTRRELQLqLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG3638 162 VQEPKLILADEPVASLDpKTARQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-212 |
2.86e-56 |
|
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: 179.26 E-value: 2.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD----R---GM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRqkvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPWMTAKGNIEFGLKSARpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVK-GMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-212 |
4.32e-55 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 176.12 E-value: 4.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIA--PTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMV 80
Cdd:cd03225 1 ELKNLSFSYPDGARPAldDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQH--HALLpwM-TAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEIL 157
Cdd:cd03225 81 FQNpdDQFF--GpTVEEEVAFGLENL--GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 158 LLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-212 |
1.54e-54 |
|
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: 175.39 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY----GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----- 77
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ---GMVFQH--HALLPWMTAKGNIEFGLKSARPQLSRAERSEIADQFLQQVGLAHA-ASRRPARLSGGMQQRVGLARAFA 151
Cdd:cd03257 82 keiQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 152 VDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-212 |
1.94e-54 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 179.46 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVT-APGPDR--GMVFQH 83
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdVPPAERgvGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKsarpqLSRAERSEIaDQFLQQVG----LAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:PRK11000 84 YALYPHLSVAENMSFGLK-----LAGAKKEEI-NQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-212 |
9.76e-54 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 177.72 E-value: 9.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQH 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpiNMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDK--LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-212 |
1.40e-52 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 173.45 E-value: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 37 ILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQHHALLPWMTAKGNIEFGLKSARpqLSRAERS 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRK--VPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 114 EIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVT 193
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVT 158
|
170
....*....|....*....
gi 1721987636 194 HDVDEAILLSDRILVMSHG 212
Cdd:TIGR01187 159 HDQEEAMTMSDRIAIMRKG 177
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-212 |
8.06e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 168.31 E-value: 8.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-------- 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQHHALLPWMTAKGNIEFGLksarpQLSRAERSEI---ADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPL-----RVTGKSRKEIrrrVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 155 EILLLDEPFGALDALTRRELqLQLRNvwEANRR--TVIMVTHDVDeaiLLSD---RILVMSHG 212
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEI-MELLE--EINRRgtTVLIATHDLE---LVDRmpkRVLELEDG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-212 |
1.10e-51 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 168.13 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGL-----AFPSTGEVFAAGHAVTAPGPDR---- 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ---GMVFQHHALLPwMTAKGNIEFGLKsARPQLSRAERSEIADQFLQQVGLAHAASRR--PARLSGGMQQRVGLARAFAV 152
Cdd:cd03260 81 rrvGMVFQKPNPFP-GSIYDNVAYGLR-LHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 153 DPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
26-212 |
1.31e-51 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 171.41 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQHHALLPWMTAKGNIEFGLKS 102
Cdd:NF040840 20 SLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKrgiAYVYQNYMLFPHKTVFENIAFGLKL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 103 ARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVW 182
Cdd:NF040840 100 RK--VPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWH 177
|
170 180 190
....*....|....*....|....*....|
gi 1721987636 183 EANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:NF040840 178 REFGFTAIHVTHNFEEALSLADRVGIMLNG 207
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
26-212 |
1.60e-51 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 172.27 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVF---AAGHA--VTAPGPDR--------GMVFQHHALLPWMTA 92
Cdd:TIGR03415 44 SLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLvkdGDGSVdvANCDAATLrrlrthrvSMVFQQFALLPWRTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 93 KGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRR 172
Cdd:TIGR03415 124 EENVAFGLEMQ--GMPKAERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1721987636 173 ELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR03415 202 QLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEGG 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-212 |
2.99e-51 |
|
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: 166.99 E-value: 2.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPT----SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----- 77
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTAlkdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ---GMVFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:cd03258 82 rriGMIFQHFNLLSSRTVFENVALPLEIAG--VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 155 EILLLDEPFGALDALTRRE-LQLqLRNVweaNRR---TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03258 160 KVLLCDEATSALDPETTQSiLAL-LRDI---NRElglTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-212 |
4.59e-51 |
|
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: 165.93 E-value: 4.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 31 EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEV-------FAAGHAVTAPGPDR--GMVFQHHALLPWMTAKGNIEFGLK 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlFDSRKKINLPPQQRkiGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 102 sarpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNV 181
Cdd:cd03297 102 ----RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|.
gi 1721987636 182 WEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-224 |
4.69e-51 |
|
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: 166.90 E-value: 4.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAA----EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----- 77
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQH--HALLPWMTAKGNIEFGLKSARpqlsRAERSEIADQFLQQVGL-AHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRILAEPLRIHG----LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 155 EILLLDEPFGALDALTRRE-LQLqLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIADIEVA 224
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEiLNL-LKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG---RIVEELTVA 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-220 |
8.50e-51 |
|
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: 166.37 E-value: 8.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA-PGPDR----GMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELarriAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFGL---KSARPQLSRAERsEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILL 158
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRyphLGLFGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 159 LDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDG---RIVAQ 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-212 |
2.73e-50 |
|
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: 165.03 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----GMVFQH 83
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqiGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFgLKSARPqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:COG4555 83 RGLYDRLTVRENIRY-FAELYG-LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNvWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4555 161 NGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-212 |
3.15e-50 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 168.10 E-value: 3.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP-DRG--MVFQ 82
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPaDRDiaMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIEFGLKSARpqLSRAERSE-IA--------DQFLQqvglahaasRRPARLSGGMQQRVGLARAFAVD 153
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKIRG--MPKAEIEErVAeaarilelEPLLD---------RKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 154 PEILLLDEPFGALDALTRRELQLQLRnvwEANRR---TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQ---RLHRRlktTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-212 |
6.65e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 166.79 E-value: 6.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSY--GAAEVIA--PTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---- 77
Cdd:COG1135 1 MIELENLSKTFptKGGPVTAldDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ----GMVFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:COG1135 81 rrkiGMIFQHFNLLSSRTVAENVALPLEIAG--VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 154 PEILLLDEPFGALDALTRRE-LQLqLRNVweaNRR---TVIMVTH--DVDEAIllSDRILVMSHG 212
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSiLDL-LKDI---NRElglTIVLITHemDVVRRI--CDRVAVLENG 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-212 |
9.19e-50 |
|
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: 163.51 E-value: 9.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAA-EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR--------G 78
Cdd:cd03256 2 EVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrrqiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPWMTAKGNIEFG-------LKSARPQLSRAERsEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFA 151
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGrlgrrstWRSLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 152 VDPEILLLDEPFGALD-ALTRRELQLqLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03256 161 QQPKLILADEPVASLDpASSRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-212 |
5.63e-49 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 159.10 E-value: 5.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----GMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIefglksarpqlsraerseiadqflqqvglahaasrrpaRLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:cd03230 81 EPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 163 FGALDALTRRELQLQLRNvWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03230 123 TSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
7.27e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.41 E-value: 7.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMV 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHAL---LPwMTAKGNIEFGLKSARP---QLSRAERsEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMGRYGRRGlfrRPSRADR-EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 155 EILLLDEPFGALDALTRRELQLQLRNvWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-212 |
1.59e-48 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 160.26 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-------GM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPWMTAKGNIEFGLKSARpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVR-GASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-212 |
2.53e-48 |
|
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: 159.52 E-value: 2.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSH--VELRNITKSYGAAE----VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG 74
Cdd:COG4181 1 MSSSSApiIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 PDR---------GMVFQHHALLPWMTAKGNI-----EFGLKSARpqlsraersEIADQFLQQVGLAHAASRRPARLSGGM 140
Cdd:COG4181 81 EDArarlrarhvGFVFQSFQLLPTLTALENVmlpleLAGRRDAR---------ARARALLERVGLGHRLDHYPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 141 QQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAiLLSDRILVMSHG 212
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAG 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-212 |
1.07e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 157.29 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA-PGPD-R---GMVFQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEwRrqvAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPwMTAKGNIEFGLKSARPQLSRaersEIADQFLQQVGLAHAA-SRRPARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFDR----ERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 162 PFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-212 |
1.13e-47 |
|
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: 157.28 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIA--PTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----GMV 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAArqslGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIEF--GLKSarpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILL 158
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLKG----LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 159 LDEPFGALDALTRRElqlqlrnVWEA-----NRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03263 157 LDEPTSGLDPASRRA-------IWDLilevrKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-209 |
2.96e-47 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 156.10 E-value: 2.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGL---AFPSTGEVFAAGHAVTAPGPDR---GMVF 81
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEVLLNGRRLTALPAEQrriGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFGLksaRPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:COG4136 83 QDDLLFPHLSVGENLAFAL---PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 162 PFGALDAltrrELQLQLRN-VWEANRRT---VIMVTHDVDEAiLLSDRILVM 209
Cdd:COG4136 160 PFSKLDA----ALRAQFREfVFEQIRQRgipALLVTHDEEDA-PAAGRVLDL 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-212 |
2.99e-47 |
|
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: 160.27 E-value: 2.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 37 ILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV--TAPG----PDR---GMVFQHHALLPWMTAKGNIEFGLKSARPQL 107
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGiflpPHRrriGYVFQEARLFPHLSVRGNLLYGRKRAPRAE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 108 SRAERSEIADQFlqqvGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRR 187
Cdd:COG4148 110 RRISFDEVVELL----GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDI 185
|
170 180
....*....|....*....|....*
gi 1721987636 188 TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4148 186 PILYVSHSLDEVARLADHVVLLEQG 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-220 |
3.03e-46 |
|
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: 154.13 E-value: 3.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR------GMVF 81
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarlgiGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIE--------FGLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:cd03219 82 QIPRLFPELTVLENVMvaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 154 PEILLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVLDQG---RVIAE 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-212 |
1.61e-45 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 150.66 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTapgpdrgmvfqhhall 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 88 pwmtakgniefglksarpQLSRAERSE-IA--DQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFG 164
Cdd:cd03214 65 ------------------SLSPKELARkIAyvPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1721987636 165 ALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-212 |
1.42e-44 |
|
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: 147.39 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrrriGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 hhallpwmtakgniefglksarpqlsraerseiadqflqqvglahaasrrparLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 163 FGALDALTRRELQLQLRNVWEaNRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd00267 108 TSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-212 |
1.58e-44 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 149.24 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQHHALLPWMTAKGNIEFGLKs 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLGLH- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 103 arPQLS-RAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNV 181
Cdd:TIGR01277 97 --PGLKlNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180 190
....*....|....*....|....*....|.
gi 1721987636 182 WEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR01277 175 CSERQRTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
7-212 |
4.61e-44 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 148.17 E-value: 4.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVtAPGPDR-------- 77
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDV-NRLRGRqlpllrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -GMVFQHHALLPWMTAKGNIEFGLksarpQLSRAERSEIADQF---LQQVGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:TIGR02673 81 iGVVFQDFRLLPDRTVYENVALPL-----EVRGKKEREIQRRVgaaLRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 154 PEILLLDEPFGALDALTRRELqlqLRNVWEANRR--TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERI---LDLLKRLNKRgtTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-212 |
1.51e-43 |
|
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: 153.91 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY--GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPS---TGEVFAAGHAVTAP-----GPD 76
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELsealrGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 77 RGMVFQH--HALLPwMTAKGNIEFGLKsaRPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALE--NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 155 EILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-220 |
4.01e-43 |
|
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: 146.72 E-value: 4.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----GMV--F 81
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiarlGIArtF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFG-------------LKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLAR 148
Cdd:COG0411 86 QNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 149 AFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDeAIL-LSDRILVMSHGprsTIIAD 220
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD-LVMgLADRIVVLDFG---RVIAE 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-213 |
4.92e-43 |
|
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: 145.37 E-value: 4.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMVFQHHaLL 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRR-SI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 88 PW---MTAKGNIEFGL---KSARPQLSRAERsEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:cd03235 80 DRdfpISVRDVVLMGLyghKGLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 162 PFGALDALTRRELqLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGP 213
Cdd:cd03235 159 PFAGVDPKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-212 |
5.00e-43 |
|
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: 146.81 E-value: 5.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPT--SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTapGPDR------- 77
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKnvSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENlweirkk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -GMVFQHhallP-----WMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFA 151
Cdd:TIGR04520 79 vGMVFQN----PdnqfvGATVEDDVAFGLENL--GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 152 VDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAIlLSDRILVMSHG 212
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKG 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-219 |
9.10e-43 |
|
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: 144.82 E-value: 9.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGH-AVTAPGPDR---GMVFQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPREVRrriGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIEFglkSARPQ-LSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:cd03265 81 DLSVDDELTGWENLYI---HARLYgVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 162 PFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIA 219
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG---RIIA 212
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-220 |
2.06e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 145.67 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAA---EVIA--PTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---- 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfEKKAldDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ----GMVFQH--HALLPwMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHA-ASRRPARLSGGMQQRVGLARAF 150
Cdd:TIGR04521 81 rkkvGLVFQFpeHQLFE-ETVYKDIAFGPKNL--GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 151 AVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKG---KIVLD 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-195 |
2.33e-42 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 143.52 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 9 LRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---------GM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrreklGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKK--LSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHD 195
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEG-KTIIIVTHD 193
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-211 |
3.00e-42 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 143.00 E-value: 3.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----GMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIEFGLKSARPQLSRAErseiADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREA----IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 163 FGALDALTRRELQLQLRNvWEANRRTVIMVTHDVDEaiLLSDRILVMSH 211
Cdd:COG4133 159 FTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLE--LAAARVLDLGD 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-212 |
5.38e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.48 E-value: 5.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY--GAAEVIA--PTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----- 77
Cdd:PRK11153 2 IELKNISKVFpqGGRTIHAlnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ---GMVFQHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:PRK11153 82 rqiGMIFQHFNLLSSRTVFDNVALPLELAG--TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 155 EILLLDEPFGALD-ALTRRELQLqLRNVweaNRR---TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11153 160 KVLLCDEATSALDpATTRSILEL-LKDI---NRElglTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
6-212 |
7.14e-42 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 143.20 E-value: 7.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGL-----AFPSTGEVFAAGHAVTAPGPD---- 76
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIYDKKIDvvel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 77 R---GMVFQHHALLPwMTAKGNIEFGLKsARPQLSRAERSEIADQFLQQVGLAHA----ASRRPARLSGGMQQRVGLARA 149
Cdd:TIGR00972 81 RrrvGMVFQKPNPFP-MSIYDNIAYGPR-LHGIKDKKELDEIVEESLKKAALWDEvkdrLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 150 FAVDPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFYDG 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-220 |
3.26e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 141.26 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQHHALLPWMTAKGNIEFGLKS 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 103 ARpQLSRAERSEIAdQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRE-LQLqLRNV 181
Cdd:PRK10771 99 GL-KLNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEmLTL-VSQV 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1721987636 182 WEANRRTVIMVTHDVDEAIllsdRIlvmshGPRSTIIAD 220
Cdd:PRK10771 176 CQERQLTLLMVSHSLEDAA----RI-----APRSLVVAD 205
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-212 |
3.72e-41 |
|
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: 141.28 E-value: 3.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAA-EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-------- 77
Cdd:TIGR02315 2 LEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQHHALLPWMTAKGNIEFGLKSARP-------QLSRAERsEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAF 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllgRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 151 AVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-212 |
3.99e-41 |
|
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: 140.32 E-value: 3.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEViaPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQH 83
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKsarPQLS-RAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLS---PGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 163 FGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-163 |
9.12e-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: 137.39 E-value: 9.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMVFQHHALLPWMTAKGNIEFGL 100
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 101 KSARpqLSRAERSEIADQFLQQVGLAHAASRR----PARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:pfam00005 85 LLKG--LSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-212 |
2.06e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 143.64 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 12 ITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---------GMVFQ 82
Cdd:PRK10070 34 ILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrkkiAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELA--GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 163 FGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-212 |
3.84e-39 |
|
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: 134.05 E-value: 3.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYG--AAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GM 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPwMTAKGNIefglksarpqlsraerseiadqflqqvglahaasrrparLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:cd03228 81 VPQDPFLFS-GTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNvwEANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03228 121 DEATSALDPETEALILEALRA--LAKGKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
4.80e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.66 E-value: 4.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 2 TNSSHVELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-- 77
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ---GMVFQHhallP-----WMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARA 149
Cdd:PRK13632 83 kkiGIIFQN----PdnqfiGATVEDDIAFGLENKK--VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 150 FAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAIlLSDRILVMSHG 212
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEG 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-219 |
1.10e-38 |
|
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: 136.75 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 14 KSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPgPDR-----GMVFQHHALLP 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVRE-PRKvrrsiGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 89 WMTAKGNIEfgLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA 168
Cdd:TIGR01188 80 DLTGRENLE--MMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 169 LTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHGprsTIIA 219
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEG-VTILLTTHYMEEADKLCDRIAIIDHG---RIIA 204
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-212 |
1.64e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 134.93 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSH--VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV-TAPGPDR 77
Cdd:COG4598 1 MTDTAPpaLEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrLKPDRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -----------------GMVFQHHALLPWMTAKGNIEFG----LKsarpqLSRAERSEIADQFLQQVGLAHAASRRPARL 136
Cdd:COG4598 81 elvpadrrqlqrirtrlGMVFQSFNLWSHMTVLENVIEApvhvLG-----RPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 137 SGGMQQRVGLARAFAVDPEILLLDEPFGALDAltrrELqlqlrnVWEANR---------RTVIMVTHDVDEAILLSDRIL 207
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDP----EL------VGEVLKvmrdlaeegRTMLVVTHEMGFARDVSSHVV 225
|
....*
gi 1721987636 208 VMSHG 212
Cdd:COG4598 226 FLHQG 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-212 |
4.98e-38 |
|
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: 140.74 E-value: 4.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----G 78
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqiG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPwmtakGNIEFGLKSARPQLSRAErseiADQFLQQVGLAHAASRRP-----------ARLSGGMQQRVGLA 147
Cdd:COG2274 553 VVLQDVFLFS-----GTIRENITLGDPDATDEE----IIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDvDEAILLSDRILVMSHG 212
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVLDKG 685
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-230 |
5.97e-38 |
|
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: 136.01 E-value: 5.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 35 VSILGPSGCGKSTILSMIAGLAFPSTGEV-------FAAGHAVTAPGPDR--GMVFQHHALLPWMTAKGNIEFGLKSARP 105
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlFDSRKGIFLPPEKRriGYVFQEARLFPHLSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 106 QLSRAERSEIadqfLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEAN 185
Cdd:TIGR02142 106 SERRISFERV----IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1721987636 186 RRTVIMVTHDVDEAILLSDRILVMSHGPRSTIIADIEVATRSNHN 230
Cdd:TIGR02142 182 GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-212 |
6.75e-38 |
|
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: 131.96 E-value: 6.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---GMVFQH 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrriGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLPWMTAKGNIEFGLKSARpqlsraERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLG------IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNvWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03268 155 NGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-212 |
9.41e-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: 131.76 E-value: 9.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEV-IAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVtAPGPDR-------- 77
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGRaipylrrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -GMVFQHHALLPWMTAKGNIEFGLK--SARPQLSRAERSEIadqfLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:cd03292 80 iGVVFQDFRLLPDRNVYENVAFALEvtGVPPREIRKRVPAA----LELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 155 EILLLDEPFGALDALTRRELqLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEI-MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-212 |
1.61e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 132.93 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSshVELRNITKSYGAAE---VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG--- 74
Cdd:PRK13650 1 MSNI--IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 --PDRGMVFQHhallP-----WMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLA 147
Cdd:PRK13650 79 irHKIGMVFQN----PdnqfvGATVEDDVAFGLENK--GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEaILLSDRILVMSHG 212
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNG 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-212 |
8.73e-37 |
|
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: 136.43 E-value: 8.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 2 TNSSHVELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR--- 77
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 --GMVFQHHALLPwMTAKGNIEFGlksaRPQLSRAErseiADQFLQQVGLAHAASRRP-----------ARLSGGMQQRV 144
Cdd:COG4988 412 qiAWVPQNPYLFA-GTIRENLRLG----RPDASDEE----LEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 145 GLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDvDEAILLSDRILVMSHG 212
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHR-LALLAQADRILVLDDG 547
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-212 |
1.61e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 129.36 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV---TAPGP-------- 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDkairelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 76 DRGMVFQHHALLPWMTAKGN-IEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVL--GLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 155 EILLLDEPFGALDAltrrELQLQLRNVWEANRRTVI---MVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11124 161 QVLLFDEPTAALDP----EITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENG 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-209 |
2.53e-36 |
|
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: 130.94 E-value: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY----GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFP---STGEVFAAGHAVTAPGPD--- 76
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 77 --RG----MVFQH--HALLPWMTAKGNIEFGLKSARPqLSRAERSEIADQFLQQVGLAHAASR---RPARLSGGMQQRVG 145
Cdd:COG0444 82 kiRGreiqMIFQDpmTSLNPVMTVGDQIAEPLRIHGG-LSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 146 LARAFAVDPEILLLDEPFGALDALTRRE-LQLqLRNVWEANRRTVIMVTHDVDEAILLSDRILVM 209
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-212 |
7.91e-36 |
|
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: 133.74 E-value: 7.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSY--GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----G 78
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrrriA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPwMTAKGNiefgLKSARPQLSRAErseiADQFLQQVGLAHAASRRP-----------ARLSGGMQQRVGLA 147
Cdd:COG4987 413 VVPQRPHLFD-TTLREN----LRLARPDATDEE----LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELqlqLRNVWEANR-RTVIMVTHDvDEAILLSDRILVMSHG 212
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAgRTVLLITHR-LAGLERMDRILVLEDG 545
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-223 |
1.04e-35 |
|
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: 126.89 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----GMVF- 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarlGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 -QHHALLPWMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIRG--LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 161 EPFGALDALTRRELQ---LQLRnvweaNRRTVIMVT-HDVDEAILLSDRILVMS------HGPRSTIIADIEV 223
Cdd:cd03218 159 EPFAGVDPIAVQDIQkiiKILK-----DRGIGVLITdHNVRETLSITDRAYIIYegkvlaEGTPEEIAANELV 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-212 |
5.55e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.51 E-value: 5.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGH-----------AVTAPGP 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpsekAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 76 DRGMVFQHHALLPWMTAKGN-IEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLG--LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 155 EILLLDEPFGALD-ALTR------RELQlqlrnvweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4161 161 QVLLFDEPTAALDpEITAqvveiiRELS--------QTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-212 |
8.18e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.15 E-value: 8.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 2 TNSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILS-------MIAGLAFpsTGEVFAAGHAVTAPG 74
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 PD----R---GMVFQHHALLPwMTAKGNIEFGLKSARpQLSRAERSEIADQFLQQVGL---------AHAASrrparLSG 138
Cdd:COG1117 85 VDvvelRrrvGMVFQKPNPFP-KSIYDNVAYGLRLHG-IKSKSELDEIVEESLRKAALwdevkdrlkKSALG-----LSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 139 GMQQRVGLARAFAVDPEILLLDEPFGALDAL-TRR--ELQLQLRnvweaNRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKieELILELK-----KDYTIVIVTHNMQQAARVSDYTAFFYLG 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-212 |
1.38e-34 |
|
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: 123.54 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-GMVFQHHA 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 LLPWMTAKGN-IEFG-LKSarpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:cd03269 81 LYPKMKVIDQlVYLAqLKG----LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-220 |
4.41e-34 |
|
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: 123.27 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTG---EVFaaghavtapGPDRGMV--- 80
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF---------GERRGGEdvw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 -----------FQHHALLPWMTAK--------GNIefGLksaRPQLSRAERsEIADQFLQQVGLAHAASRRPARLSGGMQ 141
Cdd:COG1119 75 elrkriglvspALQLRFPRDETVLdvvlsgffDSI--GL---YREPTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 142 QRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG---RVVAA 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-220 |
8.56e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.57 E-value: 8.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA-PGPD----RGMVFQ 82
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAElarrRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHAL-LPWmTAKGNIEFGLksARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFA------VDPE 155
Cdd:PRK13548 84 HSSLsFPF-TVEEVVAMGR--APHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 156 ILLLDEPFGALDaLTRRELQLQL-RNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:PRK13548 161 WLLLDEPTSALD-LAHQHHVLRLaRQLAHERGLAVIVVLHDLNLAARYADRIVLLHQG---RLVAD 222
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-212 |
9.54e-34 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 122.61 E-value: 9.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSH--VELRNITKSYGAA--EVIAPTSVHID--EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHA----- 69
Cdd:COG4107 1 MTNEEQplLSVRGLSKRYGPGcgTVVACRDVSFDlyPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDggprd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 70 -VTAPGPDR--------GMVFQH--HALLPWMTAKGNIefglksARPQLSRAERS-----EIADQFLQQVGLAhaASR-- 131
Cdd:COG4107 81 lFALSEAERrrlrrtdwGMVYQNprDGLRMDVSAGGNI------AERLMAAGERHygdirARALEWLERVEIP--LERid 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 132 -RPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALD-ALTRRELQLQLRNVWEaNRRTVIMVTHDVDEAILLSDRILVM 209
Cdd:COG4107 153 dLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDvSVQARLLDLIRRLQRE-LGLSMIVVTHDLGVIRLLADRTMVM 231
|
...
gi 1721987636 210 SHG 212
Cdd:COG4107 232 KNG 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-212 |
2.19e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.05 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPT--SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG-----PDRGM 79
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKdvSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHhallP-----WMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:PRK13635 86 VFQN----PdnqfvGATVQDDVAFGLENI--GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 155 EILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAiLLSDRILVMSHG 212
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKG 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-212 |
2.65e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 121.38 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD-----RGMVFQ 82
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrRAVLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHAL-LPWmTAKGNIEFGLksARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFA-----VDPE- 155
Cdd:COG4559 83 HSSLaFPF-TVEEVVALGR--APHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepVDGGp 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 156 -ILLLDEPFGALDaltrreLQLQLRnVWEANRR------TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4559 160 rWLFLDEPTSALD------LAHQHA-VLRLARQlarrggGVVAVLHDLNLAAQYADRILLLHQG 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-212 |
3.50e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 126.43 E-value: 3.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSYGAAE-VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GM 79
Cdd:COG1132 339 EIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrrqiGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPwMTAKGNIEFGlksaRPQLSRAErseI--------ADQFLQQV--GLAHAASRRPARLSGGMQQRVGLARA 149
Cdd:COG1132 419 VPQDTFLFS-GTIRENIRYG----RPDATDEE---VeeaakaaqAHEFIEALpdGYDTVVGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 150 FAVDPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRL-STIRNADRILVLDDG 550
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-223 |
3.57e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.52 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA-PGPDR---GM---- 79
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPMHKRarlGIgylp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 ----VFQHhallpwMTAKGNIEFGLKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPE 155
Cdd:COG1137 85 qeasIFRK------LTVEDNILAVLELRK--LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 156 ILLLDEPFGALDALTRRELQ---LQLRnvweaNRRTVIMVT-HDVDEAILLSDR--IL----VMSHGPRSTIIADIEV 223
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQkiiRHLK-----ERGIGVLITdHNVRETLGICDRayIIsegkVLAEGTPEEILNNPLV 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-212 |
4.27e-33 |
|
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: 119.78 E-value: 4.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAE----VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAG-HAVTAPGPDR---G 78
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPWMTAKGNIEF--GLKSARPQLSRAERSEIADQFlqqvGLAHAASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLEELADRL----GMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 157 LLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALG-KCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-209 |
1.55e-32 |
|
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: 124.32 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 4 SSHVELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR----- 77
Cdd:TIGR02857 319 ASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqi 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQHhallPWMTAKG---NIEFGLKSARP-QLSRAERSEIADQFLQQV--GLAHAASRRPARLSGGMQQRVGLARAFA 151
Cdd:TIGR02857 399 AWVPQH----PFLFAGTiaeNIRLARPDASDaEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 152 VDPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDvDEAILLSDRILVM 209
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-195 |
1.56e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 125.22 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSY----GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR------ 77
Cdd:PRK10535 6 ELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ---GMVFQHHALLPWMTAKGNIEfgLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:PRK10535 86 ehfGFIFQRYHLLSHLTAAQNVE--VPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721987636 155 EILLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHD 195
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRG-HTVIIVTHD 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-212 |
1.59e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 119.03 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV-TAPGPDRGMVF---- 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKRLailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFGlksaR-P----QLSRAERsEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:COG4604 82 QENHINSRLTVRELVAFG----RfPyskgRLTAEDR-EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 157 LLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDG 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-212 |
2.23e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 118.70 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 5 SHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR------- 77
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ------GMVFQHHALLPWMTAKGNIEFGLKSARPQlSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFA 151
Cdd:PRK11264 82 qlrqhvGFVFQNFNLFPHRTVLENIIEGPVIVKGE-PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 152 VDPEILLLDEPFGALDALTRRELQLQLRNVWEaNRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-212 |
7.37e-32 |
|
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: 114.83 E-value: 7.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR------GMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarragiAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQhhallpwmtakgniefglksarpqlsraerseiadqflqqvglahaasrrparLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:cd03216 81 YQ-----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 161 EPFGALDALTRRELQLQLRNVwEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-212 |
9.47e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.67 E-value: 9.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAaeVIAPTSVHID--EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR------G 78
Cdd:COG3845 6 LELRGITKRFGG--VVANDDVSLTvrPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaialgiG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPWMTAKGNIEFGL---KSARPQLSRAER--SEIADQFlqqvGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARAriRELSERY----GLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 154 PEILLLDEP------------FGALDALTrrelqlqlrnvweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG3845 160 ARILILDEPtavltpqeadelFEILRRLA-------------AEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-209 |
1.03e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.41 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 15 SYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTApgpdrgMVFQHHAL---LPwMT 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA------YVPQRSEVpdsLP-LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 92 AKGNIEFGLKSARP---QLSRAERSEIADQfLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA 168
Cdd:NF040873 74 VRDLVAMGRWARRGlwrRLTRDDRAAVDDA-LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721987636 169 LTRRELqLQLRNVWEANRRTVIMVTHDvDEAILLSDRILVM 209
Cdd:NF040873 153 ESRERI-IALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-212 |
1.27e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.17 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGhavtAPGPDR--------G 78
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG----VPVPARarlarariG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPWMTAKGNI-----EFGLkSARpqlsraERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLlvfgrYFGM-STR------EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 154 PEILLLDEPFGALDALTRRELQLQLRNVWeANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-212 |
3.69e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.47 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---------GMVFQH-HALLPWMTAKGN 95
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrkkvSLVFQFpEAQLFENTVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 96 IEFGLKSArpQLSRAERSEIADQFLQQVGLAHA-ASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRREL 174
Cdd:PRK13641 107 VEFGPKNF--GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 1721987636 175 qLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13641 185 -MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-212 |
1.25e-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: 113.30 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR------GMVF 81
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragiGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFGLKSARPQLSRAERSEIADQF--LQQVglahaASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFprLKER-----RKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVweaNRR--TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIREL---RDEgvTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-212 |
1.89e-30 |
|
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: 112.67 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVsILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTApGPDR-----GMVF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKlrrriGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAkgnIEFGLKSARPQ-LSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:cd03264 79 QEFGVYPNFTV---REFLDYIAWLKgIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 161 EPFGALDALTR---RELQLQLrnvweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03264 156 EPTAGLDPEERirfRNLLSEL-----GEDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-199 |
1.94e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 113.34 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGAAE----VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD 76
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 77 R---------GMVFQHHALLPWMTAKGNIEFglksarPQLSRAERS----EIADQFLQQVGLAHAASRRPARLSGGMQQR 143
Cdd:PRK10584 81 AraklrakhvGFVFQSFMLIPTLNALENVEL------PALLRGESSrqsrNGAKALLEQLGLGKRLDHLPAQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 144 VGLARAFAVDPEILLLDEPFGALDALTRRELQLQLrnvWEANRR---TVIMVTHDVDEA 199
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL---FSLNREhgtTLILVTHDLQLA 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
26-209 |
2.64e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 115.21 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR--------GMVFQ--HHALLPWMTAKGN 95
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrrrmQMVFQdpYASLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 96 IEFGLKSARpQLSRAERSEIADQFLQQVGL-AHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA------ 168
Cdd:COG4608 118 IAEPLRIHG-LASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaqv 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 169 ------LtRRELQLqlrnvweanrrTVIMVTHD--VDEAIllSDRILVM 209
Cdd:COG4608 197 lnlledL-QDELGL-----------TYLFISHDlsVVRHI--SDRVAVM 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-224 |
2.71e-30 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 113.75 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 5 SHVELRNITKSY---------GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP 75
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 76 --------DRGMVFQ--HHALLPWMTAKGNIEFGLKSARpQLSRAERSEIADQFLQQVGL-AHAASRRPARLSGGMQQRV 144
Cdd:TIGR02769 81 kqrrafrrDVQLVFQdsPSAVNPRMTVRQIIGEPLRHLT-SLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 145 GLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIADIEVA 224
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG---QIVEECDVA 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-212 |
7.85e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.28 E-value: 7.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD--------RG 78
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeeRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 mvfqhhaLLPWMTAKGNIEF--GLKsarpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:COG4152 82 -------LYPKMKVGEQLVYlaRLK----GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 157 LLLDEPFGALDALTRRELQ---LQLRnvweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKdviRELA----AKGTTVIFSSHQMELVEELCDRIVIINKG 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-220 |
9.40e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.14 E-value: 9.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP-----DRGM 79
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPadlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLpWMTAKGNIEFGLKSARPQ-LSRAERSEIADQFLQQ--VGLAHAASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLADDErILRAAELAGVTDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 157 LLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVdeAIL-LSDRILVMSHGprsTIIAD 220
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRP--SLLdLVDRIIVMDSG---RIVAD 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-212 |
1.84e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.06 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-------GMVFQH--HALLPWMTAKgNI 96
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdirkkvGLVFQYpeYQLFEETIEK-DI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 97 EFGLKsaRPQLSRAERSEIADQFLQQVGLAHA--ASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRREL 174
Cdd:PRK13637 106 AFGPI--NLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEI 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1721987636 175 QLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13637 184 LNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
11-212 |
2.13e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 111.26 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 11 NITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRgmVFQHHALLPW- 89
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLALLPQh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 90 -MTAKGN-----IEFGlKSarPQLS-----RAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILL 158
Cdd:PRK11231 85 hLTPEGItvrelVAYG-RS--PWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 159 LDEPFGALDALTRRELQLQLRNVwEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-212 |
3.12e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 110.29 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 3 NSSHVELRNITKSYG----AAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV-----TAP 73
Cdd:PRK11629 2 NKILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 74 GPDR----GMVFQHHALLPWMTAKGNIefglksARPQL----SRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVG 145
Cdd:PRK11629 82 AELRnqklGFIYQFHHLLPDFTALENV------AMPLLigkkKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 146 LARAFAVDPEILLLDEPFGALDALTRRELqLQLrnVWEANRR---TVIMVTHDVDEAILLSdRILVMSHG 212
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSI-FQL--LGELNRLqgtAFLVVTHDLQLAKRMS-RQLEMRDG 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-209 |
5.25e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP----DRG--MV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaqAAGiaII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIEFG-LKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 160 DEPfgaLDALTRRELQL------QLRnvweANRRTVIMVTHDVDEAILLSDRILVM 209
Cdd:COG1129 165 DEP---TASLTEREVERlfriirRLK----AQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-212 |
7.51e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.67 E-value: 7.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 14 KSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRG--------------- 78
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadknqlrllrt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 ---MVFQHHALLPWMTAKGNIefglKSARPQ---LSRAERSEIADQFLQQVGLAHAASRR-PARLSGGMQQRVGLARAFA 151
Cdd:PRK10619 93 rltMVFQHFNLWSHMTVLENV----MEAPIQvlgLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 152 VDPEILLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG-KTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-204 |
1.48e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.08 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR--------G 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrkrmS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPWMTAKGNIEFGLKSaRPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILL 158
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLRE-HTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721987636 159 LDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSD 204
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-230 |
1.78e-28 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 108.09 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAA-EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGH---AVTAPGPDR--GMV 80
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirEVTLDSLRRaiGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPwMTAKGNIEFGLKSARPQ--LSRAERSEIADQFLQ-------QVGlahaasRRPARLSGGMQQRVGLARAFA 151
Cdd:cd03253 81 PQDTVLFN-DTIGYNIRYGRPDATDEevIEAAKAAQIHDKIMRfpdgydtIVG------ERGLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 152 VDPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVDEaILLSDRILVMSHGprstiiadiEVATRSNHN 230
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLST-IVNADKIIVLKDG---------RIVERGTHE 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-212 |
2.54e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 107.27 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVT------APGPDR-- 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknreVPFLRRqi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQHHALLPWMTAKGNIEFGLKSARPQLSRAERSEIADqfLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEIL 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAA--LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 158 LLDEPFGALDALTRRELqlqLRNVWEANR--RTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10908 160 LADEPTGNLDDALSEGI---LRLFEEFNRvgVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-219 |
3.28e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.95 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfAAGHAVTAPG-------PDR---GMVFQ--HHALLPWMTAK 93
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-TIGERVITAGkknkklkPLRkkvGIVFQfpEHQLFEETVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 94 gNIEFGlksarPQ---LSRAERSEIADQFLQQVGLAHAA-SRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDAL 169
Cdd:PRK13634 106 -DICFG-----PMnfgVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 170 TRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIA 219
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKG---TVFL 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
3.84e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.30 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSY--GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG---- 74
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfekl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 -PDRGMVFQH-HALLPWMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAV 152
Cdd:PRK13648 82 rKHIGIVFQNpDNQFVGSIVKYDVAFGLENH--AVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 153 DPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAiLLSDRILVMSHG 212
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-212 |
7.68e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 109.19 E-value: 7.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 37 ILGPSGCGKSTILSMIAGLAFPSTGEVFAAGH-------AVTAPGPDR--GMVFQHHALLPWMTAKGNIEFGLKSARPql 107
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekGICLPPEKRriGYVFQDARLFPHYKVRGNLRYGMAKSMV-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 108 sraerseiaDQFLQQV---GLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEA 184
Cdd:PRK11144 107 ---------AQFDKIVallGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180
....*....|....*....|....*...
gi 1721987636 185 NRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-228 |
1.12e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.71 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAA---EVIAPTSV--HIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA-PGPDR--- 77
Cdd:COG1101 2 LELKNLSKTFNPGtvnEKRALDGLnlTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKRaky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -GMVFQHhallPWM-TAKG-NIE------------FGLKSArpqLSRAERSEIADQfL------------QQVGLahaas 130
Cdd:COG1101 82 iGRVFQD----PMMgTAPSmTIEenlalayrrgkrRGLRRG---LTKKRRELFREL-LatlglglenrldTKVGL----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 131 rrparLSGGMQQRVGLARAFAVDPEILLLDEPFGALD--------ALTRRelqlqlrnVWEANRRTVIMVTHDVDEAILL 202
Cdd:COG1101 149 -----LSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktaalvlELTEK--------IVEENNLTTLMVTHNMEQALDY 215
|
250 260
....*....|....*....|....*.
gi 1721987636 203 SDRILVMSHGprsTIIADIEVATRSN 228
Cdd:COG1101 216 GNRLIMMHEG---RIILDVSGEEKKK 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-212 |
1.28e-27 |
|
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: 110.54 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAfPSTGEVFAAGHAVTAPGPDRG--------MVFQ--HHALLPWMTAKGN 95
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALrplrrrmqVVFQdpFGSLSPRMTVGQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 96 IEFGLKSARPQLSRAERSEIADQFLQQVGL-AHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRE- 173
Cdd:COG4172 385 IAEGLRVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQi 464
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721987636 174 LQLqLRNVWEANRRTVIMVTHD--VDEAilLSDRILVMSHG 212
Cdd:COG4172 465 LDL-LRDLQREHGLAYLFISHDlaVVRA--LAHRVMVMKDG 502
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-212 |
1.71e-27 |
|
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: 105.39 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV---TAPGPDR--GM 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASLRRqiGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHhALLPWMTAKGNIEFGLKSA-RPQLSRAERSEIADQFLQQV--GLAHAASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:cd03251 81 VSQD-VFLFNDTVAENIAYGRPGAtREEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 157 LLLDEPFGALDALTRRELQLQLRNVWEanRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRL-STIENADRIVVLEDG 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-221 |
2.95e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.81 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVtaPGPDR------GMV 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV--PSRARharqrvGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIE-----FGlksarpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPE 155
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLvfgryFG-------LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 156 ILLLDEPFGALDALTRRELQLQLRNVWeANRRTVIMVTHDVDEAILLSDRILVMSHG-------PRSTIIADI 221
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGrkiaegaPHALIESEI 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-212 |
3.11e-27 |
|
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: 104.66 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 19 AEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPS---TGEVFAAGHAVTAPG-PDR-GMVFQHHALLPWMTAK 93
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQfQKCvAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 94 GNIEFGLKSARPQLSR-AERSEIADQF-LQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTR 171
Cdd:cd03234 100 ETLTYTAILRLPRKSSdAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721987636 172 RELQLQLRNVWEANrRTVIMVTHDVDEAIL-LSDRILVMSHG 212
Cdd:cd03234 180 LNLVSTLSQLARRN-RIVILTIHQPRSDLFrLFDRILLLSSG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-228 |
3.81e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.54 E-value: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-------G 78
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlevrktvG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQH---HALLPwmTAKGNIEFG-LKSARPQLSRAERSEIAdqfLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:PRK13639 82 IVFQNpddQLFAP--TVEEDVAFGpLNLGLSKEEVEKRVKEA---LKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 155 EILLLDEPFGALDALTRRELqlqLRNVWEANRR--TVIMVTHDVDEAILLSDRILVMSHG-------PRStIIADIEVAT 225
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQI---MKLLYDLNKEgiTIIISTHDVDLVPVYADKVYVMSDGkiikegtPKE-VFSDIETIR 232
|
...
gi 1721987636 226 RSN 228
Cdd:PRK13639 233 KAN 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-212 |
4.27e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.15 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 17 GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA-PGPDRG-------MVFQHH--AL 86
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKafrrdiqMVFQDSisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 87 LPWMTAKGNIEFGLKSARpQLSRAERSEIADQFLQQVGLAHA-ASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGA 165
Cdd:PRK10419 103 NPRKTVREIIREPLRHLL-SLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 166 LDaltrRELQLQLRNVWEANRR----TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10419 182 LD----LVLQAGVIRLLKKLQQqfgtACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-212 |
5.66e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 104.69 E-value: 5.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 29 IDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA-PG---PDRGMV--FQHHALLPWMTA---------- 92
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGhqiARMGVVrtFQHVRLFREMTVienllvaqhq 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 93 --KGNIEFGLkSARPQLSRAERS--EIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA 168
Cdd:PRK11300 108 qlKTGLFSGL-LKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1721987636 169 LTRRELQ---LQLRNVWEAnrrTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11300 187 KETKELDeliAELRNEHNV---TVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-204 |
7.15e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.54 E-value: 7.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGL-----AFPSTGEVFAAGHAVTAPGPDR---- 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPievr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ---GMVFQHHALLPWMTAKGNIEFGLKSARPQLSRAERSEIADQFLQQVGLAHAASRR----PARLSGGMQQRVGLARAF 150
Cdd:PRK14267 85 revGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 151 AVDPEILLLDEPFGALDALTRR---ELQLQLRNVWeanrrTVIMVTHDVDEAILLSD 204
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAkieELLFELKKEY-----TIVLVTHSPAQAARVSD 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-212 |
8.51e-27 |
|
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: 102.01 E-value: 8.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTapgpdrgmvfqhh 84
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 allpwmTAKGNIE--FGLKSARPQLsraerseIADQFLQQVGlahaasrrpARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:cd03247 68 ------DLEKALSslISVLNQRPYL-------FDTTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 163 FGALDALTRRELqlqLRNVWEANR-RTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03247 126 TVGLDPITERQL---LSLIFEVLKdKTLIWITHHL-TGIEHMDKILFLENG 172
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
8-212 |
1.17e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 104.15 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSY---------GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTaPGpDRG 78
Cdd:COG4167 6 EVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE-YG-DYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 -------MVFQH--HALLPWMTAKGNIEFGLKSArPQLSRAERSEIADQFLQQVGL-AHAASRRPARLSGGMQQRVGLAR 148
Cdd:COG4167 84 yrckhirMIFQDpnTSLNPRLNIGQILEEPLRLN-TDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALAR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 149 AFAVDPEILLLDEPFGALDALTRRE-----LQLQlrnvwEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4167 163 ALILQPKIIIADEALAALDMSVRSQiinlmLELQ-----EKLGISYIYVSQHLGIVKHISDKVLVMHQG 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-212 |
1.19e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.94 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAfpsTGE------VFAAGHAVTAPG------ 74
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDksagshIELLGRTVQREGrlardi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 ----PDRGMVFQHHALLPWMTAKGNIEFGLKSARP-------QLSRAERSEiADQFLQQVGLAHAASRRPARLSGGMQQR 143
Cdd:PRK09984 82 rksrANTGYIFQQFNLVNRLSVLENVLIGALGSTPfwrtcfsWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 144 VGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-229 |
1.29e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.84 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 5 SHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLA--FPS---TGEVFAAGHA-----VTAPG 74
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelYPEarvSGEVYLDGQDifkmdVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 PDRGMVFQHHALLPWMTAKGNIEFGLKSARPQLSRAERSEIADQFLQQVGLAHAASRR---PA-RLSGGMQQRVGLARAF 150
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 151 AVDPEILLLDEPFGALDALTR---RELQLQLRnvweaNRRTVIMVTHDVDEAILLSDRILVMSHGPRSTIIADIEVATRS 227
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTakiESLFLELK-----KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
..
gi 1721987636 228 NH 229
Cdd:PRK14247 237 RH 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-195 |
1.34e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 9 LRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTapgpdrGMVFQHHALLP 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRI------GYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 89 WMTAKGNIEFGLKSARPQLSRAER---------------SEIADQF---------------LQQVGLAHAASRRP-ARLS 137
Cdd:COG0488 75 DLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlAELQEEFealggweaearaeeiLSGLGFPEEDLDRPvSELS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 138 GGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNvweaNRRTVIMVTHD 195
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHD 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-212 |
1.53e-26 |
|
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: 101.52 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMV 80
Cdd:cd03246 2 EVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhvGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWmTAKGNIefglksarpqlsraerseiadqflqqvglahaasrrparLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:cd03246 82 PQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 161 EPFGALDALTRRELQLQLRNVwEANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVLEDG 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-212 |
1.68e-26 |
|
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: 103.00 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGA---AEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----G 78
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrsqiG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPwMTAKGNIEFGLKSA-RPQLSRAERSEIADQFLQ--------QVGlahaasRRPARLSGGMQQRVGLARA 149
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKPDAtDEEVEEAAKKANIHDFIMslpdgydtLVG------ERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 150 FAVDPEILLLDEPFGALDALTRRELQLQLRNVWEAnrRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKG--RTTIVIAHRL-STIRNADLIAVLQNG 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-204 |
4.12e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.55 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 2 TNSSHVELR--NITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTIL-------SMIAGlaFPSTGEVFAAGHAVTA 72
Cdd:PRK14243 4 LNGTETVLRteNLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPG--FRVEGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 73 PGPDR-------GMVFQHHALLPwMTAKGNIEFG-----LKSARPQLsrAERS--------EIADQfLQQVGLAhaasrr 132
Cdd:PRK14243 82 PDVDPvevrrriGMVFQKPNPFP-KSIYDNIAYGaringYKGDMDEL--VERSlrqaalwdEVKDK-LKQSGLS------ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 133 parLSGGMQQRVGLARAFAVDPEILLLDEPFGALDAL-TRR--ELQLQLRnvweaNRRTVIMVTHDVDEAILLSD 204
Cdd:PRK14243 152 ---LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIsTLRieELMHELK-----EQYTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-212 |
4.35e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 3 NSSHVELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFP---STGEVFAAGHAVTAPG--- 74
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTvwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 -PDR-GMVFQHhallP-----WMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLA 147
Cdd:PRK13640 82 iREKvGIVFQN----PdnqfvGATVGDDVAFGLENR--AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAIlLSDRILVMSHG 212
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDG 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-212 |
4.95e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.86 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG-----PDRGMVFQH-HALLPWMTAKGNIEFG 99
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIGMVFQNpDNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 100 LKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLR 179
Cdd:PRK13642 107 MENQ--GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH 184
|
170 180 190
....*....|....*....|....*....|...
gi 1721987636 180 NVWEANRRTVIMVTHDVDEAIlLSDRILVMSHG 212
Cdd:PRK13642 185 EIKEKYQLTVLSITHDLDEAA-SSDRILVMKAG 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-212 |
5.12e-26 |
|
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: 101.60 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR------GMVF 81
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgiGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFGLKSARPQLSRAERSE-IADQFLQqvgLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYARRDRAEVRADLErVYELFPR---LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 161 EPFGALDALTRRELQLQLRnvwEANRR--TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIR---RLNREgvTILLVEQNARFALEIADRAYVLERG 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-212 |
6.43e-26 |
|
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: 99.81 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITksygAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP----DRGMVF- 81
Cdd:cd03215 5 LEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdaiRAGIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 ----QHHALLPWMTAKGNIEFglksarpqlsraerseiadqflqqvglahaasrrPARLSGGMQQRVGLARAFAVDPEIL 157
Cdd:cd03215 81 pedrKREGLVLDLSVAENIAL----------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 158 LLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAG-KAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-220 |
8.91e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.47 E-value: 8.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAA-----EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEV---FAAGHAVTAPGPDR- 77
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -------------------------GMVFQ--HHALLPwMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHA-A 129
Cdd:PRK13651 83 vleklviqktrfkkikkikeirrrvGVVFQfaEYQLFE-QTIEKDIIFGPVSM--GVSKEEAKKRAAKYIELVGLDESyL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 130 SRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVM 209
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|.
gi 1721987636 210 SHGprsTIIAD 220
Cdd:PRK13651 239 KDG---KIIKD 246
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-212 |
1.33e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 10 RNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEV-FAAGHAV-----TAPGPDR------ 77
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQlrdlyALSEAERrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 --GMVFQHHA--LLPWMTAKGNIefglksARPQLSRAERS-----EIADQFLQQVGLAhaASR---RPARLSGGMQQRVG 145
Cdd:PRK11701 90 ewGFVHQHPRdgLRMQVSAGGNI------GERLMAVGARHygdirATAGDWLERVEID--AARiddLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 146 LARAFAVDPEILLLDEPFGALDA--------LTR---RELQLqlrnvweanrrTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVsvqarlldLLRglvRELGL-----------AVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-212 |
1.86e-25 |
|
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: 99.47 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGH-AVTApgpdrgmvfQhhalLPW---MTAKGNIEFGlk 101
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiAYVS---------Q----EPWiqnGTIRENILFG-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 102 sarpqlsraerSEIADQFLQQVglAHAASRRP-----------------ARLSGGMQQRVGLARAFAVDPEILLLDEPFG 164
Cdd:cd03250 90 -----------KPFDEERYEKV--IKACALEPdleilpdgdlteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 165 ALDALTRREL-QLQLRNVWeANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03250 157 AVDAHVGRHIfENCILGLL-LNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-212 |
2.32e-25 |
|
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: 104.71 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 31 EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVT----APGPDRGMVFQHHALLPWMTAKGNIEF--GLKSAR 104
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQHNILFHHLTVAEHILFyaQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 105 PQLSRAErseiADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRR---ELQLQLRnv 181
Cdd:TIGR01257 1035 WEEAQLE----MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRsiwDLLLKYR-- 1108
|
170 180 190
....*....|....*....|....*....|.
gi 1721987636 182 weaNRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR01257 1109 ---SGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-205 |
3.69e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMI--AGLAFPS---TGEVFAAGHAVTAPGPDR---- 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTvdlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ---GMVFQHHALLPwMTAKGNIEFGLKSA----RPQLSRA-ERSEIADQFLQQV-GLAHAASrrpARLSGGMQQRVGLAR 148
Cdd:PRK14239 86 keiGMVFQQPNPFP-MSIYENVVYGLRLKgikdKQVLDEAvEKSLKGASIWDEVkDRLHDSA---LGLSGGQQQRVCIAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 149 AFAVDPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVDEAILLSDR 205
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-212 |
4.64e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 99.10 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGA--AEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGH--AVTAPGPDR---GM 79
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAWLRrqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLpwmtaKGNIEFGLKSARPQLSRAERSEIAD-----QFLQQV--GLAHAASRRPARLSGGMQQRVGLARAFAV 152
Cdd:cd03252 81 VLQENVLF-----NRSIRDNIALADPGMSMERVIEAAKlagahDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 153 DPEILLLDEPFGALDALTRRELQLQLRNVWEAnrRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRL-STVKNADRIIVMEKG 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-209 |
4.75e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 101.32 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP--------DRGMVFQH--HALLPWMTAKGN 95
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewravrsDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 96 IEFGLKSARPQLSRAERSEIADQFLQQVGL-AHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDAltrrEL 174
Cdd:PRK15079 121 IAEPLRTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV----SI 196
|
170 180 190
....*....|....*....|....*....|....*....
gi 1721987636 175 QLQLRNVWEANRR----TVIMVTHDVDEAILLSDRILVM 209
Cdd:PRK15079 197 QAQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVLVM 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-195 |
5.22e-25 |
|
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: 103.21 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD----RGMVF 81
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevrrRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFGlksaRPQLSRAERSEIadqfLQQVGLAHAASRRP-----------ARLSGGMQQRVGLARAF 150
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRLA----RPDATDEELWAA----LERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721987636 151 AVDPEILLLDEPFGALDALTRRELqlqLRNVWEANR-RTVIMVTHD 195
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADEL---LEDLLAALSgRTVVLITHH 529
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-215 |
6.25e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 6.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD--RG 78
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MV---FQHHALLPwMTAKGNIEF--GLKSARPqlsraERSEIADqFLQQVGLA-HAASRRPARLSGGMQQRVGLARAFAV 152
Cdd:PRK10247 82 QVsycAQTPTLFG-DTVYDNLIFpwQIRNQQP-----DPAIFLD-DLERFALPdTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 153 DPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGPRS 215
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEM 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-212 |
6.27e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.85 E-value: 6.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 20 EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---------GMVFQH-HALLPW 89
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrkriGMVFQFpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 90 MTAKGNIEFGLKSARPQLSRAErsEIADQFLQQVGLA-HAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA 168
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDEVK--NYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1721987636 169 LTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-212 |
1.12e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.01 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 11 NITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGL-----AFPSTGEVFAAGHA------VTAPGPDRGM 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsGYRYSGDVLLGGRSifnyrdVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPwMTAKGNIEFGLKsARPQLSRAERSEIADQFLQQVGLAHAASRR----PARLSGGMQQRVGLARAFAVDPE 155
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVR-AHKLVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 156 ILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDG 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-212 |
1.23e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITksygAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP----DRGMVF-- 81
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdaiRAGIAYvp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 ---QHHALLPWMTAKGNI---EFGLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPAR-LSGGMQQRVGLARAFAVDP 154
Cdd:COG1129 334 edrKGEGLVLDLSIRENItlaSLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 155 EILLLDEPFGALDALTRRELQLQLRNVweANR-RTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIREL--AAEgKAVIVISSELPELLGLSDRILVMREG 470
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-212 |
1.57e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMVFQH-HALLPWMTAKGNIEFG 99
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskvGLVFQDpDDQVFSSTVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 100 LKSARpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELqLQLR 179
Cdd:PRK13647 105 PVNMG--LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL-MEIL 181
|
170 180 190
....*....|....*....|....*....|...
gi 1721987636 180 NVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13647 182 DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-220 |
4.97e-24 |
|
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: 96.25 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY----------GAA-----------EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFA 65
Cdd:cd03267 1 IEVSNLSKSYrvyskepgliGSLkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 66 AGHAvtaPGPDR-------GMVFQHHALLPW-MTAKGNIEF-----GLKSARPQLSRAERSEIAD--QFLQQvglahaas 130
Cdd:cd03267 81 AGLV---PWKRRkkflrriGVVFGQKTQLWWdLPVIDSFYLlaaiyDLPPARFKKRLDELSELLDleELLDT-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 131 rrPAR-LSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVM 209
Cdd:cd03267 150 --PVRqLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
250
....*....|.
gi 1721987636 210 SHGprsTIIAD 220
Cdd:cd03267 228 DKG---RLLYD 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-212 |
8.51e-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: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 4 SSHVELRNITKSY--------GAAEVIAPT--------------SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTG 61
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrSLKELLLRRrrtrreefwalkdvSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 62 EVFAAGHaVTAPgPDRGMVFQhhallPWMTAKGNIEF-----GLKsaRPQLSRAER-----SEIADQFLQQVGlahaasr 131
Cdd:COG1134 82 RVEVNGR-VSAL-LELGAGFH-----PELTGRENIYLngrllGLS--RKEIDEKFDeivefAELGDFIDQPVK------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 132 rpaRLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEaNRRTVIMVTHDVDEAILLSDRILVMSH 211
Cdd:COG1134 146 ---TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
.
gi 1721987636 212 G 212
Cdd:COG1134 222 G 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-212 |
1.99e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.74 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 2 TNSSHVELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG----- 74
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaalr 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 ------PDRGMVFQHhallpwmTAKGNiefgLKSARPQLSRAERSEIadqfLQQVGLAHAASR------------RParL 136
Cdd:PRK11160 414 qaisvvSQRVHLFSA-------TLRDN----LLLAAPNASDEALIEV----LQQVGLEKLLEDdkglnawlgeggRQ--L 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 137 SGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRE-LQLqLRNVweANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQiLEL-LAEH--AQNKTVLMITHRL-TGLEQFDRICVMDNG 549
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-212 |
2.44e-23 |
|
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: 98.34 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-----GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEV-FAAGHA---VTAPGPDR 77
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 --------GMVFQHHALLPWMTAKGNiefglksarpqLSRAERSEIADQF--------LQQVGLAHAASRR-----PARL 136
Cdd:TIGR03269 360 rgrakryiGILHQEYDLYPHRTVLDN-----------LTEAIGLELPDELarmkavitLKMVGFDEEKAEEildkyPDEL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 137 SGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-212 |
3.17e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.20 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAA-----EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---- 77
Cdd:PRK13649 3 INLQNVSYTYQAGtpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -----GMVFQH-HALLPWMTAKGNIEFGlksarPQ---LSRAERSEIADQFLQQVGLAHAA-SRRPARLSGGMQQRVGLA 147
Cdd:PRK13649 83 irkkvGLVFQFpESQLFEETVLKDVAFG-----PQnfgVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-212 |
4.99e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 94.13 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 11 NITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVF-----AAGHAVTA-PGPDR------- 77
Cdd:TIGR02323 8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimrsGAELELYQlSEAERrrlmrte 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -GMVFQHHA--LLPWMTAKGNIefglkSARPqLSRAER-----SEIADQFLQQVGLAHA-ASRRPARLSGGMQQRVGLAR 148
Cdd:TIGR02323 88 wGFVHQNPRdgLRMRVSAGANI-----GERL-MAIGARhygniRATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 149 AFAVDPEILLLDEPFGALD-ALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDvSVQARLLDLLRGLVRDLG-LAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
8-212 |
7.61e-23 |
|
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: 92.88 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSY-----GAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVF--AAGHAVT-APGPDR 77
Cdd:COG4778 6 EVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrHDGGWVDlAQASPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 ----------GMVFQHHALLPWMTAkgnIEFGLKSARPQ-LSRAERSEIADQFLQQVG----LAHAAsrrPARLSGGMQQ 142
Cdd:COG4778 86 eilalrrrtiGYVSQFLRVIPRVSA---LDVVAEPLLERgVDREEARARARELLARLNlperLWDLP---PATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 143 RVGLARAFAVDPEILLLDEPFGALDALTR---RELQLQLRnvweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAK----ARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-212 |
8.98e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 90.59 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfaaghavtapgpdrgmvfqhhal 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 87 lpwmTAKGNIEFGlksarpqlsraerseiadqFLQQvglahaasrrparLSGGMQQRVGLARAFAVDPEILLLDEPFGAL 166
Cdd:cd03221 58 ----TWGSTVKIG-------------------YFEQ-------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 167 DALTRrelqLQLRNVWEANRRTVIMVTHD---VDEailLSDRILVMSHG 212
Cdd:cd03221 102 DLESI----EALEEALKEYPGTVILVSHDryfLDQ---VATKIIELEDG 143
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-212 |
9.64e-23 |
|
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: 92.32 E-value: 9.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYG-AAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGhaVTAPGPDR----GMVFQ 82
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG--KPIKAKERrksiGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 H--HALLPwMTAKGNIEFGLKSArpqlsrAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:cd03226 79 DvdYQLFT-DSVREELLLGLKEL------DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 161 EPFGALDALTRRELQLQLRNVwEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03226 152 EPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
26-212 |
1.26e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.21 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGhAVTAPgPDRGMVFQhhallPWMTAKGNIEF-----GL 100
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL-LGLGGGFN-----PELTGRENIYLngrllGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 101 KSARPQlSRAER----SEIADQFLQQVGlahaasrrpaRLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQL 176
Cdd:cd03220 115 SRKEID-EKIDEiiefSELGDFIDLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1721987636 177 QLRNVWEaNRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:cd03220 184 RLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-212 |
1.28e-22 |
|
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: 96.32 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSV--HIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GM 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSIslVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrrqvAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPwMTAKGNIEFGlksARPQLSRAE-RSEIADQFLQQV------GLAHAASRRPARLSGGMQQRVGLARAFAV 152
Cdd:TIGR02203 411 VSQDVVLFN-DTIANNIAYG---RTEQADRAEiERALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 153 DPEILLLDEPFGALDALTRRELQLQLRNVWEAnrRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQG--RTTLVIAHRL-STIEKADRIVVMDDG 543
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-212 |
1.51e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 93.61 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAE------VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG------ 74
Cdd:PRK13633 5 IKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 PDRGMVFQH-HALLPWMTAKGNIEFGlksarPQLSRAERSEI---ADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAF 150
Cdd:PRK13633 85 NKAGMVFQNpDNQIVATIVEEDVAFG-----PENLGIPPEEIrerVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 151 AVDPEILLLDEPFGALDALTRRELqlqLRNVWEANRR---TVIMVTHDVDEAIlLSDRILVMSHG 212
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREV---VNTIKELNKKygiTIILITHYMEEAV-EADRIIVMDSG 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
7-212 |
1.67e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYG-AAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV--TAPG-----PDRG 78
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGlmklrESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQH--HALLPwMTAKGNIEFGLKSArpQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:PRK13636 86 MVFQDpdNQLFS-ASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 157 LLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-220 |
1.96e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV-----TAPGPDRGMVF 81
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 QHHALLPWMTAKGNIEFGLKSARPQLSRAERSEIA--DQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAavERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 160 DEPFGALDALTR-RELQLQLRNVWEAnrRTVIMVTHDVDEAILLSDRILVMSHG-------PRSTIIAD 220
Cdd:PRK09536 164 DEPTASLDINHQvRTLELVRRLVDDG--KTAVAAIHDLDLAARYCDELVLLADGrvraagpPADVLTAD 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-212 |
2.31e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMV 80
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfvGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQH---HALLPwmTAKGNIEFGlkSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEIL 157
Cdd:PRK13652 84 FQNpddQIFSP--TVEQDIAFG--PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 158 LLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-168 |
2.32e-22 |
|
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: 90.88 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAG--HAVTAPGPDRGMVFQHH- 84
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtpLAEQRDEPHENILYLGHl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 -ALLPWMTAKGNIEFglksARPQLSRAERSeiADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:TIGR01189 82 pGLKPELSALENLHF----WAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....*
gi 1721987636 164 GALDA 168
Cdd:TIGR01189 156 TALDK 160
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-225 |
2.70e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.41 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAfPSTGEVFAAGHA-------------VTAP 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGRVeffnqniyerrvnLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 74 GPDRGMVFQHHALLPwMTAKGNIEFGLK--SARPQLsraERSEIADQFLQQVGL----AHAASRRPARLSGGMQQRVGLA 147
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKivGWRPKL---EIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDrILVMSHGPRSTIIADIEVAT 225
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD-FTAFFKGNENRIGQLVEFGL 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-212 |
4.03e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 91.13 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAE-VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGhavtAPGPDR-------- 77
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG----IDIRDIsrkslrsm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 -GMVFQHHALLPwMTAKGNIEFGLKSARPQLSRAERSEI-ADQFLQQV--GLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:cd03254 79 iGVVLQDTFLFS-GTIMENIRLGRPNATDEEVIEAAKEAgAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 154 PEILLLDEPFGALDALTRRELQLQLRNVWEAnrRTVIMVTHDVDeAILLSDRILVMSHG 212
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLS-TIKNADKILVLDDG 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-212 |
4.96e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.44 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 23 APTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAfPSTGEVFAAGHAVTA-PGPD----RGMVFQHHALLPWMTAKGNIE 97
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAElarhRAYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 98 FGLksaRPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFA-VDPEI------LLLDEPFGALD--- 167
Cdd:COG4138 92 LHQ---PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLDvaq 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 168 --ALTR--RELQLQlrnvweanRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG4138 169 qaALDRllRELCQQ--------GITVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-212 |
9.18e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.76 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 24 PTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAfPSTGEVFAAGHAVTAPGPD--RgmvfQHHA------LLPWMTAKGN 95
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswR----KHLSwvgqnpQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 96 IEFGLKSARPQ-----LSRAERSEIADQFLQqvGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALT 170
Cdd:PRK11174 443 VLLGNPDASDEqlqqaLENAWVSEFLPLLPQ--GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721987636 171 RRELQLQLRNVWeaNRRTVIMVTHDVDEaILLSDRILVMSHG 212
Cdd:PRK11174 521 EQLVMQALNAAS--RRQTTLMVTHQLED-LAQWDQIWVMQDG 559
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-212 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.33 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 18 AAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR---------GMVFQH-HALL 87
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrkkvGVVFQFpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 88 PWMTAKGNIEFGlksarPQ---LSRAERSEIADQFLQQVGLAHAA-SRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:PRK13643 98 FEETVLKDVAFG-----PQnfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721987636 164 GALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSG-QTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
7-212 |
1.60e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.62 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY---------GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTApgPDR 77
Cdd:PRK15112 5 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF--GDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 G-------MVFQ--HHALLPWMTAKGNIEFGLKsARPQLSRAERSEIADQFLQQVGL-AHAASRRPARLSGGMQQRVGLA 147
Cdd:PRK15112 83 SyrsqrirMIFQdpSTSLNPRQRISQILDFPLR-LNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-212 |
2.18e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfAAGHAVTApgpdrGMVFQHHAL 86
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVKI-----GYFDQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 87 L-PWMTAkgnIEFgLKSARPQLSRAERSeiadQFLQQVGLAHAASRRPAR-LSGGMQQRVGLARAFAVDPEILLLDEPFG 164
Cdd:COG0488 390 LdPDKTV---LDE-LRDGAPGGTEQEVR----GYLGRFLFSGDDAFKPVGvLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 165 ALDALTRRELQLQLRNvWEAnrrTVIMVTHD---VDEailLSDRILVMSHG 212
Cdd:COG0488 462 HLDIETLEALEEALDD-FPG---TVLLVSHDryfLDR---VATRILEFEDG 505
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-223 |
6.40e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 11 NITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA-PGPDR-----GMVFQHH 84
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlPLHARarrgiGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 ALLPWMTAKGNIeFGLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFG 164
Cdd:PRK10895 88 SIFRRLSVYDNL-MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 165 ALDALTrrelQLQLRNVWEANRRT---VIMVTHDVDEAILLSDRILVMS------HGPRSTIIADIEV 223
Cdd:PRK10895 167 GVDPIS----VIDIKRIIEHLRDSglgVLITDHNVRETLAVCERAYIVSqghliaHGTPTEILQDEHV 230
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-212 |
7.55e-21 |
|
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: 91.34 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 5 SHVELRNITKSYG-AAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTapGPDRGMVFQH 83
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK--DIDRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HALLP---WMTAKGNIEFGLKSARPQLSR------AERSEIADQFLQ-QVGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:TIGR01193 550 INYLPqepYIFSGSILENLLLGAKENVSQdeiwaaCEIAEIKDDIENmPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 154 PEILLLDEPFGALDALTRRELqlqLRNVWEANRRTVIMVTHDVDEAiLLSDRILVMSHG 212
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSVA-KQSDKIIVLDHG 684
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-214 |
3.06e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 2 TNSSHVELRNIT-KSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLaFPstgevFAAGHaVTAPGPDRGMV 80
Cdd:COG4178 358 SEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL-WP-----YGSGR-IARPAGARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTakgniefgLKSA--RPQLSRAERSEIADQFLQQVGLAHAASR------RPARLSGGMQQRVGLARAFAV 152
Cdd:COG4178 431 LPQRPYLPLGT--------LREAllYPATAEAFSDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 153 DPEILLLDEPFGALDALTRRELQLQLRNvwEANRRTVIMVTHDvDEAILLSDRILVMSHGPR 214
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGDGS 561
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
37-212 |
3.87e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 37 ILGPSGCGKSTILSMIAGLAFPSTGEV----------FAAGHAVTAPGPDR-----------GMVFQ--HHALLPwMTAK 93
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkKNNHELITNPYSKKiknfkelrrrvSMVFQfpEYQLFK-DTIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 94 GNIEFG---LKsarpqLSRAERSEIADQFLQQVGLAHA-ASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDAL 169
Cdd:PRK13631 136 KDIMFGpvaLG-----VKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1721987636 170 TRRELqLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13631 211 GEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-168 |
6.76e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.47 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRgmvfqHHALL---------PWMTAKGNI 96
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-----HQDLLylghqpgikTELTALENL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 97 EFGLKSARPQlsraeRSEIADQFLQQVGLAhaasRR---PAR-LSGGMQQRVGLARAFAVDPEILLLDEPFGALDA 168
Cdd:PRK13538 96 RFYQRLHGPG-----DDEALWEALAQVGLA----GFedvPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-220 |
8.03e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.94 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY--------GAAEVIAPTSV--HIDEGQFVSILGPSGCGKSTI---LSMIAGlafPSTGEVFAAGHAVTap 73
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkPERLVKALDGVsfTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 74 GPDRG----------MVFQ--HHALLPWMTAKGNIEFGLKsARPQLSRAERSEIADQFLQQVGL-AHAASRRPARLSGGM 140
Cdd:PRK11308 81 KADPEaqkllrqkiqIVFQnpYGSLNPRKKVGQILEEPLL-INTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 141 QQRVGLARAFAVDPEILLLDEPFGALDALTRRE-------LQLQLRNVWeanrrtvIMVTHD--VDEAIllSDRILVM-- 209
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnlmmdLQQELGLSY-------VFISHDlsVVEHI--ADEVMVMyl 230
|
250
....*....|....*
gi 1721987636 210 ----SHGPRSTIIAD 220
Cdd:PRK11308 231 grcvEKGTKEQIFNN 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-205 |
1.25e-19 |
|
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: 87.68 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 37 ILGPSGCGKSTILSMIAGLAFPSTGEvfaaghAVTAPGPDRGMVFQHHALLPWMTAKGNIEFGLKSARPQLSRAErsEIA 116
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGE------ARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFN--EIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 117 DQF----------------LQ-------------QVGLAHAASRRP------ARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:TIGR03719 108 AKYaepdadfdklaaeqaeLQeiidaadawdldsQLEIAMDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 162 PFGALDALTRRELQLQLRNVweanRRTVIMVTHD------VDEAILLSDR 205
Cdd:TIGR03719 188 PTNHLDAESVAWLERHLQEY----PGTVVAVTHDryfldnVAGWILELDR 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-221 |
1.41e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 11 NITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMVFQHHA 85
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarriGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 LLPWMTAKGNIEFGLKSARPQLS--RAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:PRK10253 92 TPGDITVQELVARGRYPHQPLFTrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 164 GALDALTRRELqlqLRNVWEANRR---TVIMVTHDVDEA-------ILLSDRILVMSHGPRSTIIADI 221
Cdd:PRK10253 172 TWLDISHQIDL---LELLSELNREkgyTLAAVLHDLNQAcryashlIALREGKIVAQGAPKEIVTAEL 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-212 |
1.66e-19 |
|
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: 87.05 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGAAEVIAPT----SVHIDEGQFVSILGPSGCGKS-TILSMI----AGLAFPStGEVFAAGHAVT 71
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAvkgvSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 72 APGPDR---------GMVFQH--HALLPWMTAKGNIEFGLKSARPqLSRAERSEIADQFLQQVGLAHAASR---RPARLS 137
Cdd:COG4172 80 GLSERElrrirgnriAMIFQEpmTSLNPLHTIGKQIAEVLRLHRG-LSGAAARARALELLERVGIPDPERRldaYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 138 GGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRE-LQLqLRNVWEANRRTVIMVTHD---VDEailLSDRILVMSHG 212
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQiLDL-LKDLQRELGMALLLITHDlgvVRR---FADRVAVMRQG 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-212 |
1.88e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.71 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 11 NITKSY---GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGL------AFPSTGEVFAAGHAV-----TAPGPD 76
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIfqidaIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 77 RGMVFQHHALLPWMTAKGNIEFGLKSARPQLSRaERSEIADQFLQQVGL---AHAASRRPA-RLSGGMQQRVGLARAFAV 152
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKR-EIKKIVEECLRKVGLwkeVYDRLNSPAsQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 153 DPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-212 |
2.41e-19 |
|
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: 83.57 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGL----AFPSTGEVFAAGHAVTAP---GPDRGMVFQH--HALLPWMTAKGNI 96
Cdd:TIGR02770 6 NLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLsirGRHIATIMQNprTAFNPLFTMGNHA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 97 EFGLKSaRPQLSRAERSEIADQfLQQVGLAHAA---SRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRE 173
Cdd:TIGR02770 86 IETLRS-LGKLSKQARALILEA-LEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1721987636 174 LQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDG 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-212 |
3.00e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGAA-----EVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAP-- 73
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 74 --------GPDRGMVFQH-HALLPWMTAKGNIEFGlksarPQLSRAERSEI---ADQFLQQVGLAHA-ASRRPARLSGGM 140
Cdd:PRK13645 81 kikevkrlRKEIGLVFQFpEYQLFQETIEKDIAFG-----PVNLGENKQEAykkVPELLKLVQLPEDyVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 141 QQRVGLARAFAVDPEILLLDEPFGALDALTRRE-LQLQLRNVWEANRRtVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDfINLFERLNKEYKKR-IIMVTHNMDQVLRIADEVIVMHEG 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-212 |
4.65e-19 |
|
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: 82.90 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSY---GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTApgpdrgmvFQ 82
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--------YE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKG------------NIEFGLKSAR-PQLSRAERSEIADQFLQ--QVGLAHAASRRPARLSGGMQQRVGLA 147
Cdd:cd03248 83 HKYLHSKVSLVGqepvlfarslqdNIAYGLQSCSfECVKEAAQKAHAHSFISelASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEanRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRL-STVERADQILVLDGG 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-212 |
6.73e-19 |
|
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: 81.83 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPS--TGEVFAAGHAVTAPGPDR--GMVFQHHALLPWMTAKGNIEFglk 101
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKiiGYVPQDDILHPTLTVRETLMF--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 102 SARpqlsraerseiadqfLQQvglahaasrrparLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNV 181
Cdd:cd03213 106 AAK---------------LRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
170 180 190
....*....|....*....|....*....|..
gi 1721987636 182 WEANrRTVIMVTHDV-DEAILLSDRILVMSHG 212
Cdd:cd03213 158 ADTG-RTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-212 |
7.15e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNIT-KSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP----DRGMVF- 81
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrerrRLGVAYi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 ----QHHALLPWMTAKGNIEFGL-----KSARPQLSRAERSEIADQFLQQVGLAHAASRRPAR-LSGGMQQRVGLARAFA 151
Cdd:COG3845 339 pedrLGRGLVPDMSVAENLILGRyrrppFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARsLSGGNQQKVILARELS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 152 VDPEILLLDEPFGALD----ALTRRELqLQLRNvweaNRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:COG3845 419 RDPKLLIAAQPTRGLDvgaiEFIHQRL-LELRD----AGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-212 |
7.66e-19 |
|
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: 85.18 E-value: 7.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSYGAAE--VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----G 78
Cdd:COG4618 330 RLSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgrhiG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPwMTAKGNIefglksAR-PQLSRAERSEIAdqflQQVGlAHAA-SRRP-----------ARLSGGMQQRVG 145
Cdd:COG4618 410 YLPQDVELFD-GTIAENI------ARfGDADPEKVVAAA----KLAG-VHEMiLRLPdgydtrigeggARLSGGQRQRIG 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 146 LARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVwEANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDG 542
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-212 |
1.17e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.71 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPST---GEVFAAGHAVTAPGPDR--GMVFQHHALLPWMTAKGNIEFG- 99
Cdd:TIGR00955 45 SGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREHLMFQa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 100 -LKSARpQLSRAERSEIADQFLQQVGLAHAASRR---PAR---LSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRR 172
Cdd:TIGR00955 125 hLRMPR-RVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721987636 173 ELQLQLRNVweANR-RTVIMVTHDVDEAIL-LSDRILVMSHG 212
Cdd:TIGR00955 204 SVVQVLKGL--AQKgKTIICTIHQPSSELFeLFDKIILMAEG 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-212 |
1.38e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.63 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 4 SSHVELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAG---HAVTAPGPDR-- 77
Cdd:PRK13657 332 KGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRni 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQHhALLPWMTAKGNIEFGLKSARPQLSR--AERSEIADQFLQQV-GLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNIRVGRPDATDEEMRaaAERAQAHDFIERKPdGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 155 EILLLDEPFGALDALTRRELQLQLRNVWEAnrRTVIMVTH---DVDEAillsDRILVMSHG 212
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKG--RTTFIIAHrlsTVRNA----DRILVFDNG 545
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-212 |
1.86e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY-GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGhaVTAPGPDR-------- 77
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKlqgirklv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQH-HALLPWMTAKGNIEFGlksarPQ---LSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVD 153
Cdd:PRK13644 80 GIVFQNpETQFVGRTVEEDLAFG-----PEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 154 PEILLLDEPFGALDALTRRELqlqLRNVWEANR--RTVIMVTHDVDEaILLSDRILVMSHG 212
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAV---LERIKKLHEkgKTIVYITHNLEE-LHDADRIIVMDRG 211
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-212 |
3.22e-18 |
|
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: 83.72 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSYGAA-EVIAPTSVHIDEGQFVSILGPSGCGKSTilsmIAGLAF----PSTGEVFAAGHAVTAPGPD--R- 77
Cdd:COG5265 357 EVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKST----LARLLFrfydVTSGRILIDGQDIRDVTQAslRa 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 --GMVFQHHALLPwMTAKGNIEFGlksaRPQLSRAERSEIA-----DQFLQ--------QVGlahaasRRPARLSGGMQQ 142
Cdd:COG5265 433 aiGIVPQDTVLFN-DTIAYNIAYG----RPDASEEEVEAAAraaqiHDFIEslpdgydtRVG------ERGLKLSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 143 RVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDvdeailLS-----DRILVMSHG 212
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHR------LStivdaDEILVLEAG 568
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-212 |
3.61e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRG------MV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgiyLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIEFGLksARPQLSRAERSEIADQFLQQVGLAHAAsrrpARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL--PKRQASMQKMKQLLAALGCQLDLDSSA----GSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721987636 161 EPFGAL-----DALTRRELQLQLRNVweanrrTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK15439 166 EPTASLtpaetERLFSRIRELLAQGV------GIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-212 |
7.28e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.45 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 32 GQFVSILGPSGCGKSTilsmiAGLAF----PSTGEVFAAGHAVTAPGPdRGM---------VFQ--HHALLPWMTAKGNI 96
Cdd:PRK15134 312 GETLGLVGESGSGKST-----TGLALlrliNSQGEIWFDGQPLHNLNR-RQLlpvrhriqvVFQdpNSSLNPRLNVLQII 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 97 EFGLKSARPQLSRAERSEIADQFLQQVGLAHAASRR-PARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQ 175
Cdd:PRK15134 386 EEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
|
170 180 190
....*....|....*....|....*....|....*..
gi 1721987636 176 LQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK15134 466 ALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-220 |
7.71e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.29 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAvtaPGPDR-------GMVF-QHHALLPWMTAkgnIE 97
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PFKRRkefarriGVVFgQRSQLWWDLPA---ID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 98 -FGLKSARPQLSRAERSEIADQFLQQVGLAHAAsRRPAR-LSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQ 175
Cdd:COG4586 116 sFRLLKAIYRIPDAEYKKRLDELVELLDLGELL-DTPVRqLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIR 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1721987636 176 LQLRnvwEANRR---TVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:COG4586 195 EFLK---EYNRErgtTILLTSHDMDDIEALCDRVIVIDHG---RIIYD 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-194 |
9.17e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 9.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMVFQHH- 84
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 -ALLPWMTAKGNIEFGlksarPQLSRAERSEIADQfLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:PRK13539 82 nAMKPALTVAENLEFW-----AAFLGGEELDIAAA-LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|....
gi 1721987636 164 GALDALTrrelQLQLRNVWEANRR---TVIMVTH 194
Cdd:PRK13539 156 AALDAAA----VALFAELIRAHLAqggIVIAATH 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-205 |
2.85e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.55 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 37 ILGPSGCGKSTILSMIAGLAFPSTGEVFAAghavtaPGPDRGMVFQHHALLPWMTAKGNIEFGLKSARPQLSRAErsEIA 116
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPA------PGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFN--EIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 117 DQF----------------LQ-------------QVGLAHAASRRP------ARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:PRK11819 110 AAYaepdadfdalaaeqgeLQeiidaadawdldsQLEIAMDALRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 162 PFGALDALTRRELQLQLRNVweanRRTVIMVTHD------VDEAILLSDR 205
Cdd:PRK11819 190 PTNHLDAESVAWLEQFLHDY----PGTVVAVTHDryfldnVAGWILELDR 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-212 |
2.91e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.79 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLA-FPstGEVFAA-----GHAVTA---------PGPDRGMVFQH--HALLP 88
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYP--GRVMAEklefnGQDLQRisekerrnlVGAEVAMIFQDpmTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 89 WMTAKGNIEFGLKSARPQlSRAERSEIADQFLQQVGLAHAASR---RPARLSGGMQQRVGLARAFAVDPEILLLDEPFGA 165
Cdd:PRK11022 105 CYTVGFQIMEAIKVHQGG-NKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721987636 166 LDALTRRELQLQLRNVWEANRRTVIMVTHD---VDEAillSDRILVMSHG 212
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITHDlalVAEA---AHKIIVMYAG 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-212 |
4.92e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.67 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 23 APTSVHIDEGQFVSILGPSGCGKSTILSMIAGLaFPSTGEVFAAGHAV-TAPGPD----RG-----------M-VFQHHA 85
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeAWSAAElarhRAylsqqqtppfaMpVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 L-LPwmtakgniefglKSARPQLSRAERSEIAdqflQQVGLAHAASRRPARLSGGMQQRVGLARAF-AVDPEI------L 157
Cdd:PRK03695 92 LhQP------------DKTRTEAVASALNEVA----EALGLDDKLGRSVNQLSGGEWQRVRLAAVVlQVWPDInpagqlL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 158 LLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQG-IAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-199 |
5.04e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.17 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGpDRGMVFQHHA- 85
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR-HRRAVCPRIAy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 --------LLPWMTAKGNIEF-----GLksarpqlSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAV 152
Cdd:NF033858 81 mpqglgknLYPTLSVFENLDFfgrlfGQ-------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 153 DPEILLLDEPFGALDALTRR---ELQLQLRnvweANRR--TVIMVTHDVDEA 199
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRqfwELIDRIR----AERPgmSVLVATAYMEEA 201
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-212 |
1.08e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.15 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 11 NITKSYGAAEVIAPTSVHIDE-------------GQFVSILGPSGCGKSTILSMIAGLAFPS--TGEVFAAGHAVTAPGP 75
Cdd:PLN03211 60 NIKRILGHKPKISDETRQIQErtilngvtgmaspGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 76 DR-GMVFQHHALLPWMTAKGNIEF-GLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPAR-----LSGGMQQRVGLAR 148
Cdd:PLN03211 140 KRtGFVTQDDILYPHLTVRETLVFcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAH 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 149 AFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-212 |
1.24e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP----DRGMVF-----QHHAL-----LPWMT 91
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLyldapLAWNV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 92 ---AKGNIEFGLKSARpqlsraeRSEIADQFLQQVGLAHAASRRPAR-LSGGMQQRVGLARAFAVDPEILLLDEPFGALD 167
Cdd:PRK15439 363 calTHNRRGFWIKPAR-------ENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1721987636 168 ALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-212 |
1.35e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 78.71 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLaFPS---TGEVFAAGHAVTAPG----PDRGM 79
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNirdtERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHH--ALLPWMTAKGNIEFGLKSARP--QLSRAERSEIADQFLQQVGLAHAASRRP-ARLSGGMQQRVGLARAFAVDP 154
Cdd:TIGR02633 81 VIIHQelTLVPELSVAENIFLGNEITLPggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 155 EILLLDEPFGaldALTRRELQLQLRNVWEANRRTV--IMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR02633 161 RLLILDEPSS---SLTEKETEILLDIIRDLKAHGVacVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-212 |
2.12e-16 |
|
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: 75.45 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP------DRGMVfQHHALLPWM---TAKGNI 96
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFeatrsrNRYSV-AYAAQKPWLlnaTVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 97 EFG--LKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA-LTRRE 173
Cdd:cd03290 100 TFGspFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1721987636 174 LQLQLRNVWEANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03290 180 MQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-211 |
3.92e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 4 SSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfaaghaVTAPGPDRGMVFQH 83
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HAL---LP-----WMTAKGniefGLKSAR--PQLSRAERSEIADQFLQqvglahaasrrpaRLSGGMQQRVGLARAFAVD 153
Cdd:PRK09544 76 LYLdttLPltvnrFLRLRP----GTKKEDilPALKRVQAGHLIDAPMQ-------------KLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 154 PEILLLDEPFGALDA---LTRRELQLQLRNvwEANrRTVIMVTHDVDEAILLSDRILVMSH 211
Cdd:PRK09544 139 PQLLVLDEPTQGVDVngqVALYDLIDQLRR--ELD-CAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-212 |
4.64e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGM------V 80
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMreavaiV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIEFGLKSARPQLSRAERSEIADQFLQqvgLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 161 EPFGALDALtrreLQLQLRNVWEANRR---TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11614 163 EPSLGLAPI----IIQQIFDTIEQLREqgmTIFLVEQNANQALKLADRGYVLENG 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-212 |
5.23e-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: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGA---AEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTApgpdrgmvFQH 83
Cdd:TIGR00958 479 IEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ--------YDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 84 HAL------------LPWMTAKGNIEFGLKSA-RPQLSRAERSEIADQFLQQV--GLAHAASRRPARLSGGMQQRVGLAR 148
Cdd:TIGR00958 551 HYLhrqvalvgqepvLFSGSVRENIAYGLTDTpDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 149 AFAVDPEILLLDEPFGALDALTRRELQlQLRnvwEANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQ-ESR---SRASRTVLLIAHRL-STVERADQILVLKKG 689
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-213 |
5.78e-16 |
|
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: 74.75 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 29 IDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVT-AP---GPDRGMVFQhhALLPWMTAKgniefglKSAR 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPqyiKADYEGTVR--DLLSSITKD-------FYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 105 PQLsraeRSEIADQfLQQVGLAhaaSRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEA 184
Cdd:cd03237 93 PYF----KTEIAKP-LQIEQIL---DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180
....*....|....*....|....*....
gi 1721987636 185 NRRTVIMVTHDVDEAILLSDRILVMSHGP 213
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIVFEGEP 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-194 |
6.63e-16 |
|
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: 73.68 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD--RGMVFQHHA 85
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 --LLPWMTAKGNIEFglksarpqLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPF 163
Cdd:cd03231 82 pgIKTTLSVLENLRF--------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|.
gi 1721987636 164 GALDALTRRELQLQLRNVWEANrRTVIMVTH 194
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARG-GMVVLTTH 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-230 |
6.97e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.67 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD----RGMVFQHHALLPWMTAKGNIEFGlk 101
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswrsRLAVVSQTPFLFSDTVANNIALG-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 102 saRPQLSRAERSEIA------DQFLQ-------QVGlahaasRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA 168
Cdd:PRK10789 413 --RPDATQQEIEHVArlasvhDDILRlpqgydtEVG------ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 169 LTRRELQLQLRNvWEANrRTVIMVTHDVdEAILLSDRILVMSHGprstiiadiEVATRSNHN 230
Cdd:PRK10789 485 RTEHQILHNLRQ-WGEG-RTVIISAHRL-SALTEASEILVMQHG---------HIAQRGNHD 534
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-212 |
7.08e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLaFPS---TGEVFAAGHAVTAPG----PDRGMV 80
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNirdtERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHH--ALLPWMTAKGNI-------EFGLKSARPQLSRAERseiadqFLQQVGLAHAASRRPARLSGGMQQRVGLARAFA 151
Cdd:PRK13549 86 IIHQelALVKELSVLENIflgneitPGGIMDYDAMYLRAQK------LLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 152 VDPEILLLDEPFGaldALTRRELQLQLRNVWEANRRTV--IMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13549 160 KQARLLILDEPTA---SLTESETAVLLDIIRDLKAHGIacIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-230 |
8.72e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.21 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSYGAAEVIA--PTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV-----TAPGPDRG 78
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPAlrNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPwMTAKGNIEFGLKS--ARPQLSRAERSEIADQFLQQV--GLAHAASRRPARLSGGMQQRVGLARAFAVDP 154
Cdd:PRK11176 421 LVSQNVHLFN-DTIANNIAYARTEqySREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 155 EILLLDEPFGALDALTRRELQLQLRNVweANRRTVIMVTHDVdEAILLSDRILVMSHGprstiiadiEVATRSNHN 230
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRL-STIEKADEILVVEDG---------EIVERGTHA 563
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-219 |
2.01e-15 |
|
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: 75.22 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGL-AFPstgevfaaghavtapgPDRGMVFQHHA 85
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdQYE----------------PTSGRIIYHVA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 LLPwmtAKGNIEFGLKSARP----------------QLSRAERSEI---------------------------------- 115
Cdd:TIGR03269 65 LCE---KCGYVERPSKVGEPcpvcggtlepeevdfwNLSDKLRRRIrkriaimlqrtfalygddtvldnvlealeeigye 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 116 -------ADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRT 188
Cdd:TIGR03269 142 gkeavgrAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS 221
|
250 260 270
....*....|....*....|....*....|....*...
gi 1721987636 189 VIMVTH------DV-DEAILLSDRILVMSHGPrSTIIA 219
Cdd:TIGR03269 222 MVLTSHwpevieDLsDKAIWLENGEIKEEGTP-DEVVA 258
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-212 |
2.26e-15 |
|
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: 75.33 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 21 VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGpdrgmvfqhhalLPWM---TAKGNIE 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWImpgTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 98 FGLKSARPQLsraeRSEI-ADQFLQQVGLAHAASRRP-----ARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTR 171
Cdd:TIGR01271 509 FGLSYDEYRY----TSVIkACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721987636 172 RELQLQLRNVWEANrRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:TIGR01271 585 KEIFESCLCKLMSN-KTRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-212 |
2.98e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGlAFPST-GEVFAAGHAVTAPGP----DRGMVF-----QHHALLPWMTAKGN 95
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYG-ALPRTsGYVTLDGHEVVTRSPqdglANGIVYisedrKRDGLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 96 IEFG----LKSARPQLSRAERSEIADQFL-----------QQVGLahaasrrparLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:PRK10762 351 MSLTalryFSRAGGSLKHADEQQAVSDFIrlfniktpsmeQAIGL----------LSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 161 EPFGALDALTRRELqLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10762 421 EPTRGVDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-212 |
9.24e-15 |
|
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: 72.20 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 18 AAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPgpdrgmvfQHHALLPWmTAKGNIE 97
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS--------QFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 98 FGL-----------KSARPQLSRAERSEIADQFLQQVGLAhaasrrparLSGGMQQRVGLARAFAVDPEILLLDEPFGAL 166
Cdd:cd03291 120 FGVsydeyryksvvKACQLEEDITKFPEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721987636 167 DALTRRELQLQLRNVWEANrRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03291 191 DVFTEKEIFESCVCKLMAN-KTRILVTSKM-EHLKKADKILILHEG 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-226 |
1.00e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 4 SSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV----TAPGPDRG- 78
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAAGv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 -MVFQHHALLPWMTAKGNIEFG-LKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEI 156
Cdd:PRK11288 82 aIIYQELHLVPEMTVAENLYLGqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 157 LLLDEPFGALDAltrRELQLQLRNVWE--ANRRTVIMVTHDVDEAILLSDRILVMSHGPRSTIIADIEVATR 226
Cdd:PRK11288 162 IAFDEPTSSLSA---REIEQLFRVIRElrAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDR 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-223 |
1.05e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.46 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTilsmiagLAFPSTgevfaaghavtAPGPDRGMvfQHHAL 86
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-------GALPAH-----------V*GPDAGR--RPWRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 87 LPWMTAKGNIEFGLKSARP----------------------QLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRV 144
Cdd:NF000106 74 *TWCANRRALRRTIG*HRPvr*grresfsgrenlymigr*lDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 145 GLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEaNRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIADIEV 223
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRG---RVIADGKV 228
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-167 |
1.11e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.65 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 12 ITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMVFQHH--ALLPW 89
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 90 MTAKGNIEF--GLKSARPQlsraersEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALD 167
Cdd:PRK13543 97 LSTLENLHFlcGLHGRRAK-------QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
37-212 |
1.13e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 37 ILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPgpDRGM---------VFQH-HALLPWMTAKGNIEFGLKSArpQ 106
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS--KRGLlalrqqvatVFQDpEQQIFYTDIDSDIAFSLRNL--G 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 107 LSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANR 186
Cdd:PRK13638 108 VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN 187
|
170 180
....*....|....*....|....*.
gi 1721987636 187 RTVIMvTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13638 188 HVIIS-SHDIDLIYEISDAVYVLRQG 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-214 |
1.19e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKsygaaEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAfpstgevfaaghaVTAPGPDRGMVFQhhal 86
Cdd:COG2401 36 VELRVVER-----YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-------------KGTPVAGCVDVPD---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 87 LPWMTAKGNIEfglksarpQLSRAERSEIADQFLQQVGLAHAAS--RRPARLSGGMQQRVGLARAFAVDPEILLLDEpFG 164
Cdd:COG2401 94 NQFGREASLID--------AIGRKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDE-FC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 165 A-LDALTRRELQLQLRNVWEANRRTVIMVTHDVD-EAILLSDRILVMSHGPR 214
Cdd:COG2401 165 ShLDRQTAKRVARNLQKLARRAGITLVVATHHYDvIDDLQPDLLIFVGYGGV 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-212 |
2.16e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 23 APTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP----DRGMVF-----QHHALLPWMTAK 93
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrdaiRAGIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 94 GNIEFglkSARPQLSRA--------ERsEIADQFLQQVGLAHAASRRPAR-LSGGMQQRVGLARAFAVDPEILLLDEPFG 164
Cdd:PRK11288 350 DNINI---SARRHHLRAgclinnrwEA-ENADRFIRSLNIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1721987636 165 ALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQG-VAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-223 |
3.65e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR------GMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaaqlgiGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIEFGLKSAR-----PQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPE 155
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 156 ILLLDEPfgaLDALTRRELQL------QLRNVWEAnrrtVIMVTHDVDEAILLSDRILVMSHGPR--STIIADIEV 223
Cdd:PRK09700 166 VIIMDEP---TSSLTNKEVDYlflimnQLRKEGTA----IVYISHKLAEIRRICDRYTVMKDGSSvcSGMVSDVSN 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-212 |
7.16e-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: 70.62 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGlAFPST--GEVFAAGHAVTAPGPDRG------MV---FQHHALLPWMTAKG 94
Cdd:TIGR02633 280 SFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKPVDIRNPAQAiragiaMVpedRKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 95 NIEFG-LKS--ARPQLSRAERSEIADQFLQQVGLAHAASRRP-ARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALT 170
Cdd:TIGR02633 359 NITLSvLKSfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721987636 171 RRELqLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR02633 439 KYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-225 |
7.80e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNIT-KSYGAAEVIaptSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGP----DRGMVF- 81
Cdd:PRK09700 267 EVRNVTsRDRKKVRDI---SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavKKGMAYi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 ----QHHALLPWMTAKGNIEF-------GLKSARPQLSRAERSEIADQflQQVGLA---HAASRRPARLSGGMQQRVGLA 147
Cdd:PRK09700 344 tesrRDNGFFPNFSIAQNMAIsrslkdgGYKGAMGLFHEVDEQRTAEN--QRELLAlkcHSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHGPRSTIIADIEVAT 225
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMS 498
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-226 |
7.90e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGA-AEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GMV 80
Cdd:PRK10522 323 LELRNVTFAYQDnGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklfSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNiefglKSARPQLsraerseiADQFLQQVGLAHAASRRPAR-----LSGGMQQRVGLARAFAVDPE 155
Cdd:PRK10522 403 FTDFHLFDQLLGPEG-----KPANPAL--------VEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 156 ILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDvDEAILLSDRILVMSHGPRSTIIADI-EVATR 226
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSELTGEErDAASR 540
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-194 |
8.99e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 67.18 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 21 VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLafpstgevfaaghavtapgpdrgmvfqhhallpWMTAKGNIEfgl 100
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL---------------------------------WPWGSGRIG--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 101 ksarpqlsRAERSEIAdqFLQQ-----VGLAHAASRRP--ARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDAltrrE 173
Cdd:cd03223 60 --------MPEGEDLL--FLPQrpylpLGTLREQLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----E 125
|
170 180
....*....|....*....|.
gi 1721987636 174 LQLQLRNVWEANRRTVIMVTH 194
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGH 146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
31-212 |
9.62e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 31 EGQFVSILGPSGCGKSTILSMIAGlAFP--STGEVFAAGHAVTAPGP----DRGMVF-----QHHALLPWMTAKGNIEFG 99
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKIRNPqqaiAQGIAMvpedrKRDGIVPVMGVGKNITLA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 100 -LK--SARPQLSRAERSEIADQFLQQVGLAHAASRRP-ARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRREL- 174
Cdd:PRK13549 366 aLDrfTGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIy 445
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721987636 175 ----QLQLRNVweanrrTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK13549 446 klinQLVQQGV------AIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-208 |
1.00e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEV-IAPTSVHidEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfaaghavtapgpdrgmvfqhha 85
Cdd:COG1245 342 VEYPDLTKSYGGFSLeVEGGEIR--EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---------------------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 llpwmtakgniEFGLK-SARPQLSRAERSEIADQFLQQV------------------GLAHAASRRPARLSGGMQQRVGL 146
Cdd:COG1245 398 -----------DEDLKiSYKPQYISPDYDGTVEEFLRSAntddfgssyykteiikplGLEKLLDKNVKDLSGGELQRVAI 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 147 ARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDV---DeaiLLSDRILV 208
Cdd:COG1245 467 AACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIyliD---YISDRLMV 528
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-212 |
1.02e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEV-------------------FAAGHAVTAPGPDRGMVFQH--H 84
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvielseQSAAQMRHVRGADMAMIFQEpmT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 ALLPWMTAKGNIEFGLKsARPQLSRAERSEIADQFLQQVGLAHAA---SRRPARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:PRK10261 116 SLNPVFTVGEQIAESIR-LHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 162 PFGALDALTRRELqLQLRNVWEANRRT-VIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10261 195 PTTALDVTIQAQI-LQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-212 |
1.68e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 20 EVIAPTSVHIDEGQFVSILGPSGCGKS-TILSMIAGLAFPS----TGEVFAAGHAVT-APGPD----RG----MVFQHH- 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLhASEQTlrgvRGnkiaMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 -ALLPWMTAKGNIEFGLKSARPQLSRAERSEIAdQFLQQVGLAHAASRR---PARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:PRK15134 103 vSLNPLHTLEKQLYEVLSLHRGMRREAARGEIL-NCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 161 EPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-209 |
2.26e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.43 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 31 EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfaaghavtAPGPDRGMVFQHHA---LLPWMT--AKGNIEFGLKsarP 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRgteLQDYFKklANGEIKVAHK---P 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 106 Q----------------LSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDAL 169
Cdd:COG1245 167 QyvdlipkvfkgtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721987636 170 TRRELQLQLRNVWEANrRTVIMVTHDVdeAIL--LSDRILVM 209
Cdd:COG1245 247 QRLNVARLIRELAEEG-KYVLVVEHDL--AILdyLADYVHIL 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-208 |
2.60e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIApTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAghaVT--------APGPDrg 78
Cdd:PRK13409 341 VEYPDLTKKLGDFSLEV-EGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKisykpqyiKPDYD-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 mvfqhhallpwmtakGNIEFGLKSARPQLSRA-ERSEIADQFlqqvGLAHAASRRPARLSGGMQQRVGLARAFAVDPEIL 157
Cdd:PRK13409 415 ---------------GTVEDLLRSITDDLGSSyYKSEIIKPL----QLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 158 LLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDV---DeaiLLSDRILV 208
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIymiD---YISDRLMV 526
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-215 |
8.89e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 67.66 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYgaAEVIAPT----SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPgpdrgmvfq 82
Cdd:TIGR00957 637 ITVHNATFTW--ARDLPPTlngiTFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVP--------- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 HHALLPWMTAKGNIEFG--LKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:TIGR00957 706 QQAWIQNDSLRENILFGkaLNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 161 EPFGALDALTRREL-------QLQLRNvweanrRTVIMVTHDVdEAILLSDRILVMSHGPRS 215
Cdd:TIGR00957 786 DPLSAVDAHVGKHIfehvigpEGVLKN------KTRILVTHGI-SYLPQVDVIIVMSGGKIS 840
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-212 |
1.02e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 3 NSSHVELRNITKSYGAAE-VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAG-------HAVTAPG 74
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslsHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 PdrGMVFQHHALLPwMTAKGNIEFGlksarpqlsRAERSEIADQFLQQVGLAHAASRRPA-----------RLSGGMQQR 143
Cdd:PRK10790 417 V--AMVQQDPVVLA-DTFLANVTLG---------RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 144 VGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEanRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRL-STIVEADTILVLHRG 550
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
90-215 |
1.79e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 90 MTAKGNIEFGLKSA-RPQLSRAERSEIADQFLQQVGLAHAASRRP--ARLSGGMQQRVGLARAFAVDPEILLLDEPFGAL 166
Cdd:PTZ00265 1310 MSIYENIKFGKEDAtREDVKRACKFAAIDEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1721987636 167 DALTRRELQLQLRNVWEANRRTVIMVTHDVdEAILLSDRILVMSHGPRS 215
Cdd:PTZ00265 1390 DSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNNPDRT 1437
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-212 |
2.57e-12 |
|
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: 66.58 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYG--AAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDrgmVFQHH 84
Cdd:TIGR01257 1938 LRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 ALLPWMTAKGNIEFGLKS----ARPQLSRAERSE-IADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHlylyARLRGVPAEEIEkVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREG-RAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-212 |
2.79e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 9 LRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPgpDRGMVFQHHALLP 88
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW--SSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 89 W-------MTAKGNIEFGLKSARPQLSR--AERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:PRK10575 92 QqlpaaegMTVRELVAIGRYPWHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGG 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-212 |
3.79e-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: 63.67 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITKSY--GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----G 78
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrsriS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPwmtakGNIEFGLKSarpqLSRAERSEIAdQFLQQVGLAHAASRRPARL-----------SGGMQQRVGLA 147
Cdd:cd03244 82 IIPQDPVLFS-----GTIRSNLDP----FGEYSDEELW-QALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNvwEANRRTVIMVTHDVDeAILLSDRILVMSHG 212
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLD-TIIDSDRILVLDKG 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-209 |
4.08e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 62.39 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 32 GQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGhavtapgpdrgmvfqhhallpwmtakgniefglksarpqlsrAE 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------GE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 112 RSEIADQFLQQVGLAHaasRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVW-----EANR 186
Cdd:smart00382 40 DILEEVLDQLLLIIVG---GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkSEKN 116
|
170 180
....*....|....*....|....*...
gi 1721987636 187 RTVIMVTHDV-----DEAILLSDRILVM 209
Cdd:smart00382 117 LTVILTTNDEkdlgpALLRRRFDRRIVL 144
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-220 |
5.94e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGlAFPS---------TGEVFAAGHAVTAPGPDRgmVFQHHALLPWMTAKGNI 96
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPLAAIDAPR--LARLRAVLPQAAQPAFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 97 ----EFGLKSARPQLSRA-----ERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFA---------VDPEILL 158
Cdd:PRK13547 98 fsarEIVLLGRYPHARRAgalthRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 159 LDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGprsTIIAD 220
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADG---AIVAH 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-209 |
9.16e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 9.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 31 EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAghavtaPGPD------RGMVFQHH-ALLpwmtAKGNIEFGLKsa 103
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEE------PSWDevlkrfRGTELQNYfKKL----YNGEIKVVHK-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 104 rPQ----------------LSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALD 167
Cdd:PRK13409 166 -PQyvdlipkvfkgkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 168 -------ALTRRELqlqlrnvweANRRTVIMVTHDVdeAIL--LSDRILVM 209
Cdd:PRK13409 245 irqrlnvARLIREL---------AEGKYVLVVEHDL--AVLdyLADNVHIA 284
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
26-170 |
1.35e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTApgpDRG-----MVFQHH--ALLPWMTAKGNIEF 98
Cdd:PRK13540 21 SFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK---DLCtyqkqLCFVGHrsGINPYLTLRENCLY 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 99 GLKSARPQLsraersEIaDQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALT 170
Cdd:PRK13540 98 DIHFSPGAV------GI-TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
12-230 |
1.83e-11 |
|
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: 61.05 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 12 ITKSYGAAEVIAPTSVhIDEGQFVSILGPSGCGKSTILSMIAGLAFPStgevfaaghavtapgpdrgmvfqhhallpwmt 91
Cdd:cd03222 6 CVKRYGVFFLLVELGV-VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN-------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 92 aKGNIEFGLK--SARPQLsraerseiadqflqqvglahaasrrpARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDAL 169
Cdd:cd03222 53 -GDNDEWDGItpVYKPQY--------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 170 TRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGPRSTIIADIEVATRSNHN 230
Cdd:cd03222 106 QRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGIN 166
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-230 |
3.76e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGA---AEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAA-GHAVTAPG-- 74
Cdd:PTZ00265 377 LKDIKKIQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINlk 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 ---PDRGMVFQHhALLPWMTAKGNIEFGLKSARPQLSRAERSEiADQFLQQVGLAHAASRRP------------------ 133
Cdd:PTZ00265 457 wwrSKIGVVSQD-PLLFSNSIKNNIKYSLYSLKDLEALSNYYN-EDGNDSQENKNKRNSCRAkcagdlndmsnttdsnel 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 134 -------------------------------------------ARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALT 170
Cdd:PTZ00265 535 iemrknyqtikdsevvdvskkvlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 171 RRELQLQLRNVWEANRRTVIMVTHDVdEAILLSDRILVMSH---GPRSTIIADIEVATRSNHN 230
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITIIIAHRL-STIRYANTIFVLSNrerGSTVDVDIIGEDPTKDNKE 676
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-198 |
5.86e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAvtapgpdrGMVFQHHALLPWMTAKGNIEfgLKSARP 105
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--------ALIAISSGLNGQLTGIENIE--LKGLMM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 106 QLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDAlTRRELQLQLRNVWEAN 185
Cdd:PRK13545 114 GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ-TFTKKCLDKMNEFKEQ 192
|
170
....*....|...
gi 1721987636 186 RRTVIMVTHDVDE 198
Cdd:PRK13545 193 GKTIFFISHSLSQ 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-212 |
1.11e-10 |
|
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: 59.46 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGlaFPST----GEVFAAGHAVTAPGPDR------ 77
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKYevteGEILFKGEDITDLPPEErarlgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVFQHHALLPwmtakgniefGLKSArpqlsraerseiadQFLQQVGLAhaasrrparLSGGMQQRVGLARAFAVDPEIL 157
Cdd:cd03217 80 FLAFQYPPEIP----------GVKNA--------------DFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 158 LLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTHdvDEAILL---SDRILVMSHG 212
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEG-KSVLIITH--YQRLLDyikPDRVHVLYDG 181
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-209 |
1.13e-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: 60.07 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 31 EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDRGMVFQHH------------------ALLPwMTA 92
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYftkllegdvkvivkpqyvDLIP-KAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 93 KGNIEFGLKsarpqlsRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRR 172
Cdd:cd03236 104 KGKVGELLK-------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1721987636 173 ELQLQLRNVWEaNRRTVIMVTHDVdeAIL--LSDRILVM 209
Cdd:cd03236 177 NAARLIRELAE-DDNYVLVVEHDL--AVLdyLSDYIHCL 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
29-212 |
1.15e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 29 IDEGQFVSILGPSGCGKSTILSMIAGLaFPSTGEVfaaGHAVTAPG------PDR----------GMVFQH--HALLPWM 90
Cdd:PRK09473 39 LRAGETLGIVGESGSGKSQTAFALMGL-LAANGRI---GGSATFNGreilnlPEKelnklraeqiSMIFQDpmTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 91 TAKGNIEFGLKSARpQLSRAERSEIADQFLQQVGLAHAASRR---PARLSGGMQQRVGLARAFAVDPEILLLDEPFGALD 167
Cdd:PRK09473 115 RVGEQLMEVLMLHK-GMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1721987636 168 ALTRRELqLQLRNvwEANRR---TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK09473 194 VTVQAQI-MTLLN--ELKREfntAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-212 |
1.39e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILS-MIAGLAFPSTGEVFAAGHAVTAPGpdrgmvfqhhalLPWM---TAKGNIEFGLK 101
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAYVPQ------------VSWIfnaTVRENILFGSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 102 SARPQLSRA--------ERSEIADQFLQQVGlahaasRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRE 173
Cdd:PLN03232 705 FESERYWRAidvtalqhDLDLLPGRDLTEIG------ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1721987636 174 -----LQLQLRNvweanrRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:PLN03232 779 vfdscMKDELKG------KTRVLVTNQL-HFLPLMDRIILVSEG 815
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-162 |
1.73e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 38 LGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTApgpdRGM--------------------VFQH---HALLpwmtakg 94
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA----GDIatrrrvgymsqafslygeltVRQNlelHARL------- 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 95 nieFGLKSARpqlsRAERseiADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEP 162
Cdd:NF033858 367 ---FHLPAAE----IAAR---VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-195 |
1.89e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 15 SYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTA------PGPDRGMVF------- 81
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpPRNVEGTVYdfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 82 --------QHHALLPWMtAKGNIEFGLKsarpQLSRA-ERSEIAD--QF-------LQQVGLAhaASRRPARLSGGMQQR 143
Cdd:PRK11147 92 eeqaeylkRYHDISHLV-ETDPSEKNLN----ELAKLqEQLDHHNlwQLenrinevLAQLGLD--PDAALSSLSGGWLRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 144 VGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVweanRRTVIMVTHD 195
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHD 212
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-175 |
2.46e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.33 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfAAGHAVtapgpDRGMVFQ-HHA 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-EIGETV-----KLAYVDQsRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 LLP----WMTAKGNIEFGLKSARPQLSRAERSEI----ADQflqqvglahaaSRRPARLSGGMQQRVGLARAFAVDPEIL 157
Cdd:TIGR03719 397 LDPnktvWEEISGGLDIIKLGKREIPSRAYVGRFnfkgSDQ-----------QKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|....*...
gi 1721987636 158 LLDEPFGALDALTRRELQ 175
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALE 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
136-218 |
3.06e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 136 LSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELqLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGPRS 215
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEI-YQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
...
gi 1721987636 216 TII 218
Cdd:PRK10982 471 GIV 473
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-212 |
3.27e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITkSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFP----STGEVFAAGHAVtAPGPDRG---- 78
Cdd:PRK10418 5 IELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV-APCALRGrkia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQH--HALLPWMT-AKGNIEFGLKSARPQLSRAERseiadQFLQQVGLAHAA---SRRPARLSGGMQQRVGLARAFAV 152
Cdd:PRK10418 83 TIMQNprSAFNPLHTmHTHARETCLALGKPADDATLT-----AALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 153 DPEILLLDEPFGALDALTR-RELQLqLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQaRILDL-LESIVQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-220 |
4.79e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAaeVIAPTSVHID--EGQFVSILGPSGCGKSTILSMIAGLaFPS---TGEVFAAGHAVTAPG----PDRG 78
Cdd:NF040905 3 EMRGITKTFPG--VKALDDVNLSvrEGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKDirdsEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHH--ALLPWMTAKGNIEFGLKSARPQL-SRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPE 155
Cdd:NF040905 80 IVIIHQelALIPYLSIAENIFLGNERAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 156 ILLLDEPFGAL-----DALTrrELQLQLRnvweANRRTVIMVTHDVDEAILLSDRIlvmshgprsTIIAD 220
Cdd:NF040905 160 LLILDEPTAALneedsAALL--DLLLELK----AQGITSIIISHKLNEIRRVADSI---------TVLRD 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-212 |
7.73e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPgpdrgmvfQHhallPWM---TAKGNIEFGLKS 102
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVP--------QQ----AWImnaTVRGNILFFDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 103 ARPQLSRAERSEIADQFLQQV--GLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA----LTRRELQL 176
Cdd:PTZ00243 748 DAARLADAVRVSQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhvgeRVVEECFL 827
|
170 180 190
....*....|....*....|....*....|....*..
gi 1721987636 177 -QLRNvweanrRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:PTZ00243 828 gALAG------KTRVLATHQV-HVVPRADYVVALGDG 857
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-224 |
7.82e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEvfaaghavtapgpdRGMVFQHHALLP-----------W----- 89
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--------------RQSQFSHITRLSfeqlqklvsdeWqrnnt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 90 -MTAKGNIEFGLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDA 168
Cdd:PRK10938 89 dMLSPGEDDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 169 LTRRELQLQLRNVWEANRRTVIMVT--HD----VDEAILLSDRILVMShGPRSTIIADIEVA 224
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLVLNrfDEipdfVQFAGVLADCTLAET-GEREEILQQALVA 229
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
6-195 |
1.73e-09 |
|
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: 56.08 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNItKSYGAAEVIAptsvhIDEGQFVsILGPSGCGKSTIlsmIAGLAFPSTGEvfaaghavTAPGPDRGmvfqhhA 85
Cdd:cd03240 3 KLSIRNI-RSFHERSEIE-----FFSPLTL-IVGQNGAGKTTI---IEALKYALTGE--------LPPNSKGG------A 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 LLPWMTAKGN----IEFGLKSARPQLSRAERS-EIADQ--FLQQVGLAHAASRRPARLSGGmQQ-------RVGLARAFA 151
Cdd:cd03240 59 HDPKLIREGEvraqVKLAFENANGKKYTITRSlAILENviFCHQGESNWPLLDMRGRCSGG-EKvlasliiRLALAETFG 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1721987636 152 VDPEILLLDEPFGALDALTRRElqlQLRNVWEANR----RTVIMVTHD 195
Cdd:cd03240 138 SNCGILALDEPTTNLDEENIEE---SLAEIIEERKsqknFQLIVITHD 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-212 |
1.96e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 20 EVIAPTSVHID--EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV-TAPGP-------DRGMVFQ--HHALL 87
Cdd:PRK10261 336 EVHAVEKVSFDlwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGklqalrrDIQFIFQdpYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 88 PWMTAKGNIEFGLKSARPQLSRAERSEIAdQFLQQVGL-AHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGAL 166
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLPGKAAAARVA-WLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721987636 167 DALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-209 |
2.08e-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: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 3 NSSHVELRNITKSY--GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAfPSTGEVFAaghavtapgpdRGMV 80
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQI-----------DGVS 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 81 FQHHALLPWMTAKGNIEFGL--------KSARP--QLSRAERSEIADQflqqVGLAHAASRRPARL-----------SGG 139
Cdd:TIGR01271 1282 WNSVTLQTWRKAFGVIPQKVfifsgtfrKNLDPyeQWSDEEIWKVAEE----VGLKSVIEQFPDKLdfvlvdggyvlSNG 1357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 140 MQQRVGLARAFAVDPEILLLDEPFGALDALT----RRELQLQLRNVweanrrTVIMVTHDVdEAILLSDRILVM 209
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTlqiiRKTLKQSFSNC------TVILSEHRV-EALLECQQFLVI 1424
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-212 |
2.47e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 29 IDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAvtapgpdRGMVF-QHHA---------LLPWMTAkgnief 98
Cdd:PLN03073 532 IDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-------RMAVFsQHHVdgldlssnpLLYMMRC------ 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 99 gLKSARPQLSRAErseiadqfLQQVGLAHAASRRPA-RLSGGMQQRVGLARAFAVDPEILLLDEPFGALDaLTRRELQLQ 177
Cdd:PLN03073 599 -FPGVPEQKLRAH--------LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-LDAVEALIQ 668
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721987636 178 LRNVWEANrrtVIMVTHD-------VDEAILLSDRILVMSHG 212
Cdd:PLN03073 669 GLVLFQGG---VLMVSHDehlisgsVDELWVVSEGKVTPFHG 707
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-204 |
2.57e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 32 GQFVSILGPSGCGKSTILSMIAGLAFPSTGevfaaGHAVTapgpdRGMVfqhhALLP---WM---TAKGNIEFGLKSARP 105
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSD-----ASVVI-----RGTV----AYVPqvsWIfnaTVRDNILFGSPFDPE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 106 QLSRAERSEIADQFLQQV--GLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRE-----LQLQL 178
Cdd:PLN03130 709 RYERAIDVTALQHDLDLLpgGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQvfdkcIKDEL 788
|
170 180 190
....*....|....*....|....*....|..
gi 1721987636 179 RNvweanrRTVIMVTHD------VDEAILLSD 204
Cdd:PLN03130 789 RG------KTRVLVTNQlhflsqVDRIILVHE 814
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-195 |
4.51e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAvtapgpDRGMVFQHHA- 85
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA------NIGYYAQDHAy 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 -------LLPWMTAKGNIEFGLKSARPQLSRAERSeiADQFLQQVGLahaasrrparLSGGMQQRVGLARAFAVDPEILL 158
Cdd:PRK15064 394 dfendltLFDWMSQWRQEGDDEQAVRGTLGRLLFS--QDDIKKSVKV----------LSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190
....*....|....*....|....*....|....*..
gi 1721987636 159 LDEPFGALDALTRRELQLQLrnvwEANRRTVIMVTHD 195
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHD 494
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-213 |
6.54e-09 |
|
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: 53.87 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSmiAGLAfpstgevfAAGHAVTAPGPDRgmvFQHHALLpwmtakgniefglksARP 105
Cdd:cd03238 15 DVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--------ASGKARLISFLPK---FSRNKLI---------------FID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 106 QLsraerseiadQFLQQVGLAHAASRRPAR-LSGGMQQRVGLARAFAVDPE--ILLLDEPFGALDALTRRELQLQLRNVW 182
Cdd:cd03238 67 QL----------QFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLI 136
|
170 180 190
....*....|....*....|....*....|.
gi 1721987636 183 EANrRTVIMVTHDVDeAILLSDRILVMSHGP 213
Cdd:cd03238 137 DLG-NTVILIEHNLD-VLSSADWIIDFGPGS 165
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
109-216 |
7.22e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 109 RAERSEIADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVwEANRRT 188
Cdd:PRK15056 116 KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKT 194
|
90 100 110
....*....|....*....|....*....|...
gi 1721987636 189 VIMVTHDVDEAILLSDRIL-----VMSHGPRST 216
Cdd:PRK15056 195 MLVSTHNLGSVTEFCDYTVmvkgtVLASGPTET 227
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-161 |
8.93e-09 |
|
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: 55.53 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 21 VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLaFPstgeVFAAGHAVTAPG-----PDRgmvfqhhallPWMTakgn 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WP----VYGGRLTKPAKGklfyvPQR----------PYMT---- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 96 iefgLKSARPQLSRAERSE------IAD----QFLQQVGLAHAASRRPA---------RLSGGMQQRVGLARAFAVDPEI 156
Cdd:TIGR00954 528 ----LGTLRDQIIYPDSSEdmkrrgLSDkdleQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQF 603
|
....*
gi 1721987636 157 LLLDE 161
Cdd:TIGR00954 604 AILDE 608
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
6-216 |
9.66e-09 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 54.20 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 6 HVELRNITkSYGAAEVIAPTSVHIDeGQFVsILGPSGCGKSTILSMIAgLAFpsTGEVFAAGHAVtapgpDRGMVFQHHA 85
Cdd:cd03279 5 KLELKNFG-PFREEQVIDFTGLDNN-GLFL-ICGPTGAGKSTILDAIT-YAL--YGKTPRYGRQE-----NLRSVFAPGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 86 LlpwmTAKGNIEFglkSARPQLSRAERSE--IADQFLQQVGLA--HAAS--RRPAR-LSGGMQQRVGLARAFAVDPEI-- 156
Cdd:cd03279 74 D----TAEVSFTF---QLGGKKYRVERSRglDYDQFTRIVLLPqgEFDRflARPVStLSGGETFLASLSLALALSEVLqn 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 157 --------LLLDEPFGALDAlTRRELQLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHGPRST 216
Cdd:cd03279 147 rggarleaLFIDEGFGTLDP-EALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTPGGSR 213
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-212 |
1.23e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.48 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY--GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFpSTGEVfaaghavtapgPDRGMVFQHH 84
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDI-----------QIDGVSWNSV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 ALLPWMTAKGNIEFGL--------KSARP--QLSRAERSEIADQflqqVGLAHAASRRPARL-----------SGGMQQR 143
Cdd:cd03289 71 PLQKWRKAFGVIPQKVfifsgtfrKNLDPygKWSDEEIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 144 VGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANrrTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADC--TVILSEHRI-EAMLECQRFLVIEEN 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-179 |
1.44e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 2 TNSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIaglafpsTGEvFAAGHA--VTAPGPDRGM 79
Cdd:PRK10938 256 ANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGD-HPQGYSndLTLFGRRRGS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 ------VFQHhalLPWMTAKGNIEFGLK-SAR--------------PQLSRAERSeIADQFLQQVGLAHAASRRPAR-LS 137
Cdd:PRK10938 328 getiwdIKKH---IGYVSSSLHLDYRVStSVRnvilsgffdsigiyQAVSDRQQK-LAQQWLDILGIDKRTADAPFHsLS 403
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1721987636 138 GGmQQRVGL-ARAFAVDPEILLLDEPFGALDALTRrelQLQLR 179
Cdd:PRK10938 404 WG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNR---QLVRR 442
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-212 |
2.48e-08 |
|
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: 52.80 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGA--AEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPDR-----GM 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrsslTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 VFQHHALLPWmTAKGNIE-FGLKSARpqlsraerseiadqflqQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILL 158
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDpFDEYSDE-----------------EIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 159 LDEPFGALDALTRRELQLQLRNvwEANRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03369 149 LDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRL-RTIIDYDKILVMDAG 199
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-218 |
2.90e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.37 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTgevfaaghAVTAP---------------------GPDRGMVFQHH 84
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW--------HVTADrfrwngidllklsprerrkiiGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 85 A--LLPWMTakgnIEFGLKSARPQLS--------RAERSEIADQFLQQVGLA-HAASRR--PARLSGGMQQRVGLARAFA 151
Cdd:COG4170 99 SscLDPSAK----IGDQLIEAIPSWTfkgkwwqrFKWRKKRAIELLHRVGIKdHKDIMNsyPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721987636 152 VDPEILLLDEPFGALDALTRRE-LQL-----QLRNVweanrrTVIMVTHDVDEAILLSDRILVM------SHGPRSTII 218
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQiFRLlarlnQLQGT------SILLISHDLESISQWADTITVLycgqtvESGPTEQIL 247
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-212 |
4.38e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.26 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAE-----VIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPGPD--RGM- 79
Cdd:COG4615 329 ELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayRQLf 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 80 --VFQhhallpwmtakgniEFGLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPAR-----LSGGMQQRVGLARAFAV 152
Cdd:COG4615 409 saVFS--------------DFHLFDRLLGLDGEADPARARELLERLELDHKVSVEDGRfsttdLSQGQRKRLALLVALLE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721987636 153 DPEILLLDE-------PFgaldaltRR----ELQLQLRnvweANRRTVIMVTHDvDEAILLSDRILVMSHG 212
Cdd:COG4615 475 DRPILVFDEwaadqdpEF-------RRvfytELLPELK----ARGKTVIAISHD-DRYFDLADRVLKMDYG 533
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-161 |
1.09e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 37 ILGPSGCGKSTILSMIAGLAFPSTGEVFAAG-HAVTAPGPDRGMVFQHHALLPWMTAKGNIEFGLKSArpqlsraERSEI 115
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY-------NSAET 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1721987636 116 ADQFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDE 161
Cdd:PRK13541 104 LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
31-196 |
1.10e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 31 EGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHaVTAPGPDRGMVFQhhallpwMTAKGNIEFGL---------- 100
Cdd:PRK13546 49 EGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISAGLSGQ-------LTGIENIEFKMlcmgfkrkei 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 101 KSARPQLsrAERSEIADQFLQQVglahaasrrpARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRN 180
Cdd:PRK13546 121 KAMTPKI--IEFSELGEFIYQPV----------KKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170
....*....|....*.
gi 1721987636 181 VWEANrRTVIMVTHDV 196
Cdd:PRK13546 189 FKEQN-KTIFFVSHNL 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-212 |
1.39e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 4 SSHVELRNITKSY--GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG------- 74
Cdd:TIGR00957 1282 RGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlrfk 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 75 ----PDRGMVFQHhallpwmTAKGNIE-FGLKSARPQLSRAERSEIADqFL--QQVGLAHAASRRPARLSGGMQQRVGLA 147
Cdd:TIGR00957 1362 itiiPQDPVLFSG-------SLRMNLDpFSQYSDEEVWWALELAHLKT-FVsaLPDKLDHECAEGGENLSVGQRQLVCLA 1433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721987636 148 RAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANrrTVIMVTHDVDeAILLSDRILVMSHG 212
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLN-TIMDYTRVIVLDKG 1495
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-195 |
2.58e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 11 NITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFaaghavTAPGPDRGMVFQ-------- 82
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS------LDPNERLGKLRQdqfafeef 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 83 ---------HHAL------------LPWMTAkgniEFGLKSARPQLSRAE--------RseiADQFLQQVGLA---Haas 130
Cdd:PRK15064 80 tvldtvimgHTELwevkqerdriyaLPEMSE----EDGMKVADLEVKFAEmdgytaeaR---AGELLLGVGIPeeqH--- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721987636 131 rrparlSGGMQQ-------RVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLrnvweaNRR--TVIMVTHD 195
Cdd:PRK15064 150 ------YGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL------NERnsTMIIISHD 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-212 |
2.63e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYgAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIA----GLAFPSTGEVFAAGHavtapGPD------R 77
Cdd:TIGR00956 64 KLKKFRDTK-TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGI-----TPEeikkhyR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 GMVF---QHHALLPWMTAKGNIEFGLKSARPQ-----LSRAERSE-IADQFLQQVGLAHAASRRPAR-----LSGGMQQR 143
Cdd:TIGR00956 138 GDVVynaETDVHFPHLTVGETLDFAARCKTPQnrpdgVSREEYAKhIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKR 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 144 VGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAIL-LSDRILVMSHG 212
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYEG 287
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-174 |
3.55e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfAAGHAVtapgpDRGMVFQHHAL 86
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-KIGETV-----KLAYVDQSRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 87 LP-----W-MTAKGN--IEFGlKSARPqlSRAERSEI----ADQflQQ-VGLahaasrrparLSGGMQQRVGLARAFAVD 153
Cdd:PRK11819 399 LDpnktvWeEISGGLdiIKVG-NREIP--SRAYVGRFnfkgGDQ--QKkVGV----------LSGGERNRLHLAKTLKQG 463
|
170 180
....*....|....*....|.
gi 1721987636 154 PEILLLDEPFGALDALTRREL 174
Cdd:PRK11819 464 GNVLLLDEPTNDLDVETLRAL 484
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-212 |
6.52e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSY----GAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPS---TGEVF--------------- 64
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvTADRMrfddidllrlsprer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 65 --AAGHAVTapgpdrgMVFQH------------HAL---LPWMTAKGNI--EFGLKSARpqlsraerseiADQFLQQVGL 125
Cdd:PRK15093 84 rkLVGHNVS-------MIFQEpqscldpservgRQLmqnIPGWTYKGRWwqRFGWRKRR-----------AIELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 126 -AHAASRR--PARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNVWEANRRTVIMVTHDVDEAILL 202
Cdd:PRK15093 146 kDHKDAMRsfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQW 225
|
250
....*....|
gi 1721987636 203 SDRILVMSHG 212
Cdd:PRK15093 226 ADKINVLYCG 235
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-167 |
1.00e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 1 MTNSSHVELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGlaFPS----TGEVFAAGHAVTAPGPD 76
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 77 ----RG--MVFQHHALLPWMTakgNIEF---GLKSAR-----PQLSRAERSEIADQFLQQVGL-AHAASRRPAR-LSGGM 140
Cdd:CHL00131 80 erahLGifLAFQYPIEIPGVS---NADFlrlAYNSKRkfqglPELDPLEFLEIINEKLKLVGMdPSFLSRNVNEgFSGGE 156
|
170 180
....*....|....*....|....*..
gi 1721987636 141 QQRVGLARAFAVDPEILLLDEPFGALD 167
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLD 183
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-195 |
2.34e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 8 ELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTApgpdrgmVF-QHHAL 86
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVA-------YFdQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 87 L-PWMTAKGNIEFGLKS------ARPQLSraerseiadqFLQQVGLAHAASRRPAR-LSGGMQQRVGLARAFAVDPEILL 158
Cdd:PRK11147 394 LdPEKTVMDNLAEGKQEvmvngrPRHVLG----------YLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190
....*....|....*....|....*....|....*..
gi 1721987636 159 LDEPFGALDALTrreLQLqLRNVWEANRRTVIMVTHD 195
Cdd:PRK11147 464 LDEPTNDLDVET---LEL-LEELLDSYQGTVLLVSHD 496
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-209 |
2.79e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 24 PTSVHIDEGQFVSILGPSGCGKSTIL---SMIAGLAFPST--GEVFAAGHAVTApgpdrgmvfqhhallpwmtakgnIEF 98
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILdaiGLALGGAQSATrrRSGVKAGCIVAA-----------------------VSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 99 GLKSARPQlsraerseiadqflqqvglahaasrrparLSGGMQQRVGLARAFA---VDPEIL-LLDEPFGALDAL-TRRE 173
Cdd:cd03227 70 ELIFTRLQ-----------------------------LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRdGQAL 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 1721987636 174 LQLQLRNVweANRRTVIMVTHDvDEAILLSDRILVM 209
Cdd:cd03227 121 AEAILEHL--VKGAQVIVITHL-PELAELADKLIHI 153
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-207 |
3.37e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 29 IDEGQFVSILGPSGCGKSTILSMIaglafpsTGEVFAAGHAVTAPGP-DRGMVFQHHALLPwMTA-----KGNIEFGLKS 102
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNwQLAWVNQETPALP-QPAleyviDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 103 ARPQLSRAE---------------------RSEiADQFLQQVGLAHAASRRPAR-LSGGMQQRVGLARAFAVDPEILLLD 160
Cdd:PRK10636 96 AQLHDANERndghaiatihgkldaidawtiRSR-AASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1721987636 161 EPFGALDALTRRELQLQLRNVweanRRTVIMVTHDVDEAILLSDRIL 207
Cdd:PRK10636 175 EPTNHLDLDAVIWLEKWLKSY----QGTLILISHDRDFLDPIVDKII 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-212 |
4.27e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 4.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721987636 135 RLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELqLQLRNVWEANRRTVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEI-YTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEG 480
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
29-212 |
5.99e-06 |
|
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: 45.72 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 29 IDEGQFVSILGPSGCGKSTILSMIAGLAFPS---TGEVFAAGHAV--TAPGPDRGMVF--QHHALLPWMTAKGNIEFglk 101
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYkeFAEKYPGEIIYvsEEDVHFPTLTVRETLDF--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 102 SARPQlsraerseiADQFLQQVglahaasrrparlSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNV 181
Cdd:cd03233 107 ALRCK---------GNEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTM 164
|
170 180 190
....*....|....*....|....*....|..
gi 1721987636 182 WEANRRTVIM-VTHDVDEAILLSDRILVMSHG 212
Cdd:cd03233 165 ADVLKTTTFVsLYQASDEIYDLFDKVLVLYEG 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-194 |
1.08e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPS--------------TGEVFAAGHAVTA 72
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDGipkncqilhveqevVGDDTTALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 73 PGPDRGMVFQHHALL-------PWMTAKGNIEFGLKSARPQLSRAERSEIADQFLQQVGLAHAASRRPARL--------- 136
Cdd:PLN03073 258 TDIERTQLLEEEAQLvaqqrelEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILaglsftpem 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721987636 137 --------SGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNvWEanrRTVIMVTH 194
Cdd:PLN03073 338 qvkatktfSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WP---KTFIVVSH 399
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-195 |
1.75e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 12 ITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVfaaghaVTAPGPDRGMVFQHHalLPWMT 91
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI------GLAKGIKLGYFAQHQ--LEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 92 AKgniefglKSARPQLSRAERSEIADQFLQQVG----LAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALD 167
Cdd:PRK10636 390 AD-------ESPLQHLARLAPQELEQKLRDYLGgfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170 180
....*....|....*....|....*...
gi 1721987636 168 ALTRRELQLQLRNVWEAnrrtVIMVTHD 195
Cdd:PRK10636 463 LDMRQALTEALIDFEGA----LVVVSHD 486
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-212 |
2.74e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 44.13 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 21 VIAPTSVHIDEGQFVSILGPSGCGKSTIlsmiaGLAFPSTGEVFAAghAVTAPGPDRgmvfqhhALLPWMTAK------- 93
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSL-----SLAFFRMVDIFDG--KIVIDGIDI-------SKLPLHTLRsrlsiil 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 94 -------GNIEFGLKSARPQLSRA--ERSEIAdQFLQQV-----GLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLL 159
Cdd:cd03288 102 qdpilfsGSIRFNLDPECKCTDDRlwEALEIA-QLKNMVkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721987636 160 DEPFGALDALTRRELQLQLRNVWEanRRTVIMVTHDVdEAILLSDRILVMSHG 212
Cdd:cd03288 181 DEATASIDMATENILQKVVMTAFA--DRTVVTIAHRV-STILDADLVLVLSRG 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-212 |
4.24e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 35 VSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG-----------PDRGMVFQHhallpwmTAKGNIEFGLKSA 103
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGltdlrrvlsiiPQSPVLFSG-------TVRFNIDPFSEHN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 104 RPQLSRA-ERSEIADQFLQQ-VGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRRELQLQLRNv 181
Cdd:PLN03232 1338 DADLWEAlERAHIKDVIDRNpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE- 1416
|
170 180 190
....*....|....*....|....*....|.
gi 1721987636 182 wEANRRTVIMVTHDVDeAILLSDRILVMSHG 212
Cdd:PLN03232 1417 -EFKSCTMLVIAHRLN-TIIDCDKILVLSSG 1445
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
118-213 |
9.25e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 118 QFLQQVGLAH-AASRRPARLSGGMQQRVGLARAF--AVDPEILLLDEPFGALDALTRRELQLQLRNVWEANrRTVIMVTH 194
Cdd:cd03270 119 GFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLG-NTVLVVEH 197
|
90
....*....|....*....
gi 1721987636 195 DvDEAILLSDRILVMshGP 213
Cdd:cd03270 198 D-EDTIRAADHVIDI--GP 213
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-194 |
1.43e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 7 VELRNITKSYGAAEVIAPTSVHIDEGQFVSILGPSGCGKSTILSMIAGLA--FPSTGEVFAAGHAVTAPGP-DRG----- 78
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPeDRAgegif 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 79 MVFQHHALLPWMTAKGNIEFGLKSAR-----PQLSRAERSEIADQFLQQVGLAHAASRRPARL--SGGMQQRVGLARAFA 151
Cdd:PRK09580 82 MAFQYPVEIPGVSNQFFLQTALNAVRsyrgqEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1721987636 152 VDPEILLLDEPFGAL--DALtrrELQLQLRNVWEANRRTVIMVTH 194
Cdd:PRK09580 162 LEPELCILDESDSGLdiDAL---KIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-212 |
1.82e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 9 LRNITKSYGAAEV-------IAPTSVHidegqfvSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAV----TAPGPDR 77
Cdd:PRK10982 1 MSNISKSFPGVKAldnvnlkVRPHSIH-------ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 78 G--MVFQHHALLPWMTAKGNIEFG---LKSARPQLSRAERSEIAdqFLQQVGLAHAASRRPARLSGGMQQRVGLARAFAV 152
Cdd:PRK10982 74 GisMVHQELNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKA--IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721987636 153 DPEILLLDEPfgaLDALTRRELQLQLRNVWEANRR--TVIMVTHDVDEAILLSDRILVMSHG 212
Cdd:PRK10982 152 NAKIVIMDEP---TSSLTEKEVNHLFTIIRKLKERgcGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-212 |
3.15e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 32 GQFVSILGPSGCGKSTILSMIAGL-------------AFPSTGEVFAAghavtapgpDRGMVFQHHALLPWMTAKGNIEF 98
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRktggyiegdirisGFPKKQETFAR---------ISGYCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 99 GLKSARP-QLSRAERSEIADQFLQQV---GLAHAASRRPA--RLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRR 172
Cdd:PLN03140 977 SAFLRLPkEVSKEEKMMFVDEVMELVeldNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1721987636 173 ELQLQLRNVWEANrRTVIMVTH----DVDEAIllsDRILVMSHG 212
Cdd:PLN03140 1057 IVMRTVRNTVDTG-RTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
114-217 |
4.29e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 114 EIADQ--FLQQVGLAHAASRRPAR-LSGGMQQRVGLA-----RAFAVdpeILLLDEP-FGALDALTRRELQ--LQLRNVw 182
Cdd:TIGR00630 464 EIRERlgFLIDVGLDYLSLSRAAGtLSGGEAQRIRLAtqigsGLTGV---LYVLDEPsIGLHQRDNRRLINtlKRLRDL- 539
|
90 100 110
....*....|....*....|....*....|....*
gi 1721987636 183 eANrrTVIMVTHDvDEAILLSDRILVMshGPRSTI 217
Cdd:TIGR00630 540 -GN--TLIVVEHD-EDTIRAADYVIDI--GPGAGE 568
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
123-208 |
4.51e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 123 VGLAHAASRRPAR-LSGGMQQRVGLARAFAVDP----------EILLLDEPFGALDALTRRELQLQLRNVWEANRR-TVI 190
Cdd:TIGR00618 937 VADAYTGSVRPSAtLSGGETFLASLSLALALADllstsggtvlDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMiGII 1016
|
90
....*....|....*...
gi 1721987636 191 MVTHDVDEAIllSDRILV 208
Cdd:TIGR00618 1017 SHVPEFRERI--PHRILV 1032
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-221 |
7.16e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 32 GQFVSILGPSGCGKSTILSMIAG---LAFPSTGEVFAAGHAVTAPGPDR-GMVFQHHALLPWMTAKGNIEFGLKSARPQ- 106
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLDSSFQRSiGYVQQQDLHLPTSTVRESLRFSAYLRQPKs 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 107 LSRAERSEIADQFLQQVGL---AHAASRRPAR-LSGGMQQRVGLARAFAVDPEILL-LDEPFGALDALTRRELQLQLRNV 181
Cdd:TIGR00956 869 VSKSEKMEYVEEVIKLLEMesyADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721987636 182 weANRRTVIMVTHDVDEAILLS--DRILVMSHGPRSTIIADI 221
Cdd:TIGR00956 949 --ADHGQAILCTIHQPSAILFEefDRLLLLQKGGQTVYFGDL 988
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
14-52 |
1.53e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.60 E-value: 1.53e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1721987636 14 KSYGAaeviaPTSVHIDEGqFVSILGPSGCGKSTILSMI 52
Cdd:cd03278 10 KSFAD-----KTTIPFPPG-LTAIVGPNGSGKSNIIDAI 42
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
31-53 |
1.80e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 38.69 E-value: 1.80e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-217 |
2.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 119 FLQQVGLAHAASRRP-ARLSGGMQQRVGLARAFAVDPE--ILLLDEP-FGALDALTRRELQL--QLRNvwEANrrTVIMV 192
Cdd:PRK00635 459 ILIDLGLPYLTPERAlATLSGGEQERTALAKHLGAELIgiTYILDEPsIGLHPQDTHKLINVikKLRD--QGN--TVLLV 534
|
90 100
....*....|....*....|....*
gi 1721987636 193 THDvDEAILLSDRILVMshGPRSTI 217
Cdd:PRK00635 535 EHD-EQMISLADRIIDI--GPGAGI 556
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-212 |
3.26e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.57 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGLAFPSTGEVFAAGHAVTAPG-----PDRGMVFQHHALLpwmtaKGNIEFGL 100
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlmdlrKVLGIIPQAPVLF-----SGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 101 ----KSARPQLSRA-ERSEIADQFLQQ-VGLAHAASRRPARLSGGMQQRVGLARAFAVDPEILLLDEPFGALDALTRREL 174
Cdd:PLN03130 1334 dpfnEHNDADLWESlERAHLKDVIRRNsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413
|
170 180 190
....*....|....*....|....*....|....*...
gi 1721987636 175 QLQLRNvwEANRRTVIMVTHDVDeAILLSDRILVMSHG 212
Cdd:PLN03130 1414 QKTIRE--EFKSCTMLIIAHRLN-TIIDCDRILVLDAG 1448
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
26-189 |
4.46e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 37.10 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 26 SVHIDEGQFVSILGPSGCGKSTILSMIAGlAFPSTGEVFAAGHAVtapgpdrgmvfQHHALLPWMTAkgnieFGLKSARP 105
Cdd:pfam13191 18 RVRSGRPPSVLLTGEAGTGKTTLLRELLR-ALERDGGYFLRGKCD-----------ENLPYSPLLEA-----LTREGLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721987636 106 QLSRAERSEIADQFLQQVGLAHAASRR-----PARLSGGMQQRVGLARAFAvDPEILLLDEpFGALDALTRRELQLQLRN 180
Cdd:pfam13191 81 QLLDELESSLLEAWRAALLEALAPVPElpgdlAERLLDLLLRLLDLLARGE-RPLVLVLDD-LQWADEASLQLLAALLRL 158
|
....*....
gi 1721987636 181 VWEANRRTV 189
Cdd:pfam13191 159 LESLPLLVV 167
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
34-64 |
6.73e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 36.32 E-value: 6.73e-03
10 20 30
....*....|....*....|....*....|....
gi 1721987636 34 FVSILGPSGCGKSTILSMIA---GLAFPSTGEVF 64
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAeklGLKHVSAGEIF 35
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
35-62 |
6.91e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 35.93 E-value: 6.91e-03
10 20 30
....*....|....*....|....*....|.
gi 1721987636 35 VSILGPSGCGKSTILSMIA---GLAFPSTGE 62
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLAkklGLPYLDTGG 32
|
|
| |
