|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-274 |
1.10e-122 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 350.54 E-value: 1.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 18 AAATPAIEVLSAEKIY---SNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmLWRRDSREKAQH 94
Cdd:COG1116 2 SAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV-LVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 PLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLL 174
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 175 LMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAARPGRVVEDIPIREPFPRSEAFRVSPT 254
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTSPE 240
|
250 260
....*....|....*....|
gi 488997434 255 FSLYARQLQDSLLQASQSGM 274
Cdd:COG1116 241 FAALRAEILDLLREEAERAA 260
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-239 |
2.28e-101 |
|
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: 294.76 E-value: 2.28e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNG---TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwRRDSREKAQHP--LSF 98
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV---LVDGEPVTGPGpdRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDE 178
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488997434 179 PFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAARPGRVVEDIPI 239
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEV 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
37-245 |
3.82e-78 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 237.45 E-value: 3.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrDSREkAQHPLS---FVFQEATLMPWSSVRN 113
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL---DGVP-VTGPGAdrgVVFQKDALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 114 NVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDS 193
Cdd:COG4525 96 NVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 194 DLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAARPGRVVEDIPIrePFPR 245
Cdd:COG4525 176 LLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLEL--DFSR 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-234 |
2.30e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 230.76 E-value: 2.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 20 ATPAIEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-SREKAQH-PLS 97
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvTGLPPEKrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 98 FVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 178 EPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVV 234
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRIE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
24-235 |
7.07e-73 |
|
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: 222.39 E-value: 7.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD--SREKAQHPLSFVFQ 101
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 102 EATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFG 181
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488997434 182 ALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM--NEGRIVQ 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
43-245 |
1.47e-69 |
|
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: 214.64 E-value: 1.47e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPLsFVFQEATLMPWSSVRNNVRLPLD-- 120
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-VVFQNYSLLPWLTVRENIALAVDrv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 121 LAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQ 200
Cdd:TIGR01184 83 LPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488997434 201 EQNLTVVFVTHSIHEAVFLSQRVIMMAARPGRVVEDIpIREPFPR 245
Cdd:TIGR01184 163 EHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI-LEVPFPR 206
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
31-234 |
1.89e-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: 214.18 E-value: 1.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEATLM 106
Cdd:COG1125 9 KRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELrrriGYVIQQIGLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGL--GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:COG1125 89 PHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 185 EITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVV 234
Cdd:COG1125 169 PITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRIV 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
21-238 |
2.11e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 208.74 E-value: 2.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 21 TPAIEVLSAEKIYSNG---TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSREKA 92
Cdd:COG1136 2 SPLLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 93 Q---HPLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVT 169
Cdd:COG1136 82 RlrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 170 RPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSiHEAVFLSQRVIMMaaRPGRVVEDIP 238
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL--RDGRIVSDER 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-235 |
5.99e-65 |
|
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: 203.30 E-value: 5.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSRE----KAQHPLSFV 99
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpvELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGL--GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 178 EPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN--GEIVQ 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
23-234 |
1.53e-64 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 205.69 E-value: 1.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----------WRRDsreka 92
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtdlppKDRN----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 93 qhpLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPK 172
Cdd:COG3839 77 ---IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997434 173 LLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVV 234
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRIQ 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-226 |
4.72e-63 |
|
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: 197.84 E-value: 4.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQH--PLSFVFQ 101
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 102 EATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFG 181
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488997434 182 ALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM 204
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
43-237 |
2.20e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 201.10 E-value: 2.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW--------RRDSREKAQHPLSFVFQEATLMPWSSVRNN 114
Cdd:COG4175 46 ASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDgeditklsKKELRELRRKKMSMVFQHFALLPHRTVLEN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 VRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSD 194
Cdd:COG4175 126 VAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDE 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488997434 195 LLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVV-----EDI 237
Cdd:COG4175 206 LLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRIVqigtpEEI 251
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
43-235 |
2.36e-62 |
|
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: 197.48 E-value: 2.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM--------LWRRDSREKAQHPLSFVFQEATLMPWSSVRNN 114
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaaMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 VRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSD 194
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488997434 195 LLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLVQ 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-241 |
1.46e-61 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 198.63 E-value: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 17 PAAATPAIEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-SREKAQH- 94
Cdd:PRK09452 8 PSSLSPLVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDiTHVPAENr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 PLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLL 174
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 175 LMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIRE 241
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIEQDGTPRE 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-226 |
1.59e-61 |
|
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: 193.48 E-value: 1.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNG---TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKL---------MLWRRDSREK 91
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdiskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 92 AQHpLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRP 171
Cdd:cd03255 81 RRH-IGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 172 KLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSiHEAVFLSQRVIMM 226
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIEL 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
24-235 |
3.50e-61 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 196.91 E-value: 3.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNgTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD--SREKAQH-PLSFVF 100
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlfTNLPPRErRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 101 QEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPF 180
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 181 GALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRIEQ 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
27-239 |
5.21e-61 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 193.38 E-value: 5.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 27 LSAEKIYSN--GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-WRRDSREKAQHplSFVFQEA 103
Cdd:PRK11248 2 LQISHLYADygGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAER--GVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 104 TLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 184 DEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAARPGRVVEDIPI 239
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPL 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
24-241 |
8.01e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 187.19 E-value: 8.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW----RRDSREKAQHpLSFV 99
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvARDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997434 180 FGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:COG1131 159 TSGLDPEARREL-WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDK--GRIVADGTPDE 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-241 |
3.87e-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: 190.88 E-value: 3.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 17 PAAATPAIEVLSAEKIY----SNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WR 85
Cdd:COG1123 254 AAAAEPLLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdgkdltkLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 86 RDSREKAQHPLSFVFQ--EATLMPWSSVRNNVRLPLDLAGV-PRAEGNTRVSEVLELVGLG-KFADVLPRELSGGMQMRV 161
Cdd:COG1123 334 RRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 162 SIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRIVEDGPTEE 491
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
24-236 |
9.31e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 181.40 E-value: 9.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML---------------WRRDs 88
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlkrreipyLRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 89 rekaqhpLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLV 168
Cdd:COG2884 81 -------IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 169 TRPKLLLMDEPFGALDEITRNkldsDLLRLWQEQNL---TVVFVTHSIHeavFLSQ---RVIMMAArpGRVVED 236
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSW----EIMELLEEINRrgtTVLIATHDLE---LVDRmpkRVLELED--GRLVRD 218
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
43-235 |
7.16e-56 |
|
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: 184.21 E-value: 7.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGL---------VEPSDGKLMLWRRDS---REKAQHPLSFVFQEATLMPWSS 110
Cdd:TIGR03415 43 ASLDIEEGEICVLMGLSGSGKSTLLRAVNGLnpvsrgsvlVKDGDGSVDVANCDAatlRRLRTHRVSMVFQQFALLPWRT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:TIGR03415 123 VEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQ 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488997434 191 LDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:TIGR03415 203 LQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEG--GRIIQ 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
31-235 |
1.68e-55 |
|
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: 177.83 E-value: 1.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNGTrALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD--SREKAQHPLSFVFQEATLMPW 108
Cdd:cd03301 8 KRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtDLPPKDRDIAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITR 188
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488997434 189 NKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND--GQIQQ 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
43-241 |
1.84e-55 |
|
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: 178.63 E-value: 1.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSREKAQHPLSF--VFQEATLmpWSS--VRN 113
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqdITGLSEKELYELRRRIgmLFQGGAL--FDSltVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 114 NVRLPLD-LAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLD 192
Cdd:COG1127 102 NVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488997434 193 SDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:COG1127 182 ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD--GKIIAEGTPEE 228
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
43-247 |
9.40e-53 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 175.26 E-value: 9.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrDSREKAQHP-----LSFVFQEATLMPWSSVRNNVRL 117
Cdd:NF040840 19 ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYL---DGKDITNLPpekrgIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 118 PLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLR 197
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 198 LWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPF--PRSE 247
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIM--LNGRLSQVGDVREVFrrPKNE 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-228 |
9.62e-53 |
|
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: 169.68 E-value: 9.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS------DGKLMLWRRDSREKAQHPLS 97
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDsgsiliDGEDLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 98 FVFQEATLMPWSSVRNNVRLPLdlagvpraegntrvsevlelvglgkfadvlprelSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 178 EPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAA 228
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-226 |
1.24e-52 |
|
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: 171.37 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-SREKAQ-HPLSFVF 100
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDaTDVPVQeRNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 101 QEATLMPWSSVRNNVRLPLDL----AGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVM 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
55-236 |
3.30e-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: 173.06 E-value: 3.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 55 LLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQH--PLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTR 132
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHlrHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 133 VSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHS 212
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....
gi 488997434 213 IHEAVFLSQRVIMMaaRPGRVVED 236
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIAQI 182
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-247 |
5.97e-52 |
|
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: 169.68 E-value: 5.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTR---ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGK-------LMLWRRDSREKAQ 93
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 94 HPLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKL 173
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 174 LLMDEPFGALD-EITRNKLdsDLLR-LWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFPRSE 247
Cdd:cd03258 162 LLCDEATSALDpETTQSIL--ALLRdINRELGLTIVLITHEMEVVKRICDRVAVMEK--GEVVEEGTVEEVFANPQ 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
33-250 |
9.27e-52 |
|
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: 169.05 E-value: 9.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSREKAQHpLSFVFQEAT--- 104
Cdd:COG1122 10 YPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkdITKKNLRELRRK-VGLVFQNPDdql 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPwsSVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:COG1122 89 FAP--TVEEDVAFgPENL-GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 184 DEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFPRSEAFR 250
Cdd:COG1122 166 DPRGRREL-LELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD--GRIVADGTPREVFSDYELLE 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
36-246 |
1.34e-51 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 169.47 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmLWRRDSREKAQHPLSFVFQEATLMPWSSVRNN 114
Cdd:PRK11247 23 GERTVLnQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMFQDARLLPWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 VRLPLDLAGVPRAEgntrvsEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSD 194
Cdd:PRK11247 102 VGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 195 LLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPFPRS 246
Cdd:PRK11247 176 IESLWQQHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDLPRPRR 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
24-248 |
5.66e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 170.26 E-value: 5.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTR---ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSRE--KAQ 93
Cdd:COG1135 2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdLTALSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 94 HPLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKL 173
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 174 LLMDEPFGALD-EITRNKLdsDLL-RLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF--PRSEA 248
Cdd:COG1135 162 LLCDEATSALDpETTRSIL--DLLkDINRELGLTIVLITHEMDVVRRICDRVAVLEN--GRIVEQGPVLDVFanPQSEL 236
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-265 |
5.93e-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: 167.29 E-value: 5.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNGTR---ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML--------WRRDSREK 91
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 92 AQhplsFVFQ--EATLMPWSSVRNNVRLPLDLAGVPRAEgnTRVSEVLELVGLGK-FADVLPRELSGGMQMRVSIARGLV 168
Cdd:COG1124 81 VQ----MVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 169 TRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF--PRS 246
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTVADLLagPKH 232
|
250
....*....|....*....
gi 488997434 247 EafrvsptfslYARQLQDS 265
Cdd:COG1124 233 P----------YTRELLAA 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-226 |
9.45e-51 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 170.79 E-value: 9.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 19 AATPAIEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKA--QHPL 96
Cdd:PRK11607 15 ALTPLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPpyQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 SFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
33-226 |
1.71e-50 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 164.95 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPLS----FVFQEA---T 104
Cdd:cd03225 9 YPDGARPALdDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkvgLVFQNPddqF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPwsSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:cd03225 89 FGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488997434 185 EITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:cd03225 167 PAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
27-226 |
5.39e-50 |
|
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: 168.29 E-value: 5.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 27 LSAEKI--YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-SREK-AQHPLSFVFQE 102
Cdd:TIGR03265 5 LSIDNIrkRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDiTRLPpQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 103 ATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488997434 183 LDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
43-241 |
6.08e-50 |
|
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: 164.21 E-value: 6.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----WRRDSREKAQH---PLSFVFQEATLMPWSSVRNNV 115
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedISGLSEAELYRlrrRMGMLFQSGALFDSLTVFENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 RLPL----DLagvPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL 191
Cdd:cd03261 99 AFPLrehtRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 192 DSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAarPGRVVEDIPIRE 241
Cdd:cd03261 176 DDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLY--DGKIVAEGTPEE 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
22-241 |
8.41e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 164.46 E-value: 8.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 22 PAIEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSRE--KAQH 94
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVdgqdvTALRGRAlrRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 PLSFVFQEATLMPWSSVRNNV------RLPL--DLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARG 166
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlgRTSTwrSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 167 LVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD--GRVVFDGPPAE 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
44-250 |
1.66e-49 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 163.00 E-value: 1.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 44 NLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD--SREKAQHPLSFVFQEATLMPWSSVRNNVRLPLDL 121
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDltALPPAERPVSMLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 122 AGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLdSDLLR-LWQ 200
Cdd:COG3840 99 GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM-LDLVDeLCR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 201 EQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF--PRSEAFR 250
Cdd:COG3840 178 ERGLTVLMVTHDPEDAARIADRVLLVAD--GRIAADGPTAALLdgEPPPALA 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-236 |
2.84e-49 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 162.29 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNG---TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDSREKAQ 93
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 94 HPLSFVFQEA--TLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLG---KFADVLPRELSGGMQMRVSIARGLV 168
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 169 TRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVED 236
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKIVEE 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-236 |
2.90e-49 |
|
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: 162.60 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 17 PAAATPAIEVLSAEKIYSNGTRAL--L-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD------ 87
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELtiLkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 88 ---SREKAQHpLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGntRVSEVLELVGLGKFADVLPRELSGGMQMRVSIA 164
Cdd:COG4181 82 darARLRARH-VGFVFQSFQLLPTLTALENVMLPLELAGRRDARA--RARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 165 RGLVTRPKLLLMDEPFGALDEITRNKLdSDLL-RLWQEQNLTVVFVTHSIHEAVfLSQRVIMMAArpGRVVED 236
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQI-IDLLfELNRERGTTLVLVTHDPALAA-RCDRVLRLRA--GRLVED 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-247 |
2.99e-49 |
|
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: 162.50 E-value: 2.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNgtRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD----SREKaqHPLSFV 99
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnlPPEK--RDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 180 FGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPF--PRSE 247
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQVGKPEEVFkkPKNE 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
43-226 |
4.41e-49 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 165.66 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKA--QHPLSFVFQEATLMPWSSVRNNVRLPLD 120
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqQRDICMVFQSYALFPHMSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 121 LAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQ 200
Cdd:PRK11432 105 MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQ 184
|
170 180
....*....|....*....|....*.
gi 488997434 201 EQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK11432 185 QFNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
24-236 |
4.11e-48 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 160.02 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSRE---KAQHPLSFVF 100
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKeprEARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 101 QEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPF 180
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 181 GALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVED 236
Cdd:COG4555 161 NGLDVMARRLL-REILRALKKEGKTVLFSSHIMQEVEALCDRVVILHK--GKVVAQ 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
31-226 |
6.30e-47 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 160.01 E-value: 6.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR--DSREKAQHPLSFVFQEATLMPW 108
Cdd:PRK11650 11 KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvNELEPADRDIAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITR 188
Cdd:PRK11650 91 MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 488997434 189 NKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK11650 171 VQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
41-234 |
1.66e-46 |
|
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: 154.76 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 41 LPVNLTINqGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR---DSREKAQHP-----LSFVFQEATLMPWSSVR 112
Cdd:cd03297 15 LKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKINLPpqqrkIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNvrLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLD 192
Cdd:cd03297 94 EN--LAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488997434 193 SDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVV 234
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM--EDGRLQ 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
24-241 |
2.80e-46 |
|
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: 155.03 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDSREKAQHPL 96
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 SFVFQEATLMPWSSVRNNV------RLPL--DLAG-VPRAEGNtRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGL 167
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTwrSLFGlFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 168 VTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRIVFDGPPAE 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
32-241 |
1.00e-45 |
|
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: 153.49 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 32 IYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVE-----PSDGKLMLWRRDSREKAQHPLS------FVF 100
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLElrrrvgMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 101 QEATLMPwSSVRNNVRLPLDLAGV-PRAEGNTRVSEVLELVGL-GKFADVL-PRELSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:cd03260 88 QKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 178 EPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:cd03260 167 EPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLN--GRLVEFGPTEQ 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-243 |
3.26e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.55 E-value: 3.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 19 AATPAIEV--LSAEkiYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHpL 96
Cdd:COG1121 2 MMMPAIELenLTVS--Y-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 SFVFQEATLmPWS---SVRNNVRLPLD----LAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVT 169
Cdd:COG1121 78 GYVPQRAEV-DWDfpiTVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 170 RPKLLLMDEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAarpGRVVEDIPIREPF 243
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEAL-YELLRELRREGKTILVVTHDLGAVREYFDRVLLLN---RGLVAHGPPEEVL 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
26-234 |
1.11e-44 |
|
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: 151.35 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 26 VLSAEKI-YSNGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSREKAQHpLSF 98
Cdd:COG1120 1 MLEAENLsVGYGGRPVLdDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQEATLMPWSSVRNNV---RLP-LDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLL 174
Cdd:COG1120 80 VPQEPPAPFGLTVRELValgRYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997434 175 LMDEPFGALDeItRNKLDS-DLLR-LWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVV 234
Cdd:COG1120 160 LLDEPTSHLD-L-AHQLEVlELLRrLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRIV 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-271 |
1.24e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 153.80 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTR---ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSRE--KAQ 93
Cdd:PRK11153 2 IELKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgqdLTALSEKElrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 94 HPLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKL 173
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 174 LLMDEPFGALD-EITRNKLdsDLLR-LWQEQNLTVVFVTHSIheAVF--LSQRVIMMAArpGRVVEDIPIREPF--PRSE 247
Cdd:PRK11153 162 LLCDEATSALDpATTRSIL--ELLKdINRELGLTIVLITHEM--DVVkrICDRVAVIDA--GRLVEQGTVSEVFshPKHP 235
|
250 260 270
....*....|....*....|....*....|.
gi 488997434 248 AFR--VSPTFSL-----YARQLQDSLLQASQ 271
Cdd:PRK11153 236 LTRefIQSTLHLdlpedYLARLQAEPTTGSG 266
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
21-254 |
1.37e-44 |
|
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: 157.37 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 21 TPAIEVLSAEKIYSNGTR-ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS---DGKLMLWRRDSREKAQHPL 96
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 ----SFVFQEAT--LMPwSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTR 170
Cdd:COG1123 82 grriGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 171 PKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPFPRSEAFR 250
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVEDGPPEEILAAPQALA 238
|
....
gi 488997434 251 VSPT 254
Cdd:COG1123 239 AVPR 242
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-233 |
2.36e-44 |
|
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: 149.48 E-value: 2.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDSREKAQHPL 96
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVngqdvsdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 SFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 177 DEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVImmAARPGRV 233
Cdd:cd03292 161 DEPTGNLDPDTTWEI-MNLLKKINKAGTTVVVATHAKELVDTTRHRVI--ALERGKL 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
40-180 |
2.70e-44 |
|
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: 147.02 E-value: 2.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 40 LLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----WRRDSREKAQHPLSFVFQEATLMPWSSVRNNV 115
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 116 RLPLDLAGVPRAEGNTRVSEVLELVGLGKFAD----VLPRELSGGMQMRVSIARGLVTRPKLLLMDEPF 180
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
41-234 |
6.09e-44 |
|
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: 152.56 E-value: 6.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 41 LPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----WRrDSREK-----AQHPLSFVFQEATLMPWSSV 111
Cdd:COG4148 16 LDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevLQ-DSARGiflppHRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 RNNVRLPLDLAgvPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL 191
Cdd:COG4148 95 RGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488997434 192 DSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVV 234
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ--GRVV 213
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
40-211 |
9.47e-44 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 147.86 E-value: 9.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 40 LLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW-------RRDSREKAQHPLSFVFQEATLMPWSSVR 112
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLgqelhgaSKKQLVQLRRRIGYIFQAHNLLGFLTAR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNVRLPLDL-AGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL 191
Cdd:TIGR02982 101 QNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDV 180
|
170 180
....*....|....*....|
gi 488997434 192 DSDLLRLWQEQNLTVVFVTH 211
Cdd:TIGR02982 181 VELMQKLAKEQGCTILMVTH 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
31-234 |
1.23e-43 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 147.65 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNGTR-ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD---SREKAQHPLSFVFQEATLM 106
Cdd:cd03263 8 KTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEI 186
Cdd:cd03263 88 DELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488997434 187 TRNKLDSDLLRLwqEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVV 234
Cdd:cd03263 168 SRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSD--GKLR 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
43-247 |
1.33e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.22 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS------DGKLMLWRRDSREKAQHPLSFVFQEATLMPWSSVRNNVR 116
Cdd:COG1126 20 ISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsgtitvDGEDLTDSKKDINKLRRKVGMVFQQFNLFPHLTVLENVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 117 L-PLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD-EITRNKLdsD 194
Cdd:COG1126 100 LaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpELVGEVL--D 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 195 LLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF--PRSE 247
Cdd:COG1126 178 VMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDG--GRIVEEGPPEEFFenPQHE 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
27-228 |
2.36e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 27 LSAEKI-YSNGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML------------WRRDsreka 92
Cdd:COG4619 1 LELEGLsFRVGGKPILsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdgkplsampppeWRRQ----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 93 qhpLSFVFQEATLMPwSSVRNNVRLPLDLAGVPRAEgnTRVSEVLELVGLGkfADVL---PRELSGGMQMRVSIARGLVT 169
Cdd:COG4619 76 ---VAYVPQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLP--PDILdkpVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 170 RPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAA 228
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-226 |
2.87e-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: 146.75 E-value: 2.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW----RRDSREkAQHPLSFV 99
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvVREPRE-VRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488997434 180 FGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-269 |
8.46e-43 |
|
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: 149.49 E-value: 8.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 41 LPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR---DSREKAQHP-----LSFVFQEATLMPWSSVR 112
Cdd:TIGR02142 14 LDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPpekrrIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNVRLpldlaGVPRAEG---NTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRN 189
Cdd:TIGR02142 94 GNLRY-----GMKRARPserRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 190 KLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIrepfprsEAFRVSPTFSLYARQLQDSLLQA 269
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVAAAGPI-------AEVWASPDLPWLAREDQGSLIEG 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-226 |
1.08e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 149.08 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNgTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-SREKAQ-HPLSFVF 100
Cdd:PRK10851 2 SIEIANIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDvSRLHARdRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 101 QEATLMPWSSVRNNVRLPLDLagVPR------AEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLL 174
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTV--LPRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 175 LMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
43-233 |
1.81e-42 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 149.02 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML--WRRDSREKAQHPLSFVFQEATLMPWSSVRNNVRLPLD 120
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgeKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 121 LAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQ 200
Cdd:PRK11000 102 LAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHK 181
|
170 180 190
....*....|....*....|....*....|...
gi 488997434 201 EQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRV 233
Cdd:PRK11000 182 RLGRTMIYVTHDQVEAMTLADKIVVLDA--GRV 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
43-227 |
1.95e-41 |
|
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: 141.90 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDG-------KLMLWRRDSREKAQHpLSFVFQEATLMPWSSVRNNV 115
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKNINELRQK-VGMVFQQFNLFPHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 RL-PLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD-EITRNKLDS 193
Cdd:cd03262 98 TLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpELVGEVLDV 177
|
170 180 190
....*....|....*....|....*....|....
gi 488997434 194 dLLRLWQEqNLTVVFVTHSIHEAVFLSQRVIMMA 227
Cdd:cd03262 178 -MKDLAEE-GMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
35-230 |
2.19e-41 |
|
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: 141.52 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSrEKAQHPLSFVFQEATLmPWS---SV 111
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-EKERKRIGYVPQRRSI-DRDfpiSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 RNNVRLPLD----LAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEIT 187
Cdd:cd03235 88 RDVVLMGLYghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488997434 188 RNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAARP 230
Cdd:cd03235 168 QEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
24-233 |
4.19e-41 |
|
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: 139.46 E-value: 4.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRdsREKAQHPLSF 98
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdiKKE--PEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQEATLMPWSSVRNNVRLpldlagvpraegntrvsevlelvglgkfadvlprelSGGMQMRVSIARGLVTRPKLLLMDE 178
Cdd:cd03230 78 LPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 179 PFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRV 233
Cdd:cd03230 122 PTSGLDPESRREF-WELLRELKKEGKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-247 |
7.58e-41 |
|
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: 142.21 E-value: 7.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 32 IYSNGT----RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD---SREKAQHPL----SFVF 100
Cdd:TIGR04521 9 IYQPGTpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDitaKKKKKLKDLrkkvGLVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 101 Q-------EATlmpwssVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLG-KFADVLPRELSGGMQMRVSIARGLVTRP 171
Cdd:TIGR04521 89 QfpehqlfEET------VYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 172 KLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFPRSE 247
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK--GKIVLDGTPREVFSDVD 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
36-211 |
3.58e-40 |
|
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: 138.38 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmLWR----RDSREKAQHPLSFVFQEATLMPWSS 110
Cdd:COG4133 13 GERLLFsGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV-LWNgepiRDAREDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDLAGVPRAEgnTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:COG4133 92 VRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180
....*....|....*....|.
gi 488997434 191 LdSDLLRLWQEQNLTVVFVTH 211
Cdd:COG4133 170 L-AELIAAHLARGGAVLLTTH 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
45-236 |
4.30e-40 |
|
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: 138.39 E-value: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 45 LTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD--SREKAQHPLSFVFQEATLMPWSSVRNNVRLPLDLA 122
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvtAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 123 GVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQ 202
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178
|
170 180 190
....*....|....*....|....*....|....
gi 488997434 203 NLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVED 236
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDN--GRIAAQ 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-235 |
5.08e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 136.30 E-value: 5.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNgTRALLPVNLTINQGEFITLLGPSGCGKSTLLKmVAGLVE-PSDGKLML------WRRDSREKAQHP 95
Cdd:PRK11124 2 SIQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIagnhfdFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 96 L----SFVFQEATLMPWSSVRNN-VRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTR 170
Cdd:PRK11124 80 LrrnvGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 171 PKLLLMDEPFGALD-EITRNKLdsDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:PRK11124 160 PQVLLFDEPTAALDpEITAQIV--SIIRELAETGITQVIVTHEVEVARKTASRVVYM--ENGHIVE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
35-234 |
1.22e-38 |
|
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: 133.33 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSREKAQHpLSFVFQeatlmpws 109
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdgkdlASLSPKELARK-IAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 svrnnvrlpldlagvpraegntrvseVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRN 189
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488997434 190 KLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVV 234
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD--GRIV 177
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
31-238 |
2.58e-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: 136.37 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-SREKAQ--HPLSFVFQEATLMP 107
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDvVREPRKvrRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 WSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEIT 187
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 188 RNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVV-EDIP 238
Cdd:TIGR01188 160 RRAI-WDYIRALKEEGVTILLTTHYMEEADKLCDRIAII--DHGRIIaEGTP 208
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
31-225 |
3.46e-38 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 133.63 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNG---TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQ---HPLSFV 99
Cdd:TIGR02211 9 KRYQEGkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSlsklsSNERAKlrnKKLGFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:TIGR02211 89 YQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488997434 180 FGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIM 225
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEM 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
37-249 |
4.24e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 134.06 E-value: 4.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDSREKAQHPlSFVFQEATLMPWS 109
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdglkvndPKVDERLIRQEA-GMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNNVRL-PLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEitr 188
Cdd:PRK09493 93 TALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP--- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 189 nKLDSDLLRLWQ---EQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE-----PFPRSEAF 249
Cdd:PRK09493 170 -ELRHEVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRIAEDGDPQVliknpPSQRLQEF 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
36-234 |
6.99e-38 |
|
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: 133.33 E-value: 6.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSREKAQHPLSFVFQEATLMPWSS 110
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdgediTGLPPHEIARLGIGRTFQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRL--------PLDLAGVPRAEG--NTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPF 180
Cdd:cd03219 92 VLENVMVaaqartgsGLLLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 181 GALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIhEAVF-LSQRVIMMAArpGRVV 234
Cdd:cd03219 172 AGLNPEETEEL-AELIRELRERGITVLLVEHDM-DVVMsLADRVTVLDQ--GRVI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
35-226 |
7.38e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.83 E-value: 7.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----WRRDSREKAQHPLSFVFQeatlmpwss 110
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIdgkdIAKLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 vrnnvrlpldlagvpraegntrvsevlelvglgkfadvlpreLSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:cd00267 81 ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*.
gi 488997434 191 LdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:cd00267 119 L-LELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
44-227 |
7.52e-38 |
|
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: 132.68 E-value: 7.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 44 NLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKA--QHPLSFVFQEATLMPWSSVRNNVRLPLDL 121
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLApyQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 122 AGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQE 201
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180
....*....|....*....|....*.
gi 488997434 202 QNLTVVFVTHSIHEAVFLSQRVIMMA 227
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-236 |
1.32e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 132.40 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 44 NLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREK--AQHPLSFVFQEATLMPWSSVRNNVRLPLDL 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 122 AGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQE 201
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190
....*....|....*....|....*....|....*
gi 488997434 202 QNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVED 236
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVAD--GRIAWD 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-236 |
1.36e-37 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 132.11 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTR---ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-SREK--AQHPLS 97
Cdd:cd03266 2 ITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDvVKEPaeARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 98 FVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 178 EPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVED 236
Cdd:cd03266 162 EPTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR--GRVVYE 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
33-262 |
2.51e-37 |
|
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: 139.58 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML------------WRRDsrekaqhpLSFV 99
Cdd:COG2274 483 YPGDSPPVLdNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidpasLRRQ--------IGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPwSSVRNNVRLpldlaGVPRAEgNTRVSEVLELVGLGKFADVLP-----------RELSGGMQMRVSIARGLV 168
Cdd:COG2274 555 LQDVFLFS-GTIRENITL-----GDPDAT-DEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 169 TRPKLLLMDEPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTHSiHEAVFLSQRVIMMAArpGRVVEDIPIREPFPRSEA 248
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVLDK--GRIVEDGTHEELLARKGL 702
|
250
....*....|....
gi 488997434 249 FrvsptFSLYARQL 262
Cdd:COG2274 703 Y-----AELVQQQL 711
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
43-241 |
2.65e-37 |
|
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: 134.03 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS---------DGK--LMLWRRDSREKAQHPLSFVFQE--ATLMPWS 109
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitsgeilfDGEdlLKLSEKELRKIRGREIQMIFQDpmTSLNPVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNNVRLPLDL-AGVPRAEGNTRVSEVLELVGL---GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDE 185
Cdd:COG0444 104 TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 186 ITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:COG0444 184 TIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYA--GRIVEEGPVEE 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
32-229 |
9.83e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 129.52 E-value: 9.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 32 IYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEP---SDGKLMLWRRDSREKAQHP--LSFVFQEATLM 106
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQrrIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWSSVRNNvrLPLDL-AGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDE 185
Cdd:COG4136 89 PHLSVGEN--LAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488997434 186 ITRNKldsdlLRLW-----QEQNLTVVFVTHSiHEAVFLSQRVIMMAAR 229
Cdd:COG4136 167 ALRAQ-----FREFvfeqiRQRGIPALLVTHD-EEDAPAAGRVLDLGNW 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
44-235 |
6.54e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 132.08 E-value: 6.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 44 NLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDS--------REKAQHPLSFVFQEATLMPWSSVRNNV 115
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisdaelREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 RLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDL 195
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488997434 196 LRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIM--QNGEVVQ 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-235 |
6.88e-36 |
|
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: 134.50 E-value: 6.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 4 APKLTVMSDTRFIPAAATPAIEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML 83
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 84 ----WRRDSREKAQHPLSFVFQEATLMPWsSVRNNVRLpldlaGVPRAeGNTRVSEVLELVGLGKFADVLP--------- 150
Cdd:COG4988 397 ngvdLSDLDPASWRRQIAWVPQNPYLFAG-TIRENLRL-----GRPDA-SDEELEAALEAAGLDEFVAALPdgldtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 151 --RELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQnlTVVFVTHSIHEAVFlSQRVIMMAA 228
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDD 546
|
....*..
gi 488997434 229 rpGRVVE 235
Cdd:COG4988 547 --GRIVE 551
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-235 |
2.93e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.67 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNgTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML------WRRDSREKAQHPL 96
Cdd:COG4161 2 SIQLKNINCFYGS-HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 ----SFVFQEATLMPWSSVRNN-VRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRP 171
Cdd:COG4161 81 rqkvGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 172 KLLLMDEPFGALD-EITRNKLdsDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:COG4161 161 QVLLFDEPTAALDpEITAQVV--EIIRELSQTGITQVIVTHEVEFARKVASQVVYM--EKGRIIE 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
35-269 |
7.10e-35 |
|
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: 126.46 E-value: 7.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPV----NLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMlWR--------RDSREKAQHPLSFVFQE 102
Cdd:TIGR02769 18 FGAKQRAPVltnvSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS-FRgqdlyqldRKQRRAFRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 103 A--TLMPWSSVRNNVRLPL-DLAGVPRAEGNTRVSEVLELVGL-GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDE 178
Cdd:TIGR02769 97 SpsAVNPRMTVRQIIGEPLrHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 179 PFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFPRSeafrvSPTfsly 258
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQIVEECDVAQLLSFK-----HPA---- 245
|
250
....*....|.
gi 488997434 259 ARQLQDSLLQA 269
Cdd:TIGR02769 246 GRNLQSAVLPE 256
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
38-236 |
7.62e-35 |
|
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: 125.52 E-value: 7.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSREKAQhpLSFVFQEATLMPWS-SV 111
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvpWKRRKKFLRR--IGVVFGQKTQLWWDlPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 RNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL 191
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488997434 192 DSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVED 236
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK--GRLLYD 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
33-226 |
1.23e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 122.88 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEATLMP 107
Cdd:cd03228 10 YPGRPKPVLkDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkniAYVPQDPFLFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 wSSVRNNVrlpldlagvpraegntrvsevlelvglgkfadvlpreLSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEIT 187
Cdd:cd03228 90 -GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 488997434 188 RNKLDSDLLRLwqEQNLTVVFVTHSIHeAVFLSQRVIMM 226
Cdd:cd03228 132 EALILEALRAL--AKGKTVIVIAHRLS-TIRDADRIIVL 167
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
36-234 |
1.90e-34 |
|
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: 124.77 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQHPLSFVFQEATLMPWSS 110
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitglpPHRIARLGIARTFQNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLP-------------LDLAGVPRAEG--NTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLL 175
Cdd:COG0411 96 VLENVLVAaharlgrgllaalLRLPRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 176 MDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHeAVF-LSQRVIMMAArpGRVV 234
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD-LVMgLADRIVVLDF--GRVI 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-249 |
2.92e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.48 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------------WRRDSR 89
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 90 EKAQHpLSFVFQEATLMPWSSVRNNV-RLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLV 168
Cdd:PRK11264 82 QLRQH-VGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 169 TRPKLLLMDEPFGALD-EITRNKLDSdlLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF---- 243
Cdd:PRK11264 161 MRPEVILFDEPTSALDpELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ--GRIVEQGPAKALFadpq 236
|
....*..
gi 488997434 244 -PRSEAF 249
Cdd:PRK11264 237 qPRTRQF 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-243 |
3.03e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.16 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGT----RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM----------LWRRDSR 89
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvditdkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 90 EKA----QHPLSFVFQEatlmpwsSVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLG--KFADVLPRELSGGMQMRVS 162
Cdd:PRK13637 83 KKVglvfQYPEYQLFEE-------TIEKDIAFgPINL-GLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 163 IARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREP 242
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM--NKGKCELQGTPREV 232
|
.
gi 488997434 243 F 243
Cdd:PRK13637 233 F 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
31-225 |
5.63e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 123.00 E-value: 5.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNG---TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSREKAQ---HPLSFV 99
Cdd:PRK11629 13 KRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpMSKLSSAAKAElrnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488997434 180 FGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIM 225
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-222 |
8.88e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 122.29 E-value: 8.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-SREKA------QHPLSFVFQEA 103
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDiTRLKNrevpflRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 104 TLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 488997434 184 DEitrnKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQR 222
Cdd:PRK10908 169 DD----ALSEGILRLFEEFNRVGVTVLMATHDIGLISRR 203
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
40-211 |
9.84e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 122.19 E-value: 9.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 40 LLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW-----RRDSREKAQ---HPLSFVFQEATLMPWSSV 111
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVgqplhQMDEEARAKlraKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 RNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL 191
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|
gi 488997434 192 DSDLLRLWQEQNLTVVFVTH 211
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTH 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
30-241 |
1.15e-33 |
|
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: 122.27 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 30 EKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQHPLSFVFQEAT 104
Cdd:cd03218 7 SKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpMHKRARLGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 185 EITRNKLDSDLLRLwQEQNLTVVFVTHSIHEAVFLSQRV-------IMMAARPGRVVEDIPIRE 241
Cdd:cd03218 166 PIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAyiiyegkVLAEGTPEEIAANELVRK 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
17-235 |
1.96e-33 |
|
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: 127.57 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 17 PAAATPAIEVLSAEKIYSNGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDS 88
Cdd:COG4987 327 PAPGGPSLELEDVSFRYPGAGRPVLdGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 89 REKAqhpLSFVFQEATLMPwSSVRNNVRLpldlaGVPRAeGNTRVSEVLELVGLGKFADVLP-----------RELSGGM 157
Cdd:COG4987 407 LRRR---IAVVPQRPHLFD-TTLRENLRL-----ARPDA-TDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 158 QMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQnlTVVFVTH--SIHEAVflsQRVIMMAArpGRVVE 235
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHrlAGLERM---DRILVLED--GRIVE 549
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
43-269 |
2.68e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 122.10 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMlWR--------RDSREKAQHPLSFVFQEA--TLMPWSSVR 112
Cdd:PRK10419 31 VSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVS-WRgeplaklnRAQRKAFRRDIQMVFQDSisAVNPRKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNVRLPL-DLAGVPRAEGNTRVSEVLELVGLG-KFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:PRK10419 110 EIIREPLrHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 191 LDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIrepfprSEAFRVSptfSLYARQLQDSLLQA 269
Cdd:PRK10419 190 VIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN--GQIVETQPV------GDKLTFS---SPAGRVLQNAVLPA 257
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
38-235 |
1.16e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 122.15 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----------WRRDSREKAQhplsFVFQE--AT 104
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdgqditglsgrELRPLRRRMQ----MVFQDpyAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPWSSVRNNVRLPLDLAGV-PRAEGNTRVSEVLELVGLGK-FADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:COG4608 108 LNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 183 LDEITR----NkLdsdLLRLWQEQNLTVVFVTHSIheAV--FLSQRVIMMAArpGRVVE 235
Cdd:COG4608 188 LDVSIQaqvlN-L---LEDLQDELGLTYLFISHDL--SVvrHISDRVAVMYL--GKIVE 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-250 |
1.72e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.51 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 25 EVLSAEKI---YSNGTR-ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----------WrrDSRE 90
Cdd:PRK13635 4 EIIRVEHIsfrYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvlseetvW--DVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 91 KaqhpLSFVFQE-------ATlmpwssVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSI 163
Cdd:PRK13635 82 Q----VGMVFQNpdnqfvgAT------VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 164 ARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFlSQRVIMMaaRPGRVVEDIPIREPF 243
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM--NKGEILEEGTPEEIF 228
|
....*..
gi 488997434 244 PRSEAFR 250
Cdd:PRK13635 229 KSGHMLQ 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-241 |
1.82e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.36 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 20 ATPAIEVLSAEKIYSnGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW-----RRDSREKAQH 94
Cdd:COG1129 1 AEPLLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvrFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 PLSFVFQEATLMPWSSVRNNV---RLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRP 171
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488997434 172 KLLLMDEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEaVF-LSQRVIMMaaRPGRVVEDIPIRE 241
Cdd:COG1129 160 RVLILDEPTASLTEREVERL-FRIIRRLKAQGVAIIYISHRLDE-VFeIADRVTVL--RDGRLVGTGPVAE 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-266 |
2.02e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.51 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR----DSREKAQHPL----SFVFQ--EATLM 106
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKPLrkkvGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWSSVRNNVRLPLDLaGVPRAEGNTRVSEVLELVGLGkfADVL---PRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK13634 100 EETVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLP--EELLarsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 184 DEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFPRSE---AFRVS-PTFSLYA 259
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHK--GTVFLQGTPREIFADPDeleAIGLDlPETVKFK 254
|
....*..
gi 488997434 260 RQLQDSL 266
Cdd:PRK13634 255 RALEEKF 261
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
26-187 |
4.76e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.21 E-value: 4.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 26 VLSAE---KIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----------WRRdsrekA 92
Cdd:COG1137 3 TLEAEnlvKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdgedithlpmHKR-----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 93 QHPLSFVFQEAT----LmpwsSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLV 168
Cdd:COG1137 77 RLGIGYLPQEASifrkL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170
....*....|....*....
gi 488997434 169 TRPKLLLMDEPFGALDEIT 187
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIA 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-236 |
8.43e-32 |
|
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: 116.91 E-value: 8.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNGtRALLPVNLTINQGeFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD---SREKAQHPLSFVFQEATLMP 107
Cdd:cd03264 8 KRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkQPQKLRRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 WSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEIT 187
Cdd:cd03264 86 NFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488997434 188 RNKLDSDLLRLwqEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVED 236
Cdd:cd03264 166 RIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNK--GKLVFE 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-234 |
9.86e-32 |
|
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: 116.61 E-value: 9.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNgTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPLSFVFQEA 103
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 104 TLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 184 DEITRnKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVV 234
Cdd:cd03269 160 DPVNV-ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLL--NKGRAV 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-227 |
1.48e-31 |
|
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: 115.82 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 28 SAEKI---YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKA---------QHP 95
Cdd:cd03226 1 RIENIsfsYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrksigyvmQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 96 LSFVFQEatlmpwsSVRNNVRLPLDLAGvpraEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLL 175
Cdd:cd03226 81 DYQLFTD-------SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 176 MDEPFGALDEItRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMA 227
Cdd:cd03226 150 FDEPTSGLDYK-NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-226 |
1.49e-31 |
|
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: 122.01 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 16 IPAAATPAIEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHP 95
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 96 L----SFVFQEATLMPwSSVRNNVRLPldLAGVPRAEgntrVSEVLELVGLGKFADVLP-----------RELSGGMQMR 160
Cdd:TIGR02857 394 WrdqiAWVPQHPFLFA-GTIAENIRLA--RPDASDAE----IREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 161 VSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTHSIHEAVfLSQRVIMM 226
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
35-241 |
3.65e-31 |
|
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: 115.95 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM------LWRRDSREKAQHpLSFVFQE--ATLM 106
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWELRKR-IGLVSPAlqLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWSSVRNNVrlpL----DLAGVPR---AEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:COG1119 93 RDETVLDVV---LsgffDSIGLYReptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997434 180 FGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIRE 241
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRVVAAGPKEE 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-250 |
7.47e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.96 E-value: 7.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 34 SNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----------LWrrDSREKAqhplSFVFQE 102
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldtsdeenLW--DIRNKA----GMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 103 ------ATLmpwssVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLL 175
Cdd:PRK13633 94 pdnqivATI-----VEEDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 176 MDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVfLSQRVIMMAArpGRVVEDIPIREPFPRSEAFR 250
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMDS--GKVVMEGTPKEIFKEVEMMK 239
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-235 |
1.69e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.36 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 17 PAAATPAIEV--LSaekIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLK-------MVAGL-VEpsdGKLMLWRR 86
Cdd:COG1117 5 ASTLEPKIEVrnLN---VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGArVE---GEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 87 DSREKAQHPLSF------VFQEATLMPwSSVRNNVRLPLDLAGV-PRAEGNTRVSEVLELVGL-GKFADVL---PRELSG 155
Cdd:COG1117 79 DIYDPDVDVVELrrrvgmVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwDEVKDRLkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 156 GMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDsDLLrlwQE--QNLTVVFVTHSIHEAVFLSQRVIMMAArpGRV 233
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIE-ELI---LElkKDYTIVIVTHNMQQAARVSDYTAFFYL--GEL 231
|
..
gi 488997434 234 VE 235
Cdd:COG1117 232 VE 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
38-237 |
2.28e-30 |
|
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: 113.08 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW---RRDSREKAQHPLSFVfQEATLMPWSSVRNN 114
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDgksYQKNIEALRRIGALI-EAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 VRLPLDLAGVPRAegntRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLdSD 194
Cdd:cd03268 93 LRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL-RE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488997434 195 LLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDI 237
Cdd:cd03268 168 LILSLRDQGITVLISSHLLSEIQKVADRIGII--NKGKLIEEG 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
35-235 |
5.75e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 112.50 E-value: 5.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD----SREKAQHPLSFVFQEATLMPwSS 110
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlKPEIYRQQVSYCAQTPTLFG-DT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDLAgvpraegNTRVSEVLELVGLGKFAdvLPR--------ELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:PRK10247 97 VYDNLIFPWQIR-------NQQPDPAIFLDDLERFA--LPDtiltkniaELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488997434 183 LDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEaVFLSQRVIMMAARPGRVVE 235
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGEMQE 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-234 |
8.69e-30 |
|
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: 109.83 E-value: 8.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSnGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW-----RRDSREKAQHPLSF 98
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkevsFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQeatlmpwssvrnnvrlpldlagvpraegntrvsevlelvglgkfadvlpreLSGGMQMRVSIARGLVTRPKLLLMDE 178
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 179 PFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVV 234
Cdd:cd03216 109 PTAALTPAEVERL-FKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL--RDGRVV 161
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
35-216 |
1.87e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.02 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwrrdsREKAQHPLSFVFQEATLmPWS---SV 111
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAGGARVAYVPQRSEV-PDSlplTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 RNNVRL----PLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEIT 187
Cdd:NF040873 75 RDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....*....
gi 488997434 188 RNKLDsDLLRLWQEQNLTVVFVTHSIHEA 216
Cdd:NF040873 155 RERII-ALLAEEHARGATVVVVTHDLELV 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-241 |
2.91e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.36 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 21 TPAIEVLSAEKIYSNG---TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD---------S 88
Cdd:PRK10535 2 TALLELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldadalA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 89 REKAQHpLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLV 168
Cdd:PRK10535 82 QLRREH-FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 169 TRPKLLLMDEPFGALDEITRNKLDSDLLRLwQEQNLTVVFVTHSIHEAVfLSQRVIMMaaRPGRVVEDIPIRE 241
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAA-QAERVIEI--RDGEIVRNPPAQE 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-235 |
4.20e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.79 E-value: 4.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 18 AAATPAIEVLSAEKIYSNGtRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPLS 97
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 98 -------------FVFQEAT--LMPWSSVRNNVRLPLDLAGVpRAEGNTR--VSEVLELVGLG-KFADVLPRELSGGMQM 159
Cdd:PRK11701 80 eaerrrllrtewgFVHQHPRdgLRMQVSAGGNIGERLMAVGA-RHYGDIRatAGDWLERVEIDaARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 160 RVSIARGLVTRPKLLLMDEPFGALDEITRNKLdSDLLR-LWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARL-LDLLRgLVRELGLAVVIVTHDLAVARLLAHRLLVM--KQGRVVE 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
33-250 |
1.28e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.17 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML------WRRDSREKAQHPLSFVFQ---EA 103
Cdd:PRK13639 11 YPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikYDKKSLLEVRKTVGIVFQnpdDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 104 TLMPwsSVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:PRK13639 91 LFAP--TVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 183 LDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFPRSEAFR 250
Cdd:PRK13639 168 LDPMGASQI-MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSD--GKIIKEGTPKEVFSDIETIR 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-226 |
1.60e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.50 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 41 LPVNLTI-NQGefIT-LLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR---DSREKAQHP-----LSFVFQEATLMPWSS 110
Cdd:PRK11144 15 LTVNLTLpAQG--ITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGICLPpekrrIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLpldlaGVpRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:PRK11144 93 VRGNLRY-----GM-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 488997434 191 LDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-241 |
1.61e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.48 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 25 EVLSAEKI-YSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQH--- 94
Cdd:PRK13548 1 AMLEARNLsVRLGGRTLLDdVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladwsPAELARRrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 -----PLSFVFqeatlmpwsSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLV- 168
Cdd:PRK13548 81 lpqhsSLSFPF---------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 169 -----TRPKLLLMDEPFGALD--------EITRNkldsdllrLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDlahqhhvlRLARQ--------LAHERGLAVIVVLHDLNLAARYADRIVLLHQ--GRLVA 221
|
....*.
gi 488997434 236 DIPIRE 241
Cdd:PRK13548 222 DGTPAE 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
39-236 |
2.23e-28 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 108.06 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 39 ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSREKAQHpLSFVFQEATLMpWSSVRN 113
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdiRQLDPADLRRN-IGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 114 NVRLpldlaGVPRAEGNtRVSEVLELVGLGKFADVLP-----------RELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:cd03245 97 NITL-----GAPLADDE-RILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 183 LDEITRNKLDSDLLRLWQEQnlTVVFVThsiHEAVFLS--QRVIMMAArpGRVVED 236
Cdd:cd03245 171 MDMNSEERLKERLRQLLGDK--TLIIIT---HRPSLLDlvDRIIVMDS--GRIVAD 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
38-236 |
2.60e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 108.00 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSrekaqhplSFVFQEATLMPWSSVRNNVRL 117
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS--------SLLGLGGGFNPELTGRENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 118 PLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDsDLLR 197
Cdd:cd03220 108 NGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ-RRLR 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 488997434 198 LWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVED 236
Cdd:cd03220 187 ELLKQGKTVILVSHDPSSIKRLCDRALVLEK--GKIRFD 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
36-241 |
2.92e-28 |
|
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: 107.91 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQHPLSFVFQEATLMPWSS 110
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitglpPHERARAGIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDLAgvPRAEGNTRVSEVLELV-GLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL-----D 184
Cdd:cd03224 92 VEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLapkivE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 185 EItrnkldSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:cd03224 170 EI------FEAIRELRDEGVTILLVEQNARFALEIADRAYVLER--GRVVLEGTAAE 218
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
22-235 |
5.72e-28 |
|
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: 107.99 E-value: 5.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 22 PAIEVLSAEKIYSNGtRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwRRDSREKAQHPLsFVFQ 101
Cdd:TIGR02323 2 PLLQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSGAELEL-YQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 102 EAT---LM--PWSSVRNNVRLPLDL---AGV----------PRAEGNTRVSEVLEL----VGLGKFADvLPRELSGGMQM 159
Cdd:TIGR02323 77 EAErrrLMrtEWGFVHQNPRDGLRMrvsAGAnigerlmaigARHYGNIRATAQDWLeeveIDPTRIDD-LPRAFSGGMQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 160 RVSIARGLVTRPKLLLMDEPFGALDEITRNKLdSDLLR-LWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARL-LDLLRgLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRVVE 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
43-247 |
1.70e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.12 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM----LWRRDSREKAQHPLSFVFQE-------ATlmpwssV 111
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQNpdnqfvgAT------V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 RNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL 191
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 192 DSDLLRLWQEQNLTVVFVTHSIHEaVFLSQRVIMMaaRPGRVVEDIPIREPFPRSE 247
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM--KNGQVESTSTPRELFSRGN 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-235 |
4.18e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 109.51 E-value: 4.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 22 PAIEVLSAEKIYSNGTRALLP----VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----W------RR 86
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRGVVKavdnVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdeWvdmtkpGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 87 DSREKAQHPLSFVFQEATLMPWSSVRNNVRLPLDLAgVPRAEGNTRVSEVLELVGLG-KFA----DVLPRELSGGMQMRV 161
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDeEKAeeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 162 SIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKIVK 508
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-234 |
2.81e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.92 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 21 TPAIEVLSAEKIYSNGTR-ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW----RRDSREKAQHP 95
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitiSKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 96 LSFVFQEatlmP-----WSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTR 170
Cdd:PRK13632 85 IGIIFQN----PdnqfiGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 171 PKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVfLSQRVIMMAArpGRVV 234
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSE--GKLI 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
33-250 |
4.30e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML------WRRDSREKAQHPLSFVFQEATLM 106
Cdd:PRK13636 15 YSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFdgkpidYSRKGLMKLRESVGMVFQDPDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWS-SVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:PRK13636 95 LFSaSVYQDVSFgAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 185 EITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPFPRSEAFR 250
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM--KEGRVILQGNPKEVFAEKEMLR 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
38-235 |
4.53e-26 |
|
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: 106.69 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVePSDGKLMLWRRD---SREKAQHPL----SFVFQE--ATLMPW 108
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDldgLSRRALRPLrrrmQVVFQDpfGSLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLPLDL--AGVPRAEGNTRVSEVLELVGL-GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDE 185
Cdd:COG4172 379 MTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 186 ITRNKLdSDLLR-LWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:COG4172 459 SVQAQI-LDLLRdLQREHGLAYLFISHDLAVVRALAHRVMVM--KDGKVVE 506
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
33-235 |
4.71e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.79 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDS-REKaqhpLSFVFQEAT 104
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdLTLESlRRQ----IGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPwSSVRNNVRLpldlaGVPRAeGNTRVSEVLELVGLGKFADVLP-----------RELSGGMQMRVSIARGLVTRPKL 173
Cdd:COG1132 425 LFS-GTIRENIRY-----GRPDA-TDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 174 LLMDEPFGALD-----EITRNkldsdLLRLwqEQNLTVVFVTH---SIHEAvflsQRVIMMAArpGRVVE 235
Cdd:COG1132 498 LILDEATSALDteteaLIQEA-----LERL--MKGRTTIVIAHrlsTIRNA----DRILVLDD--GRIVE 554
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
32-222 |
5.33e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 32 IYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLK------------MVAGLVEPSDGKLMLWRRDSREkAQHPLSFV 99
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIVYNGHNIYSPRTDTVD-LRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPWSsVRNNVRLPLDLAGVPRAEgntRVSEVLE--LVGLGKFADVLPR------ELSGGMQMRVSIARGLVTRP 171
Cdd:PRK14239 92 FQQPNPFPMS-IYENVVYGLRLKGIKDKQ---VLDEAVEksLKGASIWDEVKDRlhdsalGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 172 KLLLMDEPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTHSIHEAVFLSQR 222
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
43-249 |
5.74e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 102.74 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS-----------------DGKLMLWRRDSREKAQHPLSFVFQEATL 105
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSegsivvngqtinlvrdkDGQLKVADKNQLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 106 MPWSSVRNNV-RLPLDLAGVPRAEGNTRVSEVLELVGLGKFA-DVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK10619 104 WSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 184 DEitrnKLDSDLLRLWQ---EQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPF-----PRSEAF 249
Cdd:PRK10619 184 DP----ELVGEVLRIMQqlaEEGKTMVVVTHEMGFARHVSSHVIFL--HQGKIEEEGAPEQLFgnpqsPRLQQF 251
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
26-241 |
6.48e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.08 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 26 VLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwRRDSREKAqhPLSFvfqEATL 105
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV---EVNGRVSA--LLEL---GAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 106 MPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADvLP-RELSGGMQMR----VSIArglvTRPKLLLMDEPF 180
Cdd:COG1134 100 HPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID-QPvKTYSSGMRARlafaVATA----VDPDILLVDEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488997434 181 GALDEITRNKLDSDLLRLWqEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIRE 241
Cdd:COG1134 175 AVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWL--EKGRLVMDGDPEE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-225 |
1.04e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSD-------------GKLMLWrrDS 88
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNdISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdgitlTAKTVW--DI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 89 REKaqhpLSFVFQEA-TLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGL 167
Cdd:PRK13640 83 REK----VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 168 VTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIM 225
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVL 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-241 |
1.15e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 103.24 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSREKAQhpLSFVF-QEATLMpWS-S 110
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyvpFKRRKEFARR--IGVVFgQRSQLW-WDlP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:COG4586 113 AIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 191 LDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:COG4586 193 IREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH--GRIIYDGSLEE 241
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-212 |
2.82e-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: 104.36 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 17 PAAAT-----PAIEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREK 91
Cdd:TIGR02868 323 PAAGAvglgkPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 92 AQHPL----SFVFQEATLMPwSSVRNNVRLpldlaGVPRAEGNtRVSEVLELVGLGKFADVLP-----------RELSGG 156
Cdd:TIGR02868 403 DQDEVrrrvSVCAQDAHLFD-TTVRENLRL-----ARPDATDE-ELWAALERVGLADWLRALPdgldtvlgeggARLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 157 MQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTHS 212
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-236 |
3.21e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.86 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 26 VLSAEKIYS--NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVE----------------PSDGKLMlwrRD 87
Cdd:PRK09984 4 IIRVEKLAKtfNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshiellgrtvQREGRLA---RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 88 SREKAQHPlSFVFQEATLMPWSSVRNNVrLPLDLAGVP---------RAEGNTRVSEVLELVGLGKFADVLPRELSGGMQ 158
Cdd:PRK09984 81 IRKSRANT-GYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 159 MRVSIARGLVTRPKLLLMDEPFGALD-EITRNKLDSdLLRLWQEQNLTVVFVTHSIHEAVFLSQRVImmAARPGRVVED 236
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDpESARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIV--ALRQGHVFYD 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-237 |
3.50e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.55 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGT----RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----------WRRdsr 89
Cdd:COG1101 2 LELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdgkdvtklpeYKR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 90 ekAQHpLSFVFQE-----ATLMpwsSVRNNvrlpLDLA-----------GVPRAEgNTRVSEVLELVGLGkfadvLprE- 152
Cdd:COG1101 79 --AKY-IGRVFQDpmmgtAPSM---TIEEN----LALAyrrgkrrglrrGLTKKR-RELFRELLATLGLG-----L--En 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 153 --------LSGGMQMRVSIARGLVTRPKLLLMDEPFGALD--------EITRnkldsdllRLWQEQNLTVVFVTHSIHEA 216
Cdd:COG1101 141 rldtkvglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktaalvlELTE--------KIVEENNLTTLMVTHNMEQA 212
|
250 260
....*....|....*....|.
gi 488997434 217 VFLSQRVIMMAArpGRVVEDI 237
Cdd:COG1101 213 LDYGNRLIMMHE--GRIILDV 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-223 |
6.82e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.65 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 19 AATPAIEVLSAEKIYSNGTrALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHP--- 95
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArqr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 96 LSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLL 175
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488997434 176 MDEPFGALDEITRNkLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRV 223
Cdd:PRK13537 162 LDEPTTGLDPQARH-LMWERLRSLLARGKTILLTTHFMEEAERLCDRL 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
43-241 |
8.97e-25 |
|
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: 98.90 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW-----RRDSREKAQHPLSFVFQEATLMPWSSVRNNVRL 117
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgeditGLPPHRIARLGIGYVPEGRRIFPSLTVEENLLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 118 PLdLAGVPRAEGNTRVSEVLEL--VgLGKFADVLPRELSGG-MQMrVSIARGLVTRPKLLLMDEPFGAL-----DEItrn 189
Cdd:COG0410 102 GA-YARRDRAEVRADLERVYELfpR-LKERRRQRAGTLSGGeQQM-LAIGRALMSRPKLLLLDEPSLGLaplivEEI--- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 190 kldSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:COG0410 176 ---FEIIRRLNREGVTILLVEQNARFALEIADRAYVLER--GRIVLEGTAAE 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-234 |
1.56e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SF 98
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQEATLMPWSS-VRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:PRK13647 84 VFQDPDDQVFSStVWDDVAFgPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLWQeQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVV 234
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKE--GRVL 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
38-211 |
4.82e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.04 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKlmlWRRDSREKA----QHPLsfvfqeatlMPWSSVR 112
Cdd:COG4178 376 RPLLeDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR---IARPAGARVlflpQRPY---------LPLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNVRLPLDLAGVPRAEgntrVSEVLELVGLGKFADVL------PRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEI 186
Cdd:COG4178 444 EALLYPATAEAFSDAE----LREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|....*..
gi 488997434 187 TRNKldsdLLRLWQEQ--NLTVVFVTH 211
Cdd:COG4178 520 NEAA----LYQLLREElpGTTVISVGH 542
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
43-235 |
4.86e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.01 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmLW------------RRDSREKAQhplsFVFQE--ATLMPW 108
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV-AWlgkdllgmkddeWRAVRSDIQ----MIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLPLDL--AGVPRAEGNTRVSEVLELVGL-GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDE 185
Cdd:PRK15079 115 MTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 186 ITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYL--GHAVE 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-241 |
7.40e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 19 AATPAIEVLSAEKIYsNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKlMLWR------RDSREKA 92
Cdd:COG3845 1 MMPPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGE-ILIDgkpvriRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 93 QHPLSFVFQEATLMPWSSVRNNVRL---PLDLAGVPRAEGNTRVSEVLELVGLgkfaDVLP----RELSGGMQMRVSIAR 165
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGL----DVDPdakvEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 166 GLVTRPKLLLMDEPFGAL--DEItrnklDS--DLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIRE 241
Cdd:COG3845 155 ALYRGARILILDEPTAVLtpQEA-----DElfEILRRLAAEGKSIIFITHKLREVMAIADRVTVL--RRGKVVGTVDTAE 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
43-226 |
1.01e-23 |
|
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: 95.23 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwrrdsrekaQHP--LSFVFQEATLMPwSSVRNNVrlpld 120
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-----------SVPgsIAYVSQEPWIQN-GTIRENI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 121 LAGVPRAEgnTRVSEVLELVGLGKFADVLPR-------E----LSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRN 189
Cdd:cd03250 87 LFGKPFDE--ERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488997434 190 KL-DSDLLRLWQEqNLTVVFVTHSIHeavFLSQ--RVIMM 226
Cdd:cd03250 165 HIfENCILGLLLN-NKTRILVTHQLQ---LLPHadQIVVL 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
36-211 |
1.12e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwRRDSRekaqhpLSFVFQEATLMPWSSVRNN 114
Cdd:COG0488 9 GGRPLLdDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR------IGYLPQEPPLDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 VrlpldLAGVPRA-------------------------------------EGNTRVSEVLElvGLGkFADVLP----REL 153
Cdd:COG0488 82 V-----LDGDAELraleaeleeleaklaepdedlerlaelqeefealggwEAEARAEEILS--GLG-FPEEDLdrpvSEL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 154 SGGMQMRVSIARGLVTRPKLLLMDEPfgaldeiTrNKLDSDLLRlWQEQNL-----TVVFVTH 211
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEP-------T-NHLDLESIE-WLEEFLknypgTVLVVSH 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-235 |
1.19e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.64 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 22 PAIEVLSAEkIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS-----DGKLMLW------RRDSRE 90
Cdd:PRK14258 6 PAIKVNNLS-FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFnqniyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 91 KAQHPLSFVFQEATLMPWSsVRNNVRLPLDLAG-VPRAEGNTRVSEVLELVGL-GKFADVLPR---ELSGGMQMRVSIAR 165
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMS-VYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwDEIKHKIHKsalDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 166 GLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAARPGRVVE 235
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQ 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
33-215 |
1.58e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 96.37 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlWRRD------SREK---AQHPLSFVFQE 102
Cdd:PRK11831 15 FTRGNRCIFDnISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI--LFDGenipamSRSRlytVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 103 ATLMPWSSVRNNVRLPL-DLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFG 181
Cdd:PRK11831 93 GALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 488997434 182 ALDEITRNKldsdLLRLWQEQN----LTVVFVTHSIHE 215
Cdd:PRK11831 173 GQDPITMGV----LVKLISELNsalgVTCVVVSHDVPE 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
26-251 |
1.93e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.35 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 26 VLSAEKIYS--NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDS-----REKAQHPLSF 98
Cdd:PRK10895 3 TLTAKNLAKayKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQEATLMPWSSVRNNVRLPLDL-AGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 178 EPFGALDEITRNKLDSDLLRLwQEQNLTVVFVTHSIHE-------AVFLSQRVIMMAARPGRVVEDIPIREPFpRSEAFR 250
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVREtlavcerAYIVSQGHLIAHGTPTEILQDEHVKRVY-LGEDFR 240
|
.
gi 488997434 251 V 251
Cdd:PRK10895 241 L 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-247 |
1.94e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.68 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAeKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS-----DGKLMLWRRDSREKAQHPLS 97
Cdd:PRK14267 4 AIETVNL-RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 98 ------FVFQEATLMPWSSVRNNVRLPLDLAGV--PRAEGNTRVSEVLELVGL-GKFADVL---PRELSGGMQMRVSIAR 165
Cdd:PRK14267 83 vrrevgMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 166 GLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEqnLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFPR 245
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYL--GKLIEVGPTRKVFEN 238
|
..
gi 488997434 246 SE 247
Cdd:PRK14267 239 PE 240
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-241 |
1.98e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNgTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmLW--RRDSREKAQH----Pl 96
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV-LWdgEPLDPEDRRRigylP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 sfvfQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:COG4152 78 ----EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 177 DEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIRE 241
Cdd:COG4152 154 DEPFSGLDPVNVELL-KDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINK--GRKVLSGSVDE 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
35-184 |
3.32e-23 |
|
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: 93.58 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHP---LSFVFQEATLMPWSSV 111
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhenILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 112 RNNVRLpldLAGVPRAEGNTrVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:TIGR01189 91 LENLHF---WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
43-250 |
3.65e-23 |
|
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: 94.36 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEP----SDGKLMLWRRDSREKA--QHPLSFVFQE--ATLMPWSSVRNN 114
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSirGRHIATIMQNprTAFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 VRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVL---PRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL 191
Cdd:TIGR02770 85 AIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488997434 192 DSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF--PRSEAFR 250
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRIVERGTVKEIFynPKHETTR 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
36-234 |
4.70e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSREKAQHpLSFVFQEATLMPWS 109
Cdd:PRK11231 13 GTKRILNdLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpISMLSSRQLARR-LALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNNV---RLP-LDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDe 185
Cdd:PRK11231 92 TVRELVaygRSPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488997434 186 ITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVV 234
Cdd:PRK11231 171 INHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLAN--GHVM 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
43-228 |
4.85e-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: 94.04 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDS---------REKA---QHPLSFVFQEATLMPWSS 110
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdlaqaspREILalrRRTIGYVSQFLRVIPRVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLgkfadvlPREL--------SGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:COG4778 110 ALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488997434 183 LDEITRNKLdSDLLRLWQEQNLTVVFVTHsiHEAVF--LSQRVIMMAA 228
Cdd:COG4778 183 LDAANRAVV-VELIEEAKARGTAIIGIFH--DEEVReaVADRVVDVTP 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
38-235 |
6.86e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.80 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----------WRRDSREKAQhplsFVFQE--AT 104
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqgqdllkadpeAQKLLRQKIQ----IVFQNpyGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPWSSVRNNVRLPLDL-AGVPRAEGNTRVSEVLELVGL-GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:PRK11308 105 LNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488997434 183 LDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYL--GRCVE 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
36-265 |
8.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.80 E-value: 8.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKL----MLWRRDSREKAQHPLS------FVFQEATL 105
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPVRkkvgvvFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 106 MPWSSVRNNVRLPLDLaGVPRAEGNTRVSEVLELVGLGK-FADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:PRK13643 98 FEETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 185 EITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAV-------FLSQRVIMMAARPGRVVEDIpirePFPRSEAFRVsPTFSL 257
Cdd:PRK13643 177 PKARIEM-MQLFESIHQSGQTVVLVTHLMDDVAdyadyvyLLEKGHIISCGTPSDVFQEV----DFLKAHELGV-PKATH 250
|
....*...
gi 488997434 258 YARQLQDS 265
Cdd:PRK13643 251 FADQLQKT 258
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-247 |
1.88e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVE--PS---DGKLMLwrrDSREKAQHPLS-------FVFQEAT 104
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYL---DGQDIFKMDVIelrrrvqMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPWSSVRNNVRLPLDLAGV--PRAEGNTRVSEVLELVGLgkFADVLPR------ELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQL--WDEVKDRldapagKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLWQEqnLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF--PRSE 247
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYK--GQIVEWGPTREVFtnPRHE 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
39-235 |
2.10e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 93.32 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 39 ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrdsrekAQHPLSF------------VFQEAT-- 104
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI--------DDHPLHFgdysyrsqrirmIFQDPSts 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPWSSVRNNVRLPL----DLAGVPRAEgntRVSEVLELVGL-GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:PRK15112 100 LNPRQRISQILDFPLrlntDLEPEQREK---QIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 180 FGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ--GEVVE 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
44-223 |
2.37e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.79 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 44 NLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmLWR----RDSREKAQHPLSFVFQEATLMPWSSVRNNVRLPL 119
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-LWQgepiRRQRDEYHQDLLYLGHQPGIKTELTALENLRFYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 120 DLAGVPRAEgntRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD-----EITRnkldsd 194
Cdd:PRK13538 100 RLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvaRLEA------ 170
|
170 180
....*....|....*....|....*....
gi 488997434 195 LLRLWQEQNLTVVFVTHsiHEAVFLSQRV 223
Cdd:PRK13538 171 LLAQHAEQGGMVILTTH--QDLPVASDKV 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
33-235 |
2.52e-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: 92.29 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEATLMPw 108
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrsmiGVVLQDTFLFS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLpldlaGVPRAEgNTRVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:cd03254 91 GTIMENIRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 178 EPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTHSIHEAVFlSQRVIMMaaRPGRVVE 235
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKN-ADKILVL--DDGKIIE 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-236 |
3.38e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.61 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGT----RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPLSFV 99
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 FQEATLMPWSSVR-----NNVR------------------LPLDLA------GVPRAEGNTRVSEVLELVGLGK-FADVL 149
Cdd:PRK13651 83 VLEKLVIQKTRFKkikkiKEIRrrvgvvfqfaeyqlfeqtIEKDIIfgpvsmGVSKEEAKKRAAKYIELVGLDEsYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 150 PRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaR 229
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF--K 239
|
....*..
gi 488997434 230 PGRVVED 236
Cdd:PRK13651 240 DGKIIKD 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-234 |
4.05e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.12 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 18 AAATPAIEVLSAEKIYSnGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrdsREKAQHPLS 97
Cdd:PRK15439 6 TTAPPLLCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI-----GGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 98 ----------FVFQEATLMPWSSVRNNVrlpldLAGVPRAEGNT-RVSEVLELVGLGKFADVLPRELSGGMQMRVSIARG 166
Cdd:PRK15439 80 pakahqlgiyLVPQEPLLFPNLSVKENI-----LFGLPKRQASMqKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 167 LVTRPKLLLMDEPFGALDEITRNKLDSDlLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVV 234
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSR-IRELLAQGVGIVFISHKLPEIRQLADRISVM--RDGTIA 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
43-225 |
4.77e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSREKAQHpLSFVFQEA-TLMPWSSVRNNVR 116
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITDDNFEKLRKH-IGIVFQNPdNQFVGSIVKYDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 117 LPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLL 196
Cdd:PRK13648 107 FGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVR 186
|
170 180
....*....|....*....|....*....
gi 488997434 197 RLWQEQNLTVVFVTHSIHEAVFLSQRVIM 225
Cdd:PRK13648 187 KVKSEHNITIISITHDLSEAMEADHVIVM 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-226 |
1.29e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 32 IYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVE------PSDGKLMLWRRDSRE----KAQHPLSFVFQ 101
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQidaiKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 102 EATLMPWSSVRNNVRLPLDLAGVP-RAEGNTRVSEVLELVGLGKfaDVLPR------ELSGGMQMRVSIARGLVTRPKLL 174
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWK--EVYDRlnspasQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 175 LMDEPFGALDEITRNKLDSDLLRLWQEqnLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFL 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
43-247 |
1.34e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.31 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-WRRDSREKA---QHPLSFVFQEA-TLMPWSSVRNNVRL 117
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVwnlRRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 118 PLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLR 197
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 198 LWQEQNLTVVFVTHSIHEAVFlSQRVIMMaaRPGRVVEDIPIREPFPRSE 247
Cdd:PRK13642 186 IKEKYQLTVLSITHDLDEAAS-SDRILVM--KAGEIIKEAAPSELFATSE 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-250 |
1.57e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.02 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSREkAQHPLSF 98
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepITKENIRE-VRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQEATLMPWS-SVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:PRK13652 83 VFQNPDDQIFSpTVEQDIAFgPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPFPRSEAFR 250
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM--DKGRIVAYGTVEEIFLQPDLLA 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-228 |
2.95e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.43 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 11 SDTRFIPAAATPAIEVLSAEKIYsnGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR--- 86
Cdd:PRK13536 29 AKASIPGSMSTVAIDLAGVSKSY--GDKAVVnGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 87 DSREKAQHPLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARG 166
Cdd:PRK13536 107 ARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997434 167 LVTRPKLLLMDEPFGALDEITRNkLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAA 228
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARH-LIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-271 |
3.54e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNGT----RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW------------RR 86
Cdd:PRK13641 2 SIKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetgnknLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 87 DSREKAQhpLSFVFQEATLMPwSSVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLGK-FADVLPRELSGGMQMRVSIA 164
Cdd:PRK13641 82 KLRKKVS--LVFQFPEAQLFE-NTVLKDVEFgPKNF-GFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 165 RGLVTRPKLLLMDEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPFP 244
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL--EHGKLIKHASPKEIFS 234
|
250 260 270
....*....|....*....|....*....|.
gi 488997434 245 RSE----AFRVSPTFSLYARQLQDSLLQASQ 271
Cdd:PRK13641 235 DKEwlkkHYLDEPATSRFASKLEKGGFKFSE 265
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
38-245 |
4.25e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.96 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEpSDGKLM----------LWRRDSREKAQ---HPLSFVFQEA- 103
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaeklefngqdLQRISEKERRNlvgAEVAMIFQDPm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 104 -TLMPWSSVRNNVRLPLDL-AGVPRAEGNTRVSEVLELVGLGKFA---DVLPRELSGGMQMRVSIARGLVTRPKLLLMDE 178
Cdd:PRK11022 100 tSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 179 PFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF--PR 245
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA--GQVVETGKAHDIFraPR 246
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
33-234 |
4.29e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHP-----LSFVFQEA-TLM 106
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirklVGIVFQNPeTQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEI 186
Cdd:PRK13644 91 VGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488997434 187 TRNKLDSDLLRLwQEQNLTVVFVTHSIHEaVFLSQRVIMMAArpGRVV 234
Cdd:PRK13644 171 SGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDR--GKIV 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-211 |
6.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 23 AIEVLSAEKIYSNGT----RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM----LWRRDSREKAQH 94
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtLITSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 P------LSFVFQEATLMPwSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGK-FADVLPRELSGGMQMRVSIARGL 167
Cdd:PRK13649 82 QirkkvgLVFQFPESQLFE-ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488997434 168 VTRPKLLLMDEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTH 211
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKEL-MTLFKKLHQSGMTIVLVTH 203
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
35-236 |
1.54e-20 |
|
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: 87.54 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD----SREKAQHPLSFVFQEATLMPwSS 110
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlalaDPAWLRRQVGVVLQENVLFN-RS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDlaGVPRaegnTRVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:cd03252 92 IRDNIALADP--GMSM----ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 180 FGALDEITRNKLDSDLLRLWqeQNLTVVFVTHSIhEAVFLSQRVIMMAArpGRVVED 236
Cdd:cd03252 166 TSALDYESEHAIMRNMHDIC--AGRTVIIIAHRL-STVKNADRIIVMEK--GRIVEQ 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-212 |
1.83e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrdsREKAQHpLSFVFQEAT-------LMPWSSVRNNV 115
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL-----DGGDID-DPDVAEACHylghrnaMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 RLPLDLAGvpraEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDeITRNKLDSDL 195
Cdd:PRK13539 95 EFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAVALFAEL 169
|
170
....*....|....*..
gi 488997434 196 LRLWQEQNLTVVFVTHS 212
Cdd:PRK13539 170 IRAHLAQGGIVIAATHI 186
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
36-235 |
4.60e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.04 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQHPLSFVFQEATLMPWSS 110
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitklpPHERARAGIAYVPQGREIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNvrLPLDLAGVPRAEGNtRVSEVLELVGLGKfaDVLPR---ELSGGMQMRVSIARGLVTRPKLLLMDEPF-----GA 182
Cdd:TIGR03410 92 VEEN--LLTGLAALPRRSRK-IPDEIYELFPVLK--EMLGRrggDLSGGQQQQLAIARALVTRPKLLLLDEPTegiqpSI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488997434 183 LDEITRNkldsdLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:TIGR03410 167 IKDIGRV-----IRRLRAEGGMAILLVEQYLDFARELADRYYVMER--GRVVA 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
33-233 |
5.49e-20 |
|
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: 84.58 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDsrEKAQHpLSFVFQEAT 104
Cdd:cd03246 10 YPGAEPPVLRnVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqWDPN--ELGDH-VGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPwSSVRNNVrlpldlagvpraegntrvsevlelvglgkfadvlpreLSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:cd03246 87 LFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488997434 185 EITRNKLDSDLLRLwQEQNLTVVFVTHSIhEAVFLSQRVIMMAArpGRV 233
Cdd:cd03246 129 VEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVLED--GRV 173
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
34-234 |
7.13e-20 |
|
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: 84.91 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 34 SNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS--DGKLMLWRRDSREKAQHPLS-FVFQEATLMPWS 109
Cdd:cd03213 18 SKSGKQLLKnVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKIIgYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNNVRlpldlagvpraegntrvsevlelvglgkFADVLpRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRN 189
Cdd:cd03213 98 TVRETLM----------------------------FAAKL-RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488997434 190 KLDSDLLRLWQeQNLTVVFVTHSIHEAVF-LSQRVIMMAarPGRVV 234
Cdd:cd03213 149 QVMSLLRRLAD-TGRTIICSIHQPSSEIFeLFDKLLLLS--QGRVI 191
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-211 |
7.23e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 17 PAAATPAIEVLSAEKIYSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrdsrekAQHP 95
Cdd:PRK11160 332 AAADQVSLTLNNVSFTYPDQPQPVLKgLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL--------NGQP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 96 LSfVFQEATLMPWSSV------------RNNVRLPLDLAgvpraeGNTRVSEVLELVGLGKFADVLP----------REL 153
Cdd:PRK11160 404 IA-DYSEAALRQAISVvsqrvhlfsatlRDNLLLAAPNA------SDEALIEVLQQVGLEKLLEDDKglnawlgeggRQL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 154 SGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITrnklDSDLLRLWQE--QNLTVVFVTH 211
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET----ERQILELLAEhaQNKTVLMITH 532
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
34-211 |
7.48e-20 |
|
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: 84.85 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 34 SNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR---DSREKAQHPLSFVFQEATLMPWS 109
Cdd:cd03231 9 ERDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNNVRLPLDLagvpraEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRN 189
Cdd:cd03231 89 SVLENLRFWHAD------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|..
gi 488997434 190 KLDSdLLRLWQEQNLTVVFVTH 211
Cdd:cd03231 163 RFAE-AMAGHCARGGMVVLTTH 183
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-213 |
8.75e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.75 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 25 EVLSAEkiysnGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGL-----------VEPSDGKLMLWRRDsrekaq 93
Cdd:PRK11174 356 EILSPD-----GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpyqgslkingIELRELDPESWRKH------ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 94 hpLSFVFQEATLmPWSSVRNNVRLpldlaGVPRAeGNTRVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVS 162
Cdd:PRK11174 425 --LSWVGQNPQL-PHGTLRDNVLL-----GNPDA-SDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLA 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 163 IARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQnlTVVFVTHSI 213
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQL 544
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
43-184 |
9.48e-20 |
|
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: 85.28 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEATLMPwSSVRNNVRLp 118
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLrsqiGLVSQEPVLFD-GTIAENIRY- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 119 ldlaGVPRAEgNTRVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:cd03249 100 ----GKPDAT-DEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
43-233 |
1.28e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 88.26 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR-------DSREK----AQhplSF-VFQEATlmpwss 110
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagdiATRRRvgymSQ---AFsLYGELT------ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488997434 191 LDSDLLRLWQEQNLTvVFV-THSIHEAVfLSQRVIMMAArpGRV 233
Cdd:NF033858 436 FWRLLIELSREDGVT-IFIsTHFMNEAE-RCDRISLMHA--GRV 475
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
40-234 |
1.45e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 40 LLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVePSDGKLMLWRRD---------SREKA----QHPLSF---VFQEA 103
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlsdwsaaelARHRAylsqQQSPPFampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 104 TL-MPwssvrnnvrlpldlAGVPRAEGNTRVSEVLELVGLgkfADVLPR---ELSGGMQMRVSIARGLVT-------RPK 172
Cdd:COG4138 91 ALhQP--------------AGASSEAVEQLLAQLAEALGL---EDKLSRpltQLSGGEWQRVRLAAVLLQvwptinpEGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997434 173 LLLMDEPFGALDEITRNKLDsDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVV 234
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALD-RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQ--GKLV 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
35-236 |
1.67e-19 |
|
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: 83.52 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD--SREKA-QHPLSFVFQEATLMPwSSV 111
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsDLEKAlSSLISVLNQRPYLFD-TTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 RNNvrlpldlagvpraegntrvsevlelvglgkfadvLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKl 191
Cdd:cd03247 92 RNN----------------------------------LGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 192 dsdLLRLWQEQ--NLTVVFVTH---SIHEAvflsQRVIMMAArpGRVVED 236
Cdd:cd03247 137 ---LLSLIFEVlkDKTLIWITHhltGIEHM----DKILFLEN--GKIIMQ 177
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
50-243 |
1.78e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 50 GEFITLLGPSGCGKSTLLKMVAGLVEP---------------SDGKLMLWRRDsrekaqhpLSFVFQE--ATLMPWSSVR 112
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESqggeiifngqridtlSPGKLQALRRD--------IQFIFQDpyASLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNVRLPLDLAGVPRAE-GNTRVSEVLELVGL-GKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:PRK10261 422 DSIMEPLRVHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488997434 191 LDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF 243
Cdd:PRK10261 502 IINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL--GQIVEIGPRRAVF 552
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-236 |
3.16e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.36 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNgTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQHpLSF 98
Cdd:COG4604 2 IEIKNVSKRYGG-KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvattpSRELAKR-LAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQEATLMPWSSVRNNV---RLPLDlAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLL 175
Cdd:COG4604 80 LRQENHINSRLTVRELVafgRFPYS-KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 176 MDEPFGALD-----EITRNkldsdLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVED 236
Cdd:COG4604 159 LDEPLNNLDmkhsvQMMKL-----LRRLADELGKTVVIVLHDINFASCYADHIVAM--KDGRVVAQ 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
36-235 |
3.64e-19 |
|
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: 86.78 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGL--VEPSDGKLM------------------------------- 82
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 83 ----LWRRDSREKA--QHPLSFVFQEA-TLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSG 155
Cdd:TIGR03269 92 eevdFWNLSDKLRRriRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 156 GMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTH-------SIHEAVFLSQRVIMMAA 228
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpeviedLSDKAIWLENGEIKEEG 251
|
....*..
gi 488997434 229 RPGRVVE 235
Cdd:TIGR03269 252 TPDEVVA 258
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
55-233 |
5.37e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 5.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 55 LLGPSGCGKSTLLKMVAGLVEPSDGKLmLWRRDSREKAQHPL-------SFVFQEA-TLMPWSSVRNNVRLPLDLAGVPR 126
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRGLlalrqqvATVFQDPeQQIFYTDIDSDIAFSLRNLGVPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 127 AEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNlTV 206
Cdd:PRK13638 111 AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HV 189
|
170 180 190
....*....|....*....|....*....|....
gi 488997434 207 VFVTHSI------HEAVF-LSQRVIMMAARPGRV 233
Cdd:PRK13638 190 IISSHDIdliyeiSDAVYvLRQGQILTHGAPGEV 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
24-221 |
1.60e-18 |
|
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: 79.80 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsnGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKlmlWRRDSREKaqhpLSFVFQe 102
Cdd:cd03221 1 IELENLSKTY--GGKLLLkDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI---VTWGSTVK----IGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 103 atlmpwssvrnnvrlpldlagvpraegntrvsevlelvglgkfadvlpreLSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190
....*....|....*....|....*....|....*....
gi 488997434 183 LDEITRNKLDSDLlrlwQEQNLTVVFVTHSIHeavFLSQ 221
Cdd:cd03221 101 LDLESIEALEEAL----KEYPGTVILVSHDRY---FLDQ 132
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
33-236 |
1.61e-18 |
|
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: 81.89 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEATLMP 107
Cdd:cd03251 10 YPGDGPPVLRdISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLrrqiGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 wSSVRNNVRLpldlaGVPRAEgNTRVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:cd03251 90 -DTVAENIAY-----GRPGAT-REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTH---SIHEAvflsQRVIMMAArpGRVVED 236
Cdd:cd03251 163 DEATSALDTESERLVQAALERL--MKNRTTFVIAHrlsTIENA----DRIVVLED--GKIVER 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-243 |
1.78e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 32 IYSNGT----RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----WRRDSREKAQHP------LS 97
Cdd:PRK13646 11 TYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditITHKTKDKYIRPvrkrigMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 98 FVFQEATLMPWSSVR------NNVRLPLDlagvpraEGNTRVSEVLelVGLGKFADVL---PRELSGGmQMR-VSIARGL 167
Cdd:PRK13646 91 FQFPESQLFEDTVEReiifgpKNFKMNLD-------EVKNYAHRLL--MDLGFSRDVMsqsPFQMSGG-QMRkIAIVSIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 168 VTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIREPF 243
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM--KEGSIVSQTSPKELF 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-226 |
2.08e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 20 ATPAIEVLSAEKIYSnGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR-----DSREKAQH 94
Cdd:PRK09700 2 ATPYISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynklDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 PLSFVFQEATLMPWSSVRNNV---RLPL-DLAGVP---RAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGL 167
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLyigRHLTkKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 168 VTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNlTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVM 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
38-214 |
3.93e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwRRDSREKaqhpLSFVFQEATLMPwssvrnnvRL 117
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---KRNGKLR----IGYVPQKLYLDT--------TL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 118 PLDLAGVPRAEGNTRVSEV---LELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSD 194
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKEDIlpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDL 162
|
170 180
....*....|....*....|
gi 488997434 195 LLRLWQEQNLTVVFVTHSIH 214
Cdd:PRK09544 163 IDQLRRELDCAVLMVSHDLH 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-231 |
4.71e-18 |
|
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: 80.92 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 46 TINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwrrdsrEKAQHPLSFVFQEATLMPWSSVRNNVRLPLDLAGvp 125
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------EIELDTVSYKPQYIKADYEGTVRDLLSSITKDFY-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 126 raEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLT 205
Cdd:cd03237 91 --THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKT 168
|
170 180
....*....|....*....|....*.
gi 488997434 206 VVFVTHSIHEAVFLSQRVIMMAARPG 231
Cdd:cd03237 169 AFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
37-235 |
4.99e-18 |
|
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: 83.20 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKS----TLLKMVA-GLVEPS-----DGKLML------WR--RDSRekaqhpLSF 98
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPdPAAHPSgsilfDGQDLLglsereLRriRGNR------IAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQE--ATLMPWSSVRNNVRLPLDL-AGVPRAEGNTRVSEVLELVGL---GKFADVLPRELSGGMQMRVSIARGLVTRPK 172
Cdd:COG4172 97 IFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 173 LLLMDEPFGALD-----EItrnkLdsDLLR-LWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:COG4172 177 LLIADEPTTALDvtvqaQI----L--DLLKdLQRELGMALLLITHDLGVVRRFADRVAVM--RQGEIVE 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
38-243 |
5.79e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.59 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW-----------RRDSREKAQHPLSFVFQEATLM 106
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipanlkkiKEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWSSVRNNVRLPLDLaGVPRAEGNTRVSEVLELVGLGK-FADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDE 185
Cdd:PRK13645 105 QETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 186 ITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVvedIPIREPF 243
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM--HEGKV---ISIGSPF 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
43-198 |
7.54e-18 |
|
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: 80.01 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSD---GKLMLWRRD-SREKAQHPLSFVFQEATLMPWSSVR------ 112
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPrKPDQFQKCVAYVRQDDILLPGLTVRetltyt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNVRLPLDLAG---VPRAEgntrvSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRN 189
Cdd:cd03234 106 AILRLPRKSSDairKKRVE-----DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
....*....
gi 488997434 190 KLDSDLLRL 198
Cdd:cd03234 181 NLVSTLSQL 189
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
43-262 |
8.27e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.51 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKS----TLLKMVAGLVEPSDGKLMLwrrDSREKAQHPLSFVfQEATLM--------PWSS 110
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLL---DGKPVAPCALRGR-KIATIMqnprsafnPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPLDLAGVPRAegNTRVSEVLELVGLGKFADVL---PRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEIT 187
Cdd:PRK10418 98 MHTHARETCLALGKPAD--DATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 188 RNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF--PRSEAFR--VSPTFSLYARQL 262
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRIVEQGDVETLFnaPKHAVTRslVSAHLALYGMEL 252
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
36-243 |
1.25e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSREKAQHPLSfVFQEATLMPWSS 110
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvEALSARAASRRVAS-VPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNV---RLP-LDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDeI 186
Cdd:PRK09536 94 VRQVVemgRTPhRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-I 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 187 TRNKLDSDLLRLWQEQNLTVVFVTHSIH-------EAVFLSQRVIMMAARPGRVVEDIPIREPF 243
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTAVAAIHDLDlaarycdELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-233 |
1.80e-17 |
|
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: 77.86 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 25 EVLSAEKIysNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLW-----RRDSREKAQHPLSFV 99
Cdd:cd03215 3 PVLEVRGL--SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 100 ----FQEAtLMPWSSVRNNVrlpldlagvpraegntrvsevlelvglgkfadVLPRELSGGMQMRVSIARGLVTRPKLLL 175
Cdd:cd03215 81 pedrKREG-LVLDLSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 176 MDEP-----FGALDEITRnkldsdLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRV 233
Cdd:cd03215 128 LDEPtrgvdVGAKAEIYR------LIRELADAGKAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
38-234 |
2.03e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDS--REKAQHPlsfvfQEATLMP 107
Cdd:PRK10575 24 RTLLhPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdaqplesWSSKAfaRKVAYLP-----QQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 WSSVRNNV---RLPLDLA-GVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK10575 99 GMTVRELVaigRYPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 184 DEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVImmAARPGRVV 234
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLV--ALRGGEMI 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
40-226 |
3.49e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 40 LLPVN---LTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQHPLSFVFQEATLMPWSSV 111
Cdd:PRK11300 18 LLAVNnvnLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpGHQIARMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 RNNVRLP-------------LDLAGVPRAEGN--TRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:PRK11300 98 IENLLVAqhqqlktglfsglLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
34-235 |
3.49e-17 |
|
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: 80.92 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 34 SNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSRE------KAQhpLSFVFQEATLMP 107
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytlaslRRQ--VALVSQDVVLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 wSSVRNNVRLPlDLAGVPRAegntRVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:TIGR02203 420 -DTIANNIAYG-RTEQADRA----EIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLWQEQnlTVVFVTH---SIHEAvflsQRVIMMAArpGRVVE 235
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLMQGR--TTLVIAHrlsTIEKA----DRIVVMDD--GRIVE 547
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-256 |
3.67e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.95 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNGT-RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS----------DGK--LMLWRRDSRE 90
Cdd:COG4170 6 IRNLTIEIDTPQGRvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIdlLKLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 91 KAQHPLSFVFQEatlmPWSSVRNNVRLPLDLAGV---PRAEG---------NTRVSEVLELVGLGKFADVL---PRELSG 155
Cdd:COG4170 86 IIGREIAMIFQE----PSSCLDPSAKIGDQLIEAipsWTFKGkwwqrfkwrKKRAIELLHRVGIKDHKDIMnsyPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 156 GMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYC--GQTVE 239
|
250 260
....*....|....*....|....*..
gi 488997434 236 ----DIPIREPF-PRSEA-FRVSPTFS 256
Cdd:COG4170 240 sgptEQILKSPHhPYTKAlLRSMPDFR 266
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-211 |
6.29e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.31 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVE--PSDGKLMLWRRDsrekaqhplsfVFQEATLmpwssvrnn 114
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ-----------FGREASL--------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 vrlpldLAGVPRAEGNTRVSEVLELVGLGKFADVL--PRELSGGMQMRVSIARGLVTRPKLLLMDEpFGA-LDEITRNKL 191
Cdd:COG2401 103 ------IDAIGRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDE-FCShLDRQTAKRV 175
|
170 180
....*....|....*....|
gi 488997434 192 DSDLLRLWQEQNLTVVFVTH 211
Cdd:COG2401 176 ARNLQKLARRAGITLVVATH 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-211 |
6.98e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 16 IPAAATPAIEVLSAEKI-YSNGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwrrdsreKAQ 93
Cdd:COG0488 305 FPPPERLGKKVLELEGLsKSYGDKTLLdDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---------KLG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 94 HPLSFVF--QE-ATLMPWSSVRNNVRlpldlagvpRAEGNTRVSEVLELvgLGKF----ADVL-P-RELSGGMQMRVSIA 164
Cdd:COG0488 376 ETVKIGYfdQHqEELDPDKTVLDELR---------DGAPGGTEQEVRGY--LGRFlfsgDDAFkPvGVLSGGEKARLALA 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488997434 165 RGLVTRPKLLLMDEPFGALDEITRNKLDsDLLRLWQEqnlTVVFVTH 211
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALE-EALDDFPG---TVLLVSH 487
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
39-235 |
7.18e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 39 ALLPVNLTINQGEFITLLGPSGCGKST----LLKMVA--GLVEPSDGKLMLWRRDSREKAQHPLSFVFQEatlmPWSSV- 111
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQD----PNSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 112 -RNNVR------LPLDLAGVPRAEGNTRVSEVLELVGLGKFA-DVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK15134 377 pRLNVLqiieegLRVHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 184 DEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVE 235
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL--RQGEVVE 506
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-227 |
7.32e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 80.44 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 22 PAIEVLSAEKIYS-NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD---SREKAQHPLS 97
Cdd:TIGR01257 927 PGVCVKNLVKIFEpSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDietNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 98 FVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 178 EPFGALDEITRNKLdSDLLrLWQEQNLTVVFVTHSIHEAVFLSQRVIMMA 227
Cdd:TIGR01257 1087 EPTSGVDPYSRRSI-WDLL-LKYRSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
33-235 |
1.06e-16 |
|
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: 76.89 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEATLMPw 108
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLrraiGVVPQDTVLFN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLpldlagvpraeGNTRVSEVlELVGLGKFADVLPR-----------------ELSGGMQMRVSIARGLVTRP 171
Cdd:cd03253 89 DTIGYNIRY-----------GRPDATDE-EVIEAAKAAQIHDKimrfpdgydtivgerglKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 172 KLLLMDEPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTHSIHEAVFlSQRVIMMaaRPGRVVE 235
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVL--KDGRIVE 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-254 |
1.25e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 26 VLSAE--KIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLK---MVAGLVEP--SDGKLMLWRRDSREKAQHP--- 95
Cdd:PRK14243 10 VLRTEnlNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKNLYAPDVDPvev 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 96 ---LSFVFQEATLMPwSSVRNNVrlpldlAGVPRAEGNTrvSEVLELVGLGKFADVLPRE-----------LSGGMQMRV 161
Cdd:PRK14243 90 rrrIGMVFQKPNPFP-KSIYDNI------AYGARINGYK--GDMDELVERSLRQAALWDEvkdklkqsglsLSGGQQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 162 SIARGLVTRPKLLLMDEPFGALDEITRNKLDsDLLRLWQEQnLTVVFVTHSIHEA-------VFLSQRVIMMAARPGRVV 234
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIE-ELMHELKEQ-YTIIIVTHNMQQAarvsdmtAFFNVELTEGGGRYGYLV 238
|
250 260
....*....|....*....|
gi 488997434 235 EdipirepFPRSEAFRVSPT 254
Cdd:PRK14243 239 E-------FDRTEKIFNSPQ 251
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-212 |
1.58e-16 |
|
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: 74.88 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKL-MLWRRDSREKAQHPLsfvfqeatlMPWSSVRN 113
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLPQRPY---------LPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 114 NVRLPLDlagvpraegntrvsevlelvglgkfadvlpRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKlds 193
Cdd:cd03223 83 QLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR--- 129
|
170
....*....|....*....
gi 488997434 194 dLLRLWQEQNLTVVFVTHS 212
Cdd:cd03223 130 -LYQLLKELGITVISVGHR 147
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-243 |
1.84e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.06 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 19 AATPAIEVLSAEKIYSnGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKM-------VAGLVEPSD----GKLMLWRRD 87
Cdd:PRK14271 17 AAAPAMAAVNLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSGDvllgGRSIFNYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 88 SREkAQHPLSFVFQEATLMPWSsVRNNVrlpldLAGV------PRAEGNTRVSEVLELVGL-----GKFADVlPRELSGG 156
Cdd:PRK14271 96 VLE-FRRRVGMLFQRPNPFPMS-IMDNV-----LAGVrahklvPRKEFRGVAQARLTEVGLwdavkDRLSDS-PFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 157 MQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLwqEQNLTVVFVTHSIHEAVFLSQRVIMMAarPGRVVED 236
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFF--DGRLVEE 243
|
....*..
gi 488997434 237 IPIREPF 243
Cdd:PRK14271 244 GPTEQLF 250
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
43-187 |
2.53e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.37 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD---SREKAQHPLSFVFQEATLMPWSSVRNNVRLPL 119
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkDLCTYQKQLCFVGHRSGINPYLTLRENCLYDI 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 120 DLAgvpraEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEIT 187
Cdd:PRK13540 100 HFS-----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-211 |
3.47e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRaLLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVePSDGKLMLWRRD-----SREKAQHPLSFVFQE--ATLMPw 108
Cdd:PRK03695 9 STR-LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPleawsAAELARHRAYLSQQQtpPFAMP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 ssvrnnVRLPLDL---AGVPRAEGNTRVSEVLELVGLGkfaDVLPR---ELSGGMQMRVSIA-------RGLVTRPKLLL 175
Cdd:PRK03695 86 ------VFQYLTLhqpDKTRTEAVASALNEVAEALGLD---DKLGRsvnQLSGGEWQRVRLAavvlqvwPDINPAGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 488997434 176 MDEPFGALDEITRNKLDSdLLRLWQEQNLTVVFVTH 211
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDR-LLSELCQQGIAVVMSSH 191
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
47-226 |
7.72e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 47 INQGEFITLLGPSGCGKSTLLKMVAGLVEPSD--GKLMLWRRDSREKAQHPLSFVFQEATLMPWSSVRNNV------RLP 118
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLvfcsllRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 119 LDLAgvprAEGNTRVSE-VLELVGLGK-----FADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLD 192
Cdd:PLN03211 171 KSLT----KQEKILVAEsVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190
....*....|....*....|....*....|....
gi 488997434 193 SDLLRLWQEQNLTVVfvthSIHEAvflSQRVIMM 226
Cdd:PLN03211 247 LTLGSLAQKGKTIVT----SMHQP---SSRVYQM 273
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
33-214 |
9.22e-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: 74.29 E-value: 9.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMlWR---------RDSREKAQHPLSFVFQEa 103
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-WSnknesepsfEATRSRNRYSVAYAAQK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 104 tlmPW---SSVRNNVRLpldlaGVPRaeGNTRVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVT 169
Cdd:cd03290 88 ---PWllnATVEENITF-----GSPF--NKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488997434 170 RPKLLLMDEPFGALD-EITRNKLDSDLLRLWQEQNLTVVFVTHSIH 214
Cdd:cd03290 158 NTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-265 |
1.51e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.28 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKS-TLLKMVAGLVEPS----------DGKLMLW--RRDSREKAQHPLSFVFQE--ATLMP 107
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypsgdirfHGESLLHasEQTLRGVRGNKIAMIFQEpmVSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 WSSVRNNVRLPLDL-AGVPRAEGNTRVSEVLELVGLGKFADVL---PRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK15134 108 LHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 184 DEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDipirepfPRSEAFRVSPTFSlYARQLQ 263
Cdd:PRK15134 188 DVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--QNGRCVEQ-------NRAATLFSAPTHP-YTQKLL 257
|
..
gi 488997434 264 DS 265
Cdd:PRK15134 258 NS 259
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
43-235 |
1.67e-15 |
|
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: 73.30 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----WRRDSREKAQHPLSFVFQEATLMPwSSVRNNvrlp 118
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdISKIGLHDLRSRISIIPQDPVLFS-GTIRSN---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 119 LDlagvPRAE-GNTRVSEVLELVGLGKFADVLP-----------RELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEI 186
Cdd:cd03244 98 LD----PFGEySDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 187 TrnklDSDLLRLWQEQ--NLTVVFVTHSIHeAVFLSQRVIMMAArpGRVVE 235
Cdd:cd03244 174 T----DALIQKTIREAfkDCTVLTIAHRLD-TIIDSDRILVLDK--GRVVE 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-227 |
1.77e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.89 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 25 EVLSAEKIY-------SNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlWRRDSREKAQHP-- 95
Cdd:PRK13631 20 IILRVKNLYcvfdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI--QVGDIYIGDKKNnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 96 --------------------LSFVFQ--EATLMPwSSVRNNVRL-PLDLaGVPRAEGNTRVSEVLELVGLGK-FADVLPR 151
Cdd:PRK13631 98 elitnpyskkiknfkelrrrVSMVFQfpEYQLFK-DTIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLDDsYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 152 ELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD-----EITRNKLDSdllrlwQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgehEMMQLILDA------KANNKTVFVITHTMEHVLEVADEVIVM 249
|
.
gi 488997434 227 A 227
Cdd:PRK13631 250 D 250
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
36-241 |
2.24e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.60 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGlVEPS---------DGKLMLWR--RDSREKAqhpLSFVFQEAT 104
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyegeilfDGEVCRFKdiRDSEALG---IVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPWSSVRNNVRLpldlaGVPRAEG--------NTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:NF040905 89 LIPYLSIAENIFL-----GNERAKRgvidwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488997434 177 DEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIRE 241
Cdd:NF040905 164 DEPTAALNEEDSAAL-LDLLLELKAQGITSIIISHKLNEIRRVADSITVL--RDGRTIETLDCRA 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
36-240 |
3.10e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.25 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGlVEPS---DGKLM-----LWRRDSREKAQHPLSFVFQEATLMP 107
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYwsgspLKASNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 WSSVRNNVRL--PLDLAG--VPRAEGNTRVSEVLELVGLGKFADVLP-RELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:TIGR02633 92 ELSVAENIFLgnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 183 LDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIR 240
Cdd:TIGR02633 172 LTEKETEIL-LDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI--RDGQHVATKDMS 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
47-234 |
4.43e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 47 INQGEFITLLGPSGCGKSTLLKMVAGLVEPS---DGKLML-WRRDSREKAQHPLSFVFQEATLMPWSSVRNN------VR 116
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLnGMPIDAKEMRAISAYVQQDDLFIPTLTVREHlmfqahLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 117 LPLDLAGVPRAEgntRVSEVLELVGLGKFADVL------PRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNK 190
Cdd:TIGR00955 128 MPRRVTKKEKRE---RVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488997434 191 LDSDLLRLWQEQNLTVVfvthSIH----EAVFLSQRVIMMAArpGRVV 234
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIIC----TIHqpssELFELFDKIILMAE--GRVA 246
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
38-222 |
4.77e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrDSREKAQHPLSFVFQEA-TLMPWSS---VRN 113
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF---DGKDITDWQTAKIMREAvAIVPEGRrvfSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 114 NVRLPLDLAG--VPRAEGNTRVSEVLELvglgkFADVLPRE------LSGGMQMRVSIARGLVTRPKLLLMDEPFGALDE 185
Cdd:PRK11614 96 TVEENLAMGGffAERDQFQERIKWVYEL-----FPRLHERRiqragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 488997434 186 ITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQR 222
Cdd:PRK11614 171 IIIQQI-FDTIEQLREQGMTIFLVEQNANQALKLADR 206
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
43-234 |
5.80e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSREKAQHpLSFVFQEATLMPWSSVRNNV-- 115
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiQHYASKEVARR-IGLLAQNATTPGDITVQELVar 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 -RLPLD-LAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD---EITRNK 190
Cdd:PRK10253 105 gRYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishQIDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488997434 191 LDSDLLRlwqEQNLTVVFVTHSIHEAVFLSQRVImmAARPGRVV 234
Cdd:PRK10253 185 LLSELNR---EKGYTLAAVLHDLNQACRYASHLI--ALREGKIV 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-241 |
8.87e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 12 DTRFIPAAATPAIEVLSAEKIysNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRR 86
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGL--SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdgkpvRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 87 DSREKAQHPLSFV----FQEAtLMPWSSVRNNVRLP-LDLAG----VPRAEGNTRVSEVLELVGLgKFADV--LPRELSG 155
Cdd:COG1129 320 SPRDAIRAGIAYVpedrKGEG-LVLDLSIRENITLAsLDRLSrgglLDRRRERALAEEYIKRLRI-KTPSPeqPVGNLSG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 156 GMQMRVSIARGLVTRPKLLLMDEPF-----GALDEITRnkldsdLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRP 230
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTrgidvGAKAEIYR------LIRELAAEGKAVIVISSELPELLGLSDRILVM--RE 469
|
250
....*....|.
gi 488997434 231 GRVVEDIPIRE 241
Cdd:COG1129 470 GRIVGELDREE 480
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
39-243 |
1.08e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 39 ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKL----MLWRRDSRE----------KAQH----PLSFVF 100
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkMLLRRRSRQvielseqsaaQMRHvrgaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 101 QE--ATLMPWSSVRNNVRLPLDL-AGVPRAEGNTRVSEVLELVGLGKFADVL---PRELSGGMQMRVSIARGLVTRPKLL 174
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILsryPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 175 LMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF 243
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ--GEAVETGSVEQIF 257
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-213 |
1.19e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 19 AATPAIEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPLSF 98
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 99 VFQEATLMPWSS---VRNNVRLP----LDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRP 171
Cdd:PRK15056 82 YVPQSEEVDWSFpvlVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488997434 172 KLLLMDEPFGALDEITRNKLDSdLLRLWQEQNLTVVFVTHSI 213
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIIS-LLRELRDEGKTMLVSTHNL 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-211 |
1.85e-14 |
|
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: 70.25 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEkiySNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGL--VEPSDGKLMLWRRD-----SREKAQHPL 96
Cdd:cd03217 3 IKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlpPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 SFVFQEatlmpwssvrnnvrlPLDLAGVpraegntRVSEVLELVGLGkfadvlpreLSGGMQMRVSIARGLVTRPKLLLM 176
Cdd:cd03217 80 FLAFQY---------------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190
....*....|....*....|....*....|....*
gi 488997434 177 DEPFGALDeITRNKLDSDLLRLWQEQNLTVVFVTH 211
Cdd:cd03217 129 DEPDSGLD-IDALRLVAEVINKLREEGKSVLIITH 162
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
44-243 |
2.16e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 44 NLTINQGEFITLLGPSGCGKS----TLLKMVA--GLVEPS---DGKLML---WRRDSREKAQHpLSFVFQE--ATLMPWS 109
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRIGGSatfNGREILnlpEKELNKLRAEQ-ISMIFQDpmTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNNVRLPLDL-AGVPRAEGNTRVSEVLELVGLG---KFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDE 185
Cdd:PRK09473 115 RVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPearKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 186 ITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPF 243
Cdd:PRK09473 195 TVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA--GRTMEYGNARDVF 250
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-184 |
2.38e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 17 PAAATPAIEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSR--EKAQH 94
Cdd:PRK13543 4 PLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrgDRSRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 pLSFVFQEATLMPWSSVRNNVRLpldLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLL 174
Cdd:PRK13543 84 -MAYLGHLPGLKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|
gi 488997434 175 LMDEPFGALD 184
Cdd:PRK13543 160 LLDEPYANLD 169
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
36-213 |
3.87e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 70.66 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwRRDSRekaqhpLSFVFQEATLMPwSSVRNNV 115
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGR------ISFSSQFSWIMP-GTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 rlpldLAGVPRAEgnTRVSEVLELVGL----GKFAD----VLPR---ELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:cd03291 119 -----IFGVSYDE--YRYKSVVKACQLeediTKFPEkdntVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190
....*....|....*....|....*....|
gi 488997434 185 EITRNKL-DSDLLRLWqeQNLTVVFVTHSI 213
Cdd:cd03291 192 VFTEKEIfESCVCKLM--ANKTRILVTSKM 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
45-211 |
4.05e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 45 LTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwRRD---SREKaQHP--------LSFV---FQEAT------ 104
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDlivARLQ-QDPprnvegtvYDFVaegIEEQAeylkry 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 ------LMPWSSVRNNVRLP-----LDLAGVPRAEgnTRVSEVLELVGLGkfADVLPRELSGGMQMRVSIARGLVTRPKL 173
Cdd:PRK11147 102 hdishlVETDPSEKNLNELAklqeqLDHHNLWQLE--NRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488997434 174 LLMDEPfgaldeitRNKLDSDLLRlWQEQNL-----TVVFVTH 211
Cdd:PRK11147 178 LLLDEP--------TNHLDIETIE-WLEGFLktfqgSIIFISH 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-215 |
5.43e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGlVEPS---DGKLmLWR---------RDSREKAqhpLSFVFQE 102
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEI-IFEgeelqasniRDTERAG---IAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 103 ATLMPWSSVRNNVRLPLDL--AGVPR-AEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:PRK13549 91 LALVKELSVLENIFLGNEItpGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 488997434 180 FGALDEI-TRNKLdsDLLRLWQEQNLTVVFVTHSIHE 215
Cdd:PRK13549 171 TASLTESeTAVLL--DIIRDLKAHGIACIYISHKLNE 205
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-235 |
6.67e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.15 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML----WRRDSREKAQHPLSFVFQEATLMPw 108
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdIRTVTRASLRRNIAVVFQDAGLFN- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLpldlaGVPRA-----EGNTRVSEVLELV-----GLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDE 178
Cdd:PRK13657 423 RSIEDNIRV-----GRPDAtdeemRAAAERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 179 PFGALDEITRNKLDSDLLRLwqEQNLTVVFVTH---SIHEAvflsQRVIMMAArpGRVVE 235
Cdd:PRK13657 498 ATSALDVETEAKVKAALDEL--MKGRTTFIIAHrlsTVRNA----DRILVFDN--GRVVE 549
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
36-191 |
7.33e-14 |
|
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: 71.48 E-value: 7.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwRRDSRekaqhpLSFVFQEATLMPwSSVRNNV 115
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KHSGR------ISFSPQTSWIMP-GTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 rlpldLAGVPRAEgnTRVSEVLELVGLGKFADVLPRE-----------LSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:TIGR01271 508 -----IFGLSYDE--YRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
....*..
gi 488997434 185 EITRNKL 191
Cdd:TIGR01271 581 VVTEKEI 587
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-234 |
5.22e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 68.62 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 27 LSAEKI---YSNGTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------WRRDSRekAQH- 94
Cdd:COG4618 331 LSVENLtvvPPGSKRPILrGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqWDREEL--GRHi 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 ---PlsfvfQEATLMPwSSVRNNV-RLP-LD---------LAGV-------PraEG-NTRVSEvlelVGLGkfadvlpre 152
Cdd:COG4618 409 gylP-----QDVELFD-GTIAENIaRFGdADpekvvaaakLAGVhemilrlP--DGyDTRIGE----GGAR--------- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 153 LSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHeAVFLSQRVIMMaaRPGR 232
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL-AAAIRALKARGATVVVITHRPS-LLAAVDKLLVL--RDGR 543
|
..
gi 488997434 233 VV 234
Cdd:COG4618 544 VQ 545
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
37-214 |
5.91e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPV----NLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEATLMPw 108
Cdd:TIGR00958 490 NRPDVPVlkglTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLhrqvALVGQEPVLFS- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLPLDLAgvPRAEgntrVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLMD 177
Cdd:TIGR00958 569 GSVRENIAYGLTDT--PDEE----IMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190
....*....|....*....|....*....|....*....
gi 488997434 178 EPFGALD-EITRnkldsdLLRLWQE-QNLTVVFVTHSIH 214
Cdd:TIGR00958 643 EATSALDaECEQ------LLQESRSrASRTVLLIAHRLS 675
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
37-213 |
6.48e-13 |
|
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: 66.34 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrDSREKAQHP-------LSFVFQEATLMPwS 109
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DGKPISQYEhkylhskVSLVGQEPVLFA-R 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNNVrlPLDLAGVPraegNTRVSEVLELVGLGKFADVLPRE-----------LSGGMQMRVSIARGLVTRPKLLLMDE 178
Cdd:cd03248 103 SLQDNI--AYGLQSCS----FECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190
....*....|....*....|....*....|....*
gi 488997434 179 PFGALDEITRNKLDSdLLRLWQEqNLTVVFVTHSI 213
Cdd:cd03248 177 ATSALDAESEQQVQQ-ALYDWPE-RRTVLVIAHRL 209
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
40-187 |
1.61e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.98 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 40 LLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS---DGKLMLWRRDSREKAQHP---LSFVFQEATLMPWSSVRN 113
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYpgeIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 114 NvrlpLDLAGvpRAEGNTRVsevlelvglgkfadvlpRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEIT 187
Cdd:cd03233 103 T----LDFAL--RCKGNEFV-----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-241 |
1.78e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.36 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYSNG-TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS-----------DGKLM-LWRRDSRE 90
Cdd:PRK15093 6 IRNLTIEFKTSDGwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtadrmrfdDIDLLrLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 91 KAQHPLSFVFQEatlmPWSSVRNNVRLPLDLA-GVPR--AEG---------NTRVSEVLELVGLGKFADVL---PRELSG 155
Cdd:PRK15093 86 LVGHNVSMIFQE----PQSCLDPSERVGRQLMqNIPGwtYKGrwwqrfgwrKRRAIELLHRVGIKDHKDAMrsfPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 156 GMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVE 235
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYC--GQTVE 239
|
....*.
gi 488997434 236 DIPIRE 241
Cdd:PRK15093 240 TAPSKE 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-238 |
1.92e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR-----DSREKAQHPLSFVFQEATLMPWSS 110
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaSTTAALAAGVAIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNV---RLPLDLAGVPRAEGNTRVSEVLELVGLgkfaDVLP----RELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK11288 96 VAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGV----DIDPdtplKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 184 D--EITRnkldsdLLRLWQE---QNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIP 238
Cdd:PRK11288 172 SarEIEQ------LFRVIRElraEGRVILYVSHRMEEIFALCDAITVF--KDGRYVATFD 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-276 |
2.67e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.89 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrdsrekaQHPLSFVFQEATLMPwSSVRNNVrlpldLA 122
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM---------KGSVAYVPQQAWIQN-DSLRENI-----LF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 123 GVPRAEgnTRVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD-EITRNK 190
Cdd:TIGR00957 722 GKALNE--KYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDaHVGKHI 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 191 LDSDLLRLWQEQNLTVVFVTHSIHeavFLSQRVIMMAARPGRVVEDIPIREPFPRSEAFrvSPTFSLYARQLQDSLLQAS 270
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGIS---YLPQVDVIIVMSGGKISEMGSYQELLQRDGAF--AEFLRTYAPDEQQGHLEDS 874
|
....*.
gi 488997434 271 QSGMES 276
Cdd:TIGR00957 875 WTALVS 880
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-226 |
3.54e-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: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 13 TRFIPAAATPAIEVLSAekiysnGTRAllpvnltinqGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD---SR 89
Cdd:TIGR01257 1944 TKVYSGTSSPAVDRLCV------GVRP----------GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 90 EKAQHPLSFVFQEATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVT 169
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 170 RPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNlTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
39-249 |
4.24e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.45 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 39 ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwrrdsreKAQHPLSFVFQEATLMPWSSVRNNVRLP 118
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---------DRNGEVSVIAISAGLSGQLTGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 119 LDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDE-ITRNKLDSdlLR 197
Cdd:PRK13546 110 MLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQtFAQKCLDK--IY 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488997434 198 LWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFPRSEAF 249
Cdd:PRK13546 188 EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEG--GKLKDYGELDDVLPKYEAF 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
36-241 |
4.81e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRD-----SREKAQHPLSFVFQEATLMPWSS 110
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksSKEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNV---RLPLDLAGVPRAEGNTRVSEVLELVGLgkfaDVLPRE----LS-GGMQMrVSIARGLVTRPKLLLMDEPFGA 182
Cdd:PRK10982 90 VMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDI----DIDPRAkvatLSvSQMQM-IEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 183 LDEITRNKLDSDLLRLwQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIPIRE 241
Cdd:PRK10982 165 LTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL--RDGQWIATQPLAG 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
43-242 |
7.87e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-------------WRRDSREKAQHPLSFVfqeatlmpwS 109
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnlkdinlkwWRSKIGVVSQDPLLFS---------N 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNNVRLPL---------------------------------------------DLAGVPRAEGNTRVSEVLELVGLGK 144
Cdd:PTZ00265 475 SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKDSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 145 ------FADVLP-----------RELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVV 207
Cdd:PTZ00265 555 kvlihdFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250 260 270
....*....|....*....|....*....|....*..
gi 488997434 208 FVTHSIhEAVFLSQRVIMMAARP--GRVVEDIPIREP 242
Cdd:PTZ00265 635 IIAHRL-STIRYANTIFVLSNRErgSTVDVDIIGEDP 670
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-211 |
2.03e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlWRRDSREkaqhpLSFVFQEATLMPWSS 110
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA--RPQPGIK-----VGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPL--------------DLAGVPRAEGN------TRVSEVLELVG-------LGKFADVL--P------RELSG 155
Cdd:TIGR03719 85 VRENVEEGVaeikdaldrfneisAKYAEPDADFDklaaeqAELQEIIDAADawdldsqLEIAMDALrcPpwdadvTKLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488997434 156 GMQMRVSIARGLVTRPKLLLMDEPfgaldeitRNKLDSDLLrLWQEQNL-----TVVFVTH 211
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEP--------TNHLDAESV-AWLERHLqeypgTVVAVTH 216
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
39-215 |
2.23e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 39 ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwrrDSRekaqhplsfvfQEATLMPWSSVRN----- 113
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIK-----------GSAALIAISSGLNgqltg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 114 --NVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL 191
Cdd:PRK13545 103 ieNIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180
....*....|....*....|....
gi 488997434 192 dSDLLRLWQEQNLTVVFVTHSIHE 215
Cdd:PRK13545 183 -LDKMNEFKEQGKTIFFISHSLSQ 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
16-274 |
2.29e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.22 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 16 IPAAATPAIEVLSAEKIYSNgTRALLPVNLTINQGEFITLLGPSGCG--KSTLLKMVAGlvePSDGK----LMLW---RR 86
Cdd:NF000106 6 ISNGARNAVEVRGLVKHFGE-VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpwrF*TWcanRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 87 DSREK--AQHPLSFVFQEATlmpwsSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIA 164
Cdd:NF000106 82 ALRRTig*HRPVR*GRRESF-----SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 165 RGLVTRPKLLLMDEPFGALDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAArpGRVVEDIPIREPFP 244
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEV-WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDR--GRVIADGKVDELKT 233
|
250 260 270
....*....|....*....|....*....|..
gi 488997434 245 R--SEAFRVSPTFSLYARQLQDSLLQASQSGM 274
Cdd:NF000106 234 KvgGRTLQIRPAHAAELDRMVGAIAQAGLDGI 265
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-227 |
2.38e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSRE---KAQHPLSFVF-----QEATLMPWSSVRNN 114
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstAQRLARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 V------RLPLDLAGvpraegnTRVSEVLELV--GLG-KF--ADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK15439 362 VcalthnRRGFWIKP-------ARENAVLERYrrALNiKFnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488997434 184 DEITRNKLdSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMA 227
Cdd:PRK15439 435 DVSARNDI-YQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMH 477
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
43-235 |
5.01e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.24 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGL--VEPSDGKLML-------WRRDSREKA------QHPLSFvfqeatlmP 107
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLdgedileLSPDERARAgiflafQYPVEI--------P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 WSSVR-------NNVRLPLdlagVPRAEGNTRVSEVLELVGLGKfaDVLPREL----SGGMQMRVSIARGLVTRPKLLLM 176
Cdd:COG0396 91 GVSVSnflrtalNARRGEE----LSAREFLKLLKEKMKELGLDE--DFLDRYVnegfSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 177 DEPFGALDeitrnkLD-----SDLLRLWQEQNLTVVFVTHsiheavflSQR---------VIMMAArpGRVVE 235
Cdd:COG0396 165 DETDSGLD------IDalrivAEGVNKLRSPDRGILIITH--------YQRildyikpdfVHVLVD--GRIVK 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-179 |
5.16e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.83 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLM-----LWRRDSREKAQHPLSFVFQ------EATL 105
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARHRRAVCPRIAYMPQglgknlYPTL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 106 mpwsSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:NF033858 94 ----SVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
153-248 |
5.85e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 153 LSGGMQMRVSIARGLVTRPKLLLMDEP-----FGALDEITrnkldsDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMa 227
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPtrgvdVGAKKEIY------QLINQFKAEGLSIILVSSEMPEVLGMSDRILVM- 468
|
90 100
....*....|....*....|.
gi 488997434 228 aRPGRvvedipIREPFPRSEA 248
Cdd:PRK10762 469 -HEGR------ISGEFTREQA 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
50-184 |
6.48e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 50 GEFITLLGPSGCGKSTLLKMVAGLVEP---SDGKLMLWRRDSREKAQHPLSFVFQEATLMPWSSVRNNVRLPLDL---AG 123
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqpKS 868
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 124 VPRAEGNTRVSEVLELVGLGKFADVL---PRE-LSGGMQMRVSIARGLVTRPKLLL-MDEPFGALD 184
Cdd:TIGR00956 869 VSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
38-235 |
1.86e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.96 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSR----EKAQHPLSFVFQEATLMPwSSVRN 113
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiplEDLRSSLTIIPQDPTLFS-GTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 114 NVRlPLDLAGVPRAEGNTRVSEVlelvGLgkfadvlprELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITrnklDS 193
Cdd:cd03369 101 NLD-PFDEYSDEEIYGALRVSEG----GL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT----DA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488997434 194 DLLRLWQE--QNLTVVFVTHSIHeAVFLSQRVIMMAArpGRVVE 235
Cdd:cd03369 163 LIQKTIREefTNSTILTIAHRLR-TIIDYDKILVMDA--GEVKE 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-232 |
4.46e-10 |
|
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: 59.80 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 46 TINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwrrDSREKaqhpLSFVFQEatLMPWSSVRnnVRLPLDLAGVP 125
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLK----ISYKPQY--ISPDYDGT--VEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 126 RAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLT 205
Cdd:COG1245 429 DFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
170 180
....*....|....*....|....*..
gi 488997434 206 VVFVTHSIHEAVFLSQRVIMMAARPGR 232
Cdd:COG1245 509 AMVVDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-232 |
4.80e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 46 TINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwrrDSREKaqhpLSFVFQEatlmpwssVRNNVRLPLD--LAG 123
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----DPELK----ISYKPQY--------IKPDYDGTVEdlLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 124 VPRAEGNTRV-SEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQ 202
Cdd:PRK13409 424 ITDDLGSSYYkSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170 180 190
....*....|....*....|....*....|
gi 488997434 203 NLTVVFVTHSIHEAVFLSQRVIMMAARPGR 232
Cdd:PRK13409 504 EATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
43-214 |
1.69e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlWrrdsrekAQHPLSFVFQEATLMPwSSVRNNVrLPLDLA 122
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--W-------AERSIAYVPQQAWIMN-ATVRGNI-LFFDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 123 GVPRAEGNTRVSEV---LELVGLGKFADVLPR--ELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLr 197
Cdd:PTZ00243 748 DAARLADAVRVSQLeadLAQLGGGLETEIGEKgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF- 826
|
170
....*....|....*..
gi 488997434 198 LWQEQNLTVVFVTHSIH 214
Cdd:PTZ00243 827 LGALAGKTRVLATHQVH 843
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
38-251 |
1.80e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.14 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAG-LVEPSD-------GKLMLwrrDSREKAQHPLSFVFQEATLMPWS 109
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTL---NGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRN---NVRLPLDLAGVP--RAEGNTR------VSEVLELVGlgkfADVLPRE----LSGGMQMRVSIARGL------- 167
Cdd:PRK13547 92 AQPAfafSAREIVLLGRYPhaRRAGALThrdgeiAWQALALAG----ATALVGRdvttLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 168 --VTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMAarPGRVVEDIPIR----- 240
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA--DGAIVAHGAPAdvltp 245
|
250
....*....|.
gi 488997434 241 EPFPRSEAFRV 251
Cdd:PRK13547 246 AHIARCYGFAV 256
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
33-214 |
2.90e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRR----DSREKAQHPLSFVFQEATLmpW 108
Cdd:PRK10522 332 YQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvtaEQPEDYRKLFSAVFTDFHL--F 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 109 SSVRNNVRLPLDLAGVPRAEGNTRVSEVLELVGlGKFADVlprELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITR 188
Cdd:PRK10522 410 DQLLGPEGKPANPALVEKWLERLKMAHKLELED-GRISNL---KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180
....*....|....*....|....*.
gi 488997434 189 NKLDSDLLRLWQEQNLTVVFVTHSIH 214
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHDDH 511
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-215 |
3.29e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-WRRDSR---EKAQHPLSFVFQeatlmpwssvR 112
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSqFSHITRlsfEQLQKLVSDEWQ----------R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNVRL---PLDLAGVPRAE-------GNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:PRK10938 86 NNTDMlspGEDDTGRTTAEiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190
....*....|....*....|....*....|...
gi 488997434 183 LDEITRNKLdSDLLRLWQEQNLTVVFVTHSIHE 215
Cdd:PRK10938 166 LDVASRQQL-AELLASLHQSGITLVLVLNRFDE 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-211 |
3.46e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 26 VLSAEKIySNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML---WRrdsrekaqhpLSFVFQ 101
Cdd:PRK10636 3 VFSSLQI-RRGVRVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnWQ----------LAWVNQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 102 EATLMPWSSV-------RNNVRLPLDLAGV-PRAEGN------------------TRVSEVLElvGLGKFADVLPR---E 152
Cdd:PRK10636 72 ETPALPQPALeyvidgdREYRQLEAQLHDAnERNDGHaiatihgkldaidawtirSRAASLLH--GLGFSNEQLERpvsD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 153 LSGGMQMRVSIARGLVTRPKLLLMDEPfgaldeitRNKLDSDLLrLWQEQNL-----TVVFVTH 211
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEP--------TNHLDLDAV-IWLEKWLksyqgTLILISH 204
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
47-231 |
3.66e-09 |
|
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: 54.89 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 47 INQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPlsfvfqeatlmpwssvrnnvrlpldlagvpr 126
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 127 aegntrvsevlelvglgkfadvlprELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRLWQEQNLTV 206
Cdd:cd03222 71 -------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|....*
gi 488997434 207 VFVTHSIHEAVFLSQRVIMMAARPG 231
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-235 |
5.94e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrDSRekaqhPLS------------FVF 100
Cdd:PRK10790 350 YRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL---DGR-----PLSslshsvlrqgvaMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 101 QEATLMPwSSVRNNVRLPLDLAgvpraegNTRVSEVLELVGLGKFADVLP-----------RELSGGMQMRVSIARGLVT 169
Cdd:PRK10790 422 QDPVVLA-DTFLANVTLGRDIS-------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 170 RPKLLLMDEPFGALDEITRNKLDSdLLRLWQEQNlTVVFVTH---SIHEAvflsqRVIMMAARpGRVVE 235
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQ-ALAAVREHT-TLVVIAHrlsTIVEA-----DTILVLHR-GQAVE 554
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
49-226 |
9.28e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 49 QGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrdsrekaqhplsfvfqeatlmpwssvrnnvrlpLDLagvprae 128
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------IDG------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 129 gnTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKL-----DSDLLRLWQEQN 203
Cdd:smart00382 39 --EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLLLKSEKN 116
|
170 180
....*....|....*....|....*...
gi 488997434 204 LTVVFVTHSI-----HEAVFLSQRVIMM 226
Cdd:smart00382 117 LTVILTTNDEkdlgpALLRRRFDRRIVL 144
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
44-211 |
1.87e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 44 NLTINQGEFITLLGPSGCGKSTLLKMVAGlvepsD------GKLMLW--RRDSREK----AQHpLSFVFQEATL--MPWS 109
Cdd:PRK10938 280 SWQVNPGEHWQIVGPNGAGKSTLLSLITG-----DhpqgysNDLTLFgrRRGSGETiwdiKKH-IGYVSSSLHLdyRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 110 SVRNnVRLP--LDLAGVPRAEGNTR---VSEVLELVGLGK-FADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGAL 183
Cdd:PRK10938 354 SVRN-VILSgfFDSIGIYQAVSDRQqklAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGL 432
|
170 180 190
....*....|....*....|....*....|...
gi 488997434 184 DEITRNkldsdLLRLWQEQNLT-----VVFVTH 211
Cdd:PRK10938 433 DPLNRQ-----LVRRFVDVLISegetqLLFVSH 460
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
39-211 |
1.95e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.72 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 39 ALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDG------------KLMLWRRDSREKAQHPlsFVFQEatlm 106
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGdirfhdipltklQLDSWRSRLAVVSQTP--FLFSD---- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 pwsSVRNNVRLpldlaGVPRAegntrVSEVLELVglGKFADV------LPR-----------ELSGGMQMRVSIARGLVT 169
Cdd:PRK10789 404 ---TVANNIAL-----GRPDA-----TQQEIEHV--ARLASVhddilrLPQgydtevgergvMLSGGQKQRISIARALLL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488997434 170 RPKLLLMDEPFGALDEITRNKLDSDlLRLWQEQNlTVVFVTH 211
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHN-LRQWGEGR-TVIISAH 508
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-211 |
2.28e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 31 KIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGklmlwrrDSREKAQHPLSFVFQEATLMPWSS 110
Cdd:PRK11819 14 KVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIKVGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 111 VRNNVRLPL--------------DLAGVPRAEGN------TRVSEVLELVG-------LGKFADVL---PRE-----LSG 155
Cdd:PRK11819 87 VRENVEEGVaevkaaldrfneiyAAYAEPDADFDalaaeqGELQEIIDAADawdldsqLEIAMDALrcpPWDakvtkLSG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488997434 156 GMQMRVSIARGLVTRPKLLLMDEPfgaldeiTrNKLDSDLLrLWQEQNL-----TVVFVTH 211
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEP-------T-NHLDAESV-AWLEQFLhdypgTVVAVTH 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
33-226 |
2.50e-08 |
|
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: 54.92 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEpSDGKLML----WRRDSREKAQHPLSFVFQEATLMP 107
Cdd:TIGR01271 1227 YTEAGRAVLQdLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIdgvsWNSVTLQTWRKAFGVIPQKVFIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 wssvrNNVRLPLDlagvPRAE-GNTRVSEVLELVGLGKFADVLPREL-----------SGGMQMRVSIARGLVTRPKLLL 175
Cdd:TIGR01271 1306 -----GTFRKNLD----PYEQwSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488997434 176 MDEPFGALDEITRNKLDSDLLRLWqeQNLTVVFVTHSIhEAVFLSQRVIMM 226
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTLKQSF--SNCTVILSEHRV-EALLECQQFLVI 1424
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
43-184 |
2.73e-08 |
|
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: 54.44 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEaTLMPWSSVRNNVRLP 118
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLraaiGIVPQD-TVLFNDTIAYNIAYG 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488997434 119 LdlAGVPRAEgntrVSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:COG5265 456 R--PDASEEE----VEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-238 |
2.89e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 27 LSAEKIYSNGTRAllPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrRDSREKAQHPLSFVFQEATL- 105
Cdd:PRK11288 258 LRLDGLKGPGLRE--PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL--DGKPIDIRSPRDAIRAGIMLc 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 106 ---------MPWSSVRNNV-------RLPLDLAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVT 169
Cdd:PRK11288 334 pedrkaegiIPVHSVADNInisarrhHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488997434 170 RPKLLLMDEP-----FGALDEITrnkldsDLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMMaaRPGRVVEDIP 238
Cdd:PRK11288 414 DMKVILLDEPtrgidVGAKHEIY------NVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM--REGRIAGELA 479
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-215 |
3.80e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 36 GTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGlVEPSDGKLMLWR---------RDSREKAqhpLSFVFQEATLM 106
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG-IYTRDAGSILYLgkevtfngpKSSQEAG---IGIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 107 PWSSVRNNVRLPLD----LAGVPRAEGNTRVSEVLELVGLGKFADVLPRELSGGMQMRVSIARGLVTRPKLLLMDEPFGA 182
Cdd:PRK10762 92 PQLTIAENIFLGREfvnrFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190
....*....|....*....|....*....|...
gi 488997434 183 LDEITRNKLDSdLLRLWQEQNLTVVFVTHSIHE 215
Cdd:PRK10762 172 LTDTETESLFR-VIRELKSQGRGIVYISHRLKE 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-211 |
3.96e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 46 TINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmlwRRDSR-EKA---QHplsfvfqEATLMPWSSVRNNVrlpldl 121
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---HCGTKlEVAyfdQH-------RAELDPEKTVMDNL------ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 122 agvprAEG------NTRVSEVlelvgLGKFADVL--P-------RELSGGMQMRVSIARgLVTRP-KLLLMDEPfgalde 185
Cdd:PRK11147 405 -----AEGkqevmvNGRPRHV-----LGYLQDFLfhPkramtpvKALSGGERNRLLLAR-LFLKPsNLLILDEP------ 467
|
170 180 190
....*....|....*....|....*....|.
gi 488997434 186 itRNKLDSDLLRLWQE-----QNlTVVFVTH 211
Cdd:PRK11147 468 --TNDLDVETLELLEElldsyQG-TVLLVSH 495
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-236 |
4.24e-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: 53.65 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 42 PVNLTINQGE--FITllGPSGCGKSTLLKMVAGLVEPSDGKLML----WRRDSREKAQHPLSFVFQEATLMPwssvrnnv 115
Cdd:COG4615 350 PIDLTIRRGElvFIV--GGNGSGKSTLAKLLTGLYRPESGEILLdgqpVTADNREAYRQLFSAVFSDFHLFD-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 rlplDLAGVPRAEGNTRVSEVLELVGL--------GKFADvlpRELSGGMQMRVsiarGLVTrpkLLLMDEPFGALDE-- 185
Cdd:COG4615 420 ----RLLGLDGEADPARARELLERLELdhkvsvedGRFST---TDLSQGQRKRL----ALLV---ALLEDRPILVFDEwa 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488997434 186 -----ITRNKLDSDLLRLWQEQNLTVVFVTHS---IHEAvflsQRVIMMAArpGRVVED 236
Cdd:COG4615 486 adqdpEFRRVFYTELLPELKARGKTVIAISHDdryFDLA----DRVLKMDY--GKLVEL 538
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
43-226 |
8.22e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEP-SDGKLMLwrRDSreKAQHP-LSFVFQeatlmpwSSVRNNVR--LP 118
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVI--RGT--VAYVPqVSWIFN-------ATVRDNILfgSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 119 LDLAGVPRAEGNTRVSEVLELVGLGKFADVLPR--ELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD-EITRNKLDSDL 195
Cdd:PLN03130 705 FDPERYERAIDVTALQHDLDLLPGGDLTEIGERgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDaHVGRQVFDKCI 784
|
170 180 190
....*....|....*....|....*....|...
gi 488997434 196 LRlwQEQNLTVVFVTHSIHeavFLSQ--RVIMM 226
Cdd:PLN03130 785 KD--ELRGKTRVLVTNQLH---FLSQvdRIILV 812
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-226 |
9.78e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPLSFvfqEATLMPWSSV--RNNVRLPLD 120
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF---KITIIPQDPVlfSGSLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 121 LAGVPRAEgntRVSEVLELVGLGKFADVLP-----------RELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRN 189
Cdd:TIGR00957 1382 PFSQYSDE---EVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
170 180 190
....*....|....*....|....*....|....*..
gi 488997434 190 KLDSDLLRlwQEQNLTVVFVTHSIHeAVFLSQRVIMM 226
Cdd:TIGR00957 1459 LIQSTIRT--QFEDCTVLTIAHRLN-TIMDYTRVIVL 1492
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
35-211 |
1.39e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGlvEPS----DGKLmLWR------RDSREKAQHPLSFVFQeat 104
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDI-LFKgesildLEPEERAHLGIFLAFQ--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 lmpwssvrnnvrLPLDLAGVP-----RAEGNTR-----------------VSEVLELVGLGkfADVLPREL----SGGMQ 158
Cdd:CHL00131 92 ------------YPIEIPGVSnadflRLAYNSKrkfqglpeldplefleiINEKLKLVGMD--PSFLSRNVnegfSGGEK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488997434 159 MRVSIARGLVTRPKLLLMDEPFGALDeITRNKLDSDLLRLWQEQNLTVVFVTH 211
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLD-IDALKIIAEGINKLMTSENSIILITH 209
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-250 |
1.81e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 21 TPAIEV----LSAEKIYSNGTraLLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQhpL 96
Cdd:PLN03232 612 APAISIkngyFSWDSKTSKPT--LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQ--V 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 97 SFVFQeatlmpwSSVRNNVRLPLDLAgvpraegNTRVSEVLELVGLGKFADVLP-REL----------SGGMQMRVSIAR 165
Cdd:PLN03232 688 SWIFN-------ATVRENILFGSDFE-------SERYWRAIDVTALQHDLDLLPgRDLteigergvniSGGQKQRVSMAR 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 166 GLVTRPKLLLMDEPFGALD-EITRNKLDSDLLRlwQEQNLTVVFVTHSIHeavFLSQ--RVIMMAArpGRVVEDIPIREP 242
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDaHVAHQVFDSCMKD--ELKGKTRVLVTNQLH---FLPLmdRIILVSE--GMIKEEGTFAEL 826
|
....*...
gi 488997434 243 FPRSEAFR 250
Cdd:PLN03232 827 SKSGSLFK 834
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-214 |
1.91e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 26 VLSAEKIYSN-GTRALL-PVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREK-AQHPLSFVFQE 102
Cdd:PRK10636 312 LLKMEKVSAGyGDRIILdSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYfAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 103 AtlmpwSSVRNNVRLpldlagVPRaEGNTRVSEVLELVGL--GKFADVLPReLSGGMQMRVSIARGLVTRPKLLLMDEPF 180
Cdd:PRK10636 392 E-----SPLQHLARL------APQ-ELEQKLRDYLGGFGFqgDKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190
....*....|....*....|....*....|....
gi 488997434 181 GALDEITRNKLDSDLLrlwqEQNLTVVFVTHSIH 214
Cdd:PRK10636 459 NHLDLDMRQALTEALI----DFEGALVVVSHDRH 488
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-197 |
2.00e-07 |
|
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: 51.86 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 24 IEVLSAEKIYsnGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrdsREKAQhpLSFVFQE 102
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDdLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----GETVK--LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 103 -ATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSevlelvgLGKF----ADVLPR--ELSGGMQMRVSIARGLVTRPKLLL 175
Cdd:TIGR03719 394 rDALDPNKTVWEEISGGLDIIKLGKREIPSRAY-------VGRFnfkgSDQQKKvgQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180
....*....|....*....|..
gi 488997434 176 MDEPfgaldeitRNKLDSDLLR 197
Cdd:TIGR03719 467 LDEP--------TNDLDVETLR 480
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-193 |
2.23e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLmLWRRDSREKAQHP-LSFVFQEATLMPWSSVRNNVR 116
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI-YYKNCNINNIAKPyCTYIGHNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 117 LpldlagvpRAEGNTRVSEVLELVGLGKFADVLPRE---LSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDS 193
Cdd:PRK13541 93 F--------WSEIYNSAETLYAAIHYFKLHDLLDEKcysLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-184 |
2.36e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.93 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 35 NGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVA-----GLVEpsdGKLMLWRRDSREKAQHPLSFVFQEATLMPW 108
Cdd:cd03232 17 GGKRQLLNnISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVIT---GEILINGRPLDKNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488997434 109 SSVRnnvrlpldlagvpraegntrvsEVLElvglgkFADVLpRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:cd03232 94 LTVR----------------------EALR------FSALL-RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
38-237 |
2.96e-07 |
|
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: 49.24 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 38 RALLPVNLTINQGEFITLLGPSGCGKSTLLKmvAGLVEpsDGKLMLwrRDSREKA-QHPLSFVFQEATLMPwssvrnnvr 116
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA--SGKARL--ISFLPKFsRNKLIFIDQLQFLID--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 117 lpldlagvpraegntrvsevlelVGLGKFAdvLPRE---LSGGMQMRVSIARGLVTRPK--LLLMDEPFGALDEITRNKL 191
Cdd:cd03238 74 -----------------------VGLGYLT--LGQKlstLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488997434 192 DSDLLRLWQEQNlTVVFVTHsiHEAVF-LSQRVIMMAARPGRVVEDI 237
Cdd:cd03238 129 LEVIKGLIDLGN-TVILIEH--NLDVLsSADWIIDFGPGSGKSGGKV 172
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
33-235 |
5.18e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.52 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrDSREKAQHPL-------SFVFQEAT 104
Cdd:cd03288 29 YENNLKPVLKhVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI---DGIDISKLPLhtlrsrlSIILQDPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 105 LMPWSsvrnnVRLPLDlagvPRAE-GNTRVSEVLELVGLGKFADVLPREL-----------SGGMQMRVSIARGLVTRPK 172
Cdd:cd03288 106 LFSGS-----IRFNLD----PECKcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488997434 173 LLLMDEPFGALDEITRNKLDSDLLRLWQEQnlTVVFVTHSIHEavFLSQRVIMMAARpGRVVE 235
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVST--ILDADLVLVLSR-GILVE 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
33-226 |
1.02e-06 |
|
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: 49.08 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 33 YSNGTRALLP-VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEpSDGKLML----WRRDSREKAQHPLSFVFQEATLMP 107
Cdd:cd03289 12 YTEGGNAVLEnISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIdgvsWNSVPLQKWRKAFGVIPQKVFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 108 wSSVRNNvrlpLDLAGVPRAEgntRVSEVLELVGLGKFADVLPREL-----------SGGMQMRVSIARGLVTRPKLLLM 176
Cdd:cd03289 91 -GTFRKN----LDPYGKWSDE---EIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 177 DEPFGALDEITRNKLDSDLLRLWqeQNLTVVFVTHSIhEAVFLSQRVIMM 226
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKQAF--ADCTVILSEHRI-EAMLECQRFLVI 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
128-213 |
1.04e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 128 EGNTR--VSEVLELVGLGKFADVLP-----------RELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSD 194
Cdd:PTZ00265 1321 EDATRedVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
90
....*....|....*....
gi 488997434 195 LLRLWQEQNLTVVFVTHSI 213
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRI 1419
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-187 |
2.41e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 40 LLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPS----DGKLMLWRRDSRE-KAQHPLSFVFqeatlmpwsSVRNN 114
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEiKKHYRGDVVY---------NAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 115 VRLP-------LDLAGVPRAEGNtRVSEVLELVGLGKFADV------------------LPRELSGGMQMRVSIARGLVT 169
Cdd:TIGR00956 148 VHFPhltvgetLDFAARCKTPQN-RPDGVSREEYAKHIADVymatyglshtrntkvgndFVRGVSGGERKRVSIAEASLG 226
|
170
....*....|....*...
gi 488997434 170 RPKLLLMDEPFGALDEIT 187
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSAT 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-241 |
3.47e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 18 AAATPAIEVLSAEKIY---SNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLML-----WRRDSR 89
Cdd:COG3845 249 APAEPGEVVLEVENLSvrdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdgediTGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 90 EKAQHPLSFV----FQEATLMPWSSVRNNV-----RLPLDLAGV---PRAEGNTRvsevlELVGlgKFaDVLP------- 150
Cdd:COG3845 329 ERRRLGVAYIpedrLGRGLVPDMSVAENLIlgryrRPPFSRGGFldrKAIRAFAE-----ELIE--EF-DVRTpgpdtpa 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 151 RELSGGMQMRVSIARGLVTRPKLLLMDEP-----FGALDEItRNKLDSdlLRlwqEQNLTVVFVTHSIHEAVFLSQRVIM 225
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPtrgldVGAIEFI-HQRLLE--LR---DAGAAVLLISEDLDEILALSDRIAV 474
|
250
....*....|....*.
gi 488997434 226 MAArpGRVVEDIPIRE 241
Cdd:COG3845 475 MYE--GRIVGEVPAAE 488
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-184 |
4.26e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 22 PAIEVLSAEKIYSNGTRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMlwrRDSREK----AQH--- 94
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKVRmavfSQHhvd 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 95 -------PLSFVFQEATLMPWSSVRNNVrlpldlagvpraeGNTRVSEVLELVGLgkfadvlpRELSGGMQMRVSIARGL 167
Cdd:PLN03073 584 gldlssnPLLYMMRCFPGVPEQKLRAHL-------------GSFGVTGNLALQPM--------YTLSGGQKSRVAFAKIT 642
|
170
....*....|....*..
gi 488997434 168 VTRPKLLLMDEPFGALD 184
Cdd:PLN03073 643 FKKPHILLLDEPSNHLD 659
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
43-211 |
6.62e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGL--VEPSDGKLMLWRRD-----SREKAQHPLSFVFQEATLMPWSSVR--- 112
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDllelsPEDRAGEGIFMAFQYPVEIPGVSNQffl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 ----NNVRLPLDLAGVPRAEGNTRVSEVLELVGLGkfADVLPREL----SGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:PRK09580 100 qtalNAVRSYRGQEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
170 180
....*....|....*....|....*..
gi 488997434 185 eITRNKLDSDLLRLWQEQNLTVVFVTH 211
Cdd:PRK09580 178 -IDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-234 |
1.11e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMlWrrdsREKAQ-------HPLSFVfQEATLMPWSSvrnNV 115
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-W----SENANigyyaqdHAYDFE-NDLTLFDWMS---QW 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 116 RLPLDLAGVPRAEgntrvsevlelvgLGK--FA--DVL--PRELSGGMQMRVSIARGLVTRPKLLLMDEPFGALD----E 185
Cdd:PRK15064 409 RQEGDDEQAVRGT-------------LGRllFSqdDIKksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDmesiE 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488997434 186 ITRNKLDsdllrlwqEQNLTVVFVTHSiHEAV-FLSQRVIMMaaRPGRVV 234
Cdd:PRK15064 476 SLNMALE--------KYEGTLIFVSHD-REFVsSLATRIIEI--TPDGVV 514
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
47-274 |
1.38e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 47 INQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrDSREKAQHPLSFVFQEATLMPWSSV--RNNVRLPLDL--- 121
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI---DDCDVAKFGLTDLRRVLSIIPQSPVlfSGTVRFNIDPfse 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 122 ---AGVPRAEGNTRVSEVLELVGLGKFADVLP--RELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEitrnKLDSDLL 196
Cdd:PLN03232 1336 hndADLWEALERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVDV----RTDSLIQ 1411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 197 RLWQEQ--NLTVVFVTHSIHeAVFLSQRVIMMAArpGRVVEDIPIREPFPR--SEAFR-VSPTFSLYARQLQDSLLQASQ 271
Cdd:PLN03232 1412 RTIREEfkSCTMLVIAHRLN-TIIDCDKILVLSS--GQVLEYDSPQELLSRdtSAFFRmVHSTGPANAQYLSNLVFERRE 1488
|
...
gi 488997434 272 SGM 274
Cdd:PLN03232 1489 NGM 1491
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
153-241 |
2.12e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 153 LSGGMQMRVSIARGLVTRPKLLLMDEP-----FGALDEITrnKLDSDLLRlwqeQNLTVVFVTHSIHEAVFLSQRVIMMA 227
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPtrgidVGAKYEIY--KLINQLVQ----QGVAIIVISSELPEVLGLSDRVLVMH 479
|
90
....*....|....
gi 488997434 228 ArpGRVVEDIPIRE 241
Cdd:PRK13549 480 E--GKLKGDLINHN 491
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
43-226 |
2.14e-05 |
|
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: 45.59 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 43 VNLTINQGEFITLLGPSGCGKSTLLKMVAGlVEPSDGKLMLWRRDSREKAQHPLSFVFQEATLMPWSSVRNNVrLP---- 118
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGI-VPilgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 119 ---LDLAGVPRAEGNTRVSEVLELVGLGK---------FADVLP-RELSGGMQMRVSIARGLVTRPKLLLMDEP-----F 180
Cdd:TIGR02633 357 gknITLSVLKSFCFKMRIDAAAELQIIGSaiqrlkvktASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPtrgvdV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488997434 181 GALDEITRnkldsdLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:TIGR02633 437 GAKYEIYK------LINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
37-211 |
3.93e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 37 TRALLPVNLTINQGEFITLLGPSGCGKSTLLKMVAGLVEPSDGKLMLWRRDSREKAQHPL----SFVFQEATLMPwSSVR 112
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLrnqvALVSQNVHLFN-DTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 113 NNVrlpldlaGVPRAEGNTR--VSEVLELVGLGKFADVLPR-----------ELSGGMQMRVSIARGLVTRPKLLLMDEP 179
Cdd:PRK11176 435 NNI-------AYARTEQYSReqIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190
....*....|....*....|....*....|..
gi 488997434 180 FGALDEITRNKLDSDLLRLwqEQNLTVVFVTH 211
Cdd:PRK11176 508 TSALDTESERAIQAALDEL--QKNRTSLVIAH 537
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
55-227 |
5.54e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 55 LLGPSGCGKSTLLKMVAGLVEPSDGKLMLwrrDSREKAQHpLS---FVFQEATLMP---------WSSVRNNVR---LP- 118
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSL---DPNERLGK-LRqdqFAFEEFTVLDtvimghtelWEVKQERDRiyaLPe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 119 ---------LDLAGVpRAE--GNT---RVSEVLELVGL------GKFADVLPrelsgGMQMRVSIARGLVTRPKLLLMDE 178
Cdd:PRK15064 108 mseedgmkvADLEVK-FAEmdGYTaeaRAGELLLGVGIpeeqhyGLMSEVAP-----GWKLRVLLAQALFSNPDILLLDE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488997434 179 PfgaldeitRNKLDSDLLRlWQEQNL-----TVVFVTHSIHeavFLSQRVIMMA 227
Cdd:PRK15064 182 P--------TNNLDINTIR-WLEDVLnernsTMIIISHDRH---FLNSVCTHMA 223
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
151-212 |
5.72e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 5.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997434 151 RELSGGMQMRVSIARGLVTRPKLLLMDEPFGALDEITRNKLDSDLLRlWQEqnlTVVFVTHS 212
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPK---TFIVVSHA 400
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
57-197 |
8.24e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 57 GPSGCGKSTLLKMVAGLVEPSDGKLMLwrrdsREKAQhpLSFVFQE-ATLMPWSSVRNNVRLPLDLAGVPRAEGNTRVSe 135
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTIKI-----GETVK--LAYVDQSrDALDPNKTVWEEISGGLDIIKVGNREIPSRAY- 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488997434 136 vlelvgLGKF----ADVLPR--ELSGGMQMRVSIARGLVTRPKLLLMDEPfgaldeitRNKLDSDLLR 197
Cdd:PRK11819 429 ------VGRFnfkgGDQQKKvgVLSGGERNRLHLAKTLKQGGNVLLLDEP--------TNDLDVETLR 482
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
143-231 |
9.57e-04 |
|
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: 39.56 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 143 GKFADVLPRE---LSGGMQMRVSIARGLV----------TRPKLLLMDEPFGALDEITRNKLDSdLLRLWQEQNLTVVFV 209
Cdd:cd03279 111 GEFDRFLARPvstLSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALEAVAT-ALELIRTENRMVGVI 189
|
90 100
....*....|....*....|..
gi 488997434 210 THSIHEAVFLSQRVIMMAARPG 231
Cdd:cd03279 190 SHVEELKERIPQRLEVIKTPGG 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
152-235 |
2.16e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.38 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997434 152 ELSGGMQMRVSIARGLVTRPKLLLMDEP-----FGALDEITRnkldsdLLRLWQEQNLTVVFVTHSIHEAVFLSQRVIMM 226
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPtrgidVGAKAEIYK------VMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
|
....*....
gi 488997434 227 aaRPGRVVE 235
Cdd:PRK09700 483 --CEGRLTQ 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
153-184 |
3.10e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.56 E-value: 3.10e-03
10 20 30
....*....|....*....|....*....|..
gi 488997434 153 LSGGMQMRVSIARGLVTRPKLLLMDEPFGALD 184
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
53-70 |
9.74e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 35.59 E-value: 9.74e-03
|
| |
