|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-426 |
1.15e-76 |
|
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: 247.89 E-value: 1.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSY--GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGgqLTSGQVSLGG-------- 70
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG--RISGEVLLDGrdllelse 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ----RSQAMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVA 146
Cdd:COG1123 79 alrgRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 147 MDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDDYQGKVDGV-YRFKGEQVDLLTKDE--------Q 216
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVvVMDDGRIVEDGPPEEilaapqalA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 217 ALLLATEPIGLHFPLPENEPAAFVMKN----FAIKQGRPL--LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-Y 289
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPLLEVRNlskrYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRpT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 290 QGSLTWEGKEVAKLKE---RTYFQHVAQIFQNASDQFMA-ITVKEELA---LSQKHASPYFTPEVLDQALADLDL-ADHM 361
Cdd:COG1123 319 SGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYSSLNPrMTVGDIIAeplRLHGLLSRAERRERVAELLERVGLpPDLA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 362 DQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG1123 399 DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH 463
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-204 |
5.18e-59 |
|
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: 192.30 E-value: 5.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLT-SGQV----SLGGRSQ--AMMF 77
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvDGKDltklSLKELRRkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 78 QEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEP 157
Cdd:cd03225 82 QNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 158 FASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRFK 204
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-201 |
3.59e-55 |
|
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: 182.92 E-value: 3.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG-----------RS 72
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK-----PTSGEVLVDGkditkknlrelRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 Q-AMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:COG1122 76 KvGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVY 201
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
247-441 |
4.13e-54 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 179.59 E-value: 4.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMA 325
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALSQKHA--SPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSI 403
Cdd:cd03225 91 PTVEEEVAFGLENLglPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 404 EQVVQLLQKCQEKsGQTILLISHHFYGISTWCDYHLRL 441
Cdd:cd03225 171 RELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVL 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
244-448 |
4.24e-44 |
|
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: 154.03 E-value: 4.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 244 FAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQ 322
Cdd:COG1122 8 FSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKpTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 FMAITVKEELAlsqkhaspyFTPEVL-----------DQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLI 391
Cdd:COG1122 88 LFAPTVEEDVA---------FGPENLglpreeirervEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 392 DEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISHHFYGISTWCDYHLRLAGRELAF 448
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-188 |
1.48e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 156.39 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG----------RS 72
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLED-----PTSGEILIGGrdvtdlppkdRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 QAMMFQeageQF----TMaTPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALA-VLVAm 147
Cdd:COG3839 77 IAMVFQ----SYalypHM-TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGrALVR- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTH 192
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-188 |
3.97e-43 |
|
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: 151.13 E-value: 3.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG----------RSQA 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER-----PDSGEILIDGrdvtgvpperRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:cd03259 76 MVFQDYA-LFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 155 DEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTH 189
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-192 |
9.57e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.90 E-value: 9.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQA---------- 74
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRP-----TSGEVRVLGEDVArdpaevrrri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 -MMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:COG1131 76 gYVPQEPA-LYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 154 LDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDD 192
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEE 193
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-188 |
5.19e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.39 E-value: 5.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMMFQEA 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-----PTSGTVRLFGKPPRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 G-----EQFTMATP---REeiIFAMENLGK-------SKtefADRLKLAS--EFAEIDSLLDQKIVTMSGGEKQRVALAV 143
Cdd:COG1121 78 GyvpqrAEVDWDFPitvRD--VVLMGRYGRrglfrrpSR---ADREAVDEalERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTH 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-188 |
6.50e-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: 142.23 E-value: 6.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMMFQEAGEQF 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP-----PSAGEVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMA----------TPREEIIFAMENLGKSKTefADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:COG4133 78 AYLghadglkpelTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 155 DEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-188 |
1.68e-38 |
|
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: 138.82 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAG--EQF 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-----TSGSIRVFGKPLEKERKRIGyvPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 T-------------MATPREEIIFAMENLGKSKTEFADRlklASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:cd03235 77 RsidrdfpisvrdvVLMGLYGHKGLFRRLSKADKAKVDE---ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-186 |
2.95e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 2.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSY----GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQ--- 73
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEK-----PTSGEVLVDGKPVtgp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 ----AMMFQEageqFTM---ATPREEIIFAMENLGKSKTEFADRlklasefaeIDSLLDQkiV-----------TMSGGE 135
Cdd:COG1116 79 gpdrGVVFQE----PALlpwLTVLDNVALGLELRGVPKAERRER---------ARELLEL--VglagfedayphQLSGGM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489717269 136 KQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTII-IT 186
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVT 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-215 |
4.20e-37 |
|
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: 135.76 E-value: 4.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQA---------- 74
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP-----DSGSILIDGEDVRkeprearrqi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 -MMFQEAGEQFTMaTPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:COG4555 77 gVLPDERGLYDRL-TVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489717269 154 LDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRF-KGEQVDLLTKDE 215
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILhKGKVVAQGSLDE 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
243-443 |
1.02e-35 |
|
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: 130.84 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 243 NFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKeVAKLKERtyFQHVAQIFQNASD 321
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKeSSGSILLNGK-PIKAKER--RKSIGYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 322 QFMAITVKEELALSQKHASPYftPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:cd03226 83 QLFTDSVREELLLGLKELDAG--NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 402 SIEQVVQLLQKCQEKsGQTILLISHHFYGISTWCDYHLRLAG 443
Cdd:cd03226 161 NMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
249-427 |
1.17e-35 |
|
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: 130.68 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEVAKLKErTYFQHVAQIF-QNASDQFMai 326
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLpPSAGEVLWNGEPIRDARE-DYRRRLAYLGhADGLKPEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:COG4133 91 TVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180
....*....|....*....|.
gi 489717269 407 VQLLQKCQEKsGQTILLISHH 427
Cdd:COG4133 171 AELIAAHLAR-GGAVLLTTHQ 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-188 |
1.19e-35 |
|
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: 132.09 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRS------------ 72
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-----PSSGEVLLDGRDlaslsrrelarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 QAMMFQEAGEQFTMaTPREEIIF-------AMENLGKSKTEFADRlklASEFAEIDSLLDQKIVTMSGGEKQRVALAVLV 145
Cdd:COG1120 77 IAYVPQEPPAPFGL-TVRELVALgryphlgLFGRPSAEDREAVEE---ALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 146 AMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLH 196
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-185 |
1.26e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.84 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQA------ 74
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET-----PDSGRILLDGRDVTglppek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 ----MMFQEAgeqftmA-----TPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLV 145
Cdd:COG3842 77 rnvgMVFQDY------AlfphlTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 146 AMDVDLFLLDEPFASVDPAAR---RFLIGRLakLKEQGKTIII 185
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLReemREELRRL--QRELGITFIY 191
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-194 |
2.24e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.32 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG-----------RSQ 73
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP-----PTSGEIYLDGkplsampppewRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 -AMMFQEA-------GEQFTMATPREEIIFAMENLgkskTEFADRLKLAsefaeiDSLLDQKIVTMSGGEKQRVALAVLV 145
Cdd:COG4619 76 vAYVPQEPalwggtvRDNLPFPFQLRERKFDRERA----LELLERLGLP------PDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 146 AMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHlfDDYQ 194
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSH--DPEQ 193
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
239-446 |
2.61e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.94 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 239 FVMKNFAIK-QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKERTYFQHVAQIF 316
Cdd:COG4619 1 LELEGLSFRvGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 317 QNAsdQFMAITVKEELALSQKHASPYFTPEVLDQALADLDLADH-MDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:COG4619 81 QEP--ALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCDYHLRLAGREL 446
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-188 |
3.27e-35 |
|
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: 130.07 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG----------RSQA 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE-----EPTSGRIYIGGrdvtdlppkdRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAGEQFTMaTPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:cd03301 76 MVFQNYALYPHM-TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 155 DEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTH 189
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-194 |
6.20e-35 |
|
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: 127.90 E-value: 6.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSqammFQEAGEQF 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP-----DSGEIKVLGKD----IKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 tmatpREEIIFAMENLGkskteFADRLKlASEFaeidslldqkiVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPA 164
Cdd:cd03230 72 -----KRRIGYLPEEPS-----LYENLT-VREN-----------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190
....*....|....*....|....*....|
gi 489717269 165 ARRFLIGRLAKLKEQGKTIIITDHLFDDYQ 194
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILEEAE 159
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-186 |
9.41e-35 |
|
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: 128.74 E-value: 9.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDR----EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG-------RSQ 73
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER-----PTSGEVLVDGepvtgpgPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:cd03293 76 GYVFQQDA-LLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 154 LDEPFASVDPAARRFLIGRLAKL-KEQGKTII-IT 186
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIwRETGKTVLlVT 189
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-188 |
1.95e-34 |
|
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: 126.78 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 6 TIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMMfqeageqft 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-----PSSGEILLDGKDLASL--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 86 matpreeiifamenlgkSKTEFADRLKL---ASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD 162
Cdd:cd03214 67 -----------------SPKELARKIAYvpqALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180
....*....|....*....|....*..
gi 489717269 163 PAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:cd03214 130 IAHQIELLELLRRLaRERGKTVVMVLH 156
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-204 |
2.94e-34 |
|
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: 125.43 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 6 TIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAGeqft 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP-----TSGEILIDGKDIAKLPLEEL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 86 matpREEIifamenlgksktefadrlklasefaeidSLLDQkivtMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAA 165
Cdd:cd00267 72 ----RRRI----------------------------GYVPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 166 RRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRFK 204
Cdd:cd00267 116 RERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-436 |
5.56e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 133.27 E-value: 5.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQ-AMMFQEAGEqFT 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGEL-----EPDSGEVSIPKGLRiGYLPQEPPL-DD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 86 MATPREEIIFAMENLGKSKTEFA-------------DRL-KLASEFAEID-------------------SLLDQKIVTMS 132
Cdd:COG0488 75 DLTVLDTVLDGDAELRALEAELEeleaklaepdedlERLaELQEEFEALGgweaearaeeilsglgfpeEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 133 GGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKeqgKTIII-----------TDHLFDDYQGKvdgVY 201
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP---GTVLVvshdryfldrvATRILELDRGK---LT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 202 RFKG----------EQVDLLTKDEQAL--LLATEpigLHF----------------------------PLPENEPAAFVM 241
Cdd:COG0488 229 LYPGnysayleqraERLEQEAAAYAKQqkKIAKE---EEFirrfrakarkakqaqsrikaleklereePPRRDKTVEIRF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 242 KNfAIKQGRPLLEQKELS---------------IPKG-KVTLItGPNGSGKSSLFKAMTKLLD-YQGSLTWeGKEVaklk 304
Cdd:COG0488 306 PP-PERLGKKVLELEGLSksygdktllddlslrIDRGdRIGLI-GPNGAGKSTLLKLLAGELEpDSGTVKL-GETV---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 305 ERTYF-QHVAQIFQNAsdqfmaiTVKEELAlsqkHASPYFTPEVLDQALADLDLA-DHMDQVVYSLSGGQKKKLEILLML 382
Cdd:COG0488 379 KIGYFdQHQEELDPDK-------TVLDELR----DGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLL 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 383 LSGQEVLLIDEPLSGLDQKSIEQVVQLLqkcQEKSGqTILLISH--HFygISTWCD 436
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEAL---DDFPG-TVLLVSHdrYF--LDRVAT 497
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
249-448 |
1.09e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.74 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERT-YfqhVAQifQNASDQFMAI 326
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGKPPRRARRRIgY---VPQ--RAEVDWDFPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQKHASPYFTP------EVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:COG1121 93 TVRDVVLMGRYGRRGLFRRpsradrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 401 KSIEQVVQLLQKCQEKsGQTILLISHHFYGISTWCDYHLRLAGRELAF 448
Cdd:COG1121 173 ATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-188 |
2.42e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 124.68 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 6 TIDHLTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG---------RSQAM 75
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI-----KESSGSILLNGkpikakerrKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLasefAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:cd03226 76 VMQDVDYQLFTDSVREELLLGLKELDAGNEQAETVLKD----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-186 |
5.85e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 125.24 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSY--GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG------------RS 72
Cdd:TIGR04520 3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLL-----LPTSGKVTVDGldtldeenlweiRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 QA-MMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:TIGR04520 78 KVgMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKL-KEQGKTII-IT 186
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLnKEEGITVIsIT 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-188 |
1.31e-32 |
|
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: 123.44 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGG-------------- 70
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGkdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQAMMFQEAgeqfTM--ATPREEIIFAMENLGKSKTEFADR-----LKLASEFAEIDSLLDQKivTMSGGEKQRVALAV 143
Cdd:cd03260 81 RRVGMVFQKP----NPfpGSIYDNVAYGLRLHGIKLKEELDErveeaLRKAALWDEVKDRLHAL--GLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQgKTIIITDH 188
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTH 198
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-188 |
2.94e-32 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 121.57 E-value: 2.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ----------LTSGQVSLGGRSQ-AM 75
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQvylngqetppLNSKKASKFRREKlGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEAG---EQftmaTPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:TIGR03608 81 LFQNFAlieNE----TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 153 LLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTH 192
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-188 |
2.22e-30 |
|
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: 115.75 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGG-------------- 70
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP-----DSGSILIDGedltdledelpplr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQAMMFQEAGEQFTMaTPREEIIFAmenlgksktefadrlklasefaeidslldqkivtMSGGEKQRVALAVLVAMDVD 150
Cdd:cd03229 76 RRIGMVFQDFALFPHL-TVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQ-GKTIIITDH 188
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTH 159
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
241-448 |
2.62e-30 |
|
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: 116.48 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 241 MKNFAIK-QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKlkERTYFQHVAQIFQn 318
Cdd:cd03235 2 VEDLTVSyGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGKPLEK--ERKRIGYVPQRRS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 aSDQFMAITVKEELALS-QKHASPYFTP-----EVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLID 392
Cdd:cd03235 79 -IDRDFPISVRDVVLMGlYGHKGLFRRLskadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 393 EPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISHHFYGISTWCDYHLRLAGRELAF 448
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-188 |
1.42e-29 |
|
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: 114.89 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGD----REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLypkygGQLTSGQVSLGGRSQAMM---- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL-----DRPTSGEVRVDGTDISKLseke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 ------------FQeageQFTM---ATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVAL 141
Cdd:cd03255 76 laafrrrhigfvFQ----SFNLlpdLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 142 AVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTH 199
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
248-436 |
2.52e-29 |
|
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: 120.01 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD----YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQF 323
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrISGEVLLDGRDLLELSEALRGRRIGMVFQDPMTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 MAITVKEELA--LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:COG1123 97 NPVTVGDQIAeaLENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVT 176
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 402 SIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCD 436
Cdd:COG1123 177 TQAEILDLLRELQRERGTTVLLITHDLGVVAEIAD 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
248-436 |
2.71e-29 |
|
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: 111.95 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQnasdqfmai 326
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 tvkeelalsqkhaspyftpevldqaladldladhmdqvvysLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:cd00267 81 -----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|
gi 489717269 407 VQLLQKCQEKsGQTILLISHHFYGISTWCD 436
Cdd:cd00267 120 LELLRELAEE-GRTVIIVTHDPELAELAAD 148
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-188 |
3.12e-29 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 114.18 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGR--SQAMMFQEAG- 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV-----KPDSGKILLDGQdiTKLPMHKRARl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 -------EQ--FTMATPREEIIFAMENLGKSKTEFADRLK-LASEFaEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:cd03218 76 gigylpqEAsiFRKLTVEENILAVLEIRGLSKKEREEKLEeLLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-188 |
3.12e-29 |
|
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: 112.48 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDR--EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGG------RSQ-AM 75
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldleslRKNiAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEAgeqftmatpreeIIFAM---ENLgksktefadrlklasefaeidslldqkivtMSGGEKQRVALAVLVAMDVDLF 152
Cdd:cd03228 81 VPQDP------------FLFSGtirENI------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 153 LLDEPFASVDPAARRFLIGRLAKLKeQGKTIIITDH 188
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALA-KGKTVIVIAH 153
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
249-427 |
3.17e-29 |
|
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: 114.76 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFmAIT 327
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAYVPQEPPAPF-GLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQK-HASPYFTP-----EVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:COG1120 92 VRELVALGRYpHLGLFGRPsaedrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180
....*....|....*....|....*.
gi 489717269 402 SIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHD 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-197 |
1.48e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.07 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQA--------- 74
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER-----PTSGQVLVNGQDLSrlkrreipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 ------MMFQEageqF------TMAtprEEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALA 142
Cdd:COG2884 77 lrrrigVVFQD----FrllpdrTVY---ENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 143 VLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH---LFDDYQGKV 197
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHdleLVDRMPKRV 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-188 |
2.26e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.41 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLG-------GRSQAMM 76
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlssrqlARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 FQEageqftMATP-----REEIIFAME---NL-GKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAM 147
Cdd:PRK11231 82 PQH------HLTPegitvRELVAYGRSpwlSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-159 |
2.56e-28 |
|
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: 109.27 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLT-SGQVSLGGRSQ------AMMFQEAGeQFTMATPREE 92
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILlDGQDLTDDERKslrkeiGYVFQDPQ-LFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 93 IIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIV----TMSGGEKQRVALAVLVAMDVDLFLLDEPFA 159
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-188 |
3.27e-28 |
|
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: 111.61 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQA------ 74
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP-----DSGEILVDGQDITglseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 ---------MMFQEAGeQFTMATPREEIIFAM-ENLGKSKTEFADR--LKLasEFAEIDSLLDQKIVTMSGGEKQRVALA 142
Cdd:COG1127 77 lyelrrrigMLFQGGA-LFDSLTVFENVAFPLrEHTDLSEAEIRELvlEKL--ELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489717269 143 VLVAMDVDLFLLDEPFASVDP-AARRF--LIGRLAklKEQGKTIIITDH 188
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPiTSAVIdeLIRELR--DELGLTSVVVTH 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-188 |
4.04e-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: 111.09 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 12 FSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMMFQEAGEQfTMATPRE 91
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP-----PDSGTVTVRGRVSSLLGLGGGFN-PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 92 EIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIG 171
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170
....*....|....*..
gi 489717269 172 RLAKLKEQGKTIIITDH 188
Cdd:cd03220 184 RLRELLKQGKTVILVSH 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-188 |
5.74e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.52 E-value: 5.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGD----REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPkyggqlTSGQVSLGGRSQAM 75
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRP------TSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 M----------------FQeageQFTM---ATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEK 136
Cdd:COG1136 75 LserelarlrrrhigfvFQ----FFNLlpeLTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489717269 137 QRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTH 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-188 |
8.80e-28 |
|
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: 110.28 E-value: 8.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGR-----SQA------- 74
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP-----DSGEVLIDGEdisglSEAelyrlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 ---MMFQEaGEQFTMATPREEIIFAM-ENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:cd03261 78 rmgMLFQS-GALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 151 LFLLDEPFASVDP-AARRF--LIGRLAklKEQGKTIIITDH 188
Cdd:cd03261 157 LLLYDEPTAGLDPiASGVIddLIRSLK--KELGLTSIMVTH 195
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-188 |
9.75e-28 |
|
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: 116.47 E-value: 9.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG-------- 70
Cdd:COG2274 470 LKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY-----EPTSGRILIDGidlrqidp 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ---RSQ-AMMFQEaGEQFTmATPREEIIFAMENLGKsktefaDRLKLASEFAEIDSL-------LDQKI----VTMSGGE 135
Cdd:COG2274 545 aslRRQiGVVLQD-VFLFS-GTIRENITLGDPDATD------EEIIEAARLAGLHDFiealpmgYDTVVgeggSNLSGGQ 616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489717269 136 KQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKeQGKTIIITDH 188
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAH 668
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
230-447 |
1.34e-27 |
|
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: 115.24 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 230 PLPENEPAAFVMKN--FAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKER 306
Cdd:COG4988 328 PLPAAGPPSIELEDvsFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPpYSGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 307 TYFQHVAQIFQNAsdQFMAITVKEELALsqkhASPYFTPEVLDQALADLDLADHMDQ-------VV----YSLSGGQKKK 375
Cdd:COG4988 408 SWRRQIAWVPQNP--YLFAGTIRENLRL----GRPDASDEELEAALEAAGLDEFVAAlpdgldtPLgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489717269 376 LEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEksGQTILLISHHFYGIsTWCDYHLRLAGRELA 447
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIV 550
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-185 |
1.83e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.88 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG---------- 70
Cdd:COG1132 337 RGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD-----PTSGRILIDGvdirdltles 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 -RSQ-AMMFQEA-------GEQFTMATP---REEIIFAMENLGksktefadrlklASEFaeIDSL---LDQKI----VTM 131
Cdd:COG1132 412 lRRQiGVVPQDTflfsgtiRENIRYGRPdatDEEVEEAAKAAQ------------AHEF--IEALpdgYDTVVgergVNL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489717269 132 SGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKeQGKTIII 185
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIV 530
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
258-427 |
2.02e-27 |
|
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: 109.45 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE---------RTyFQHVaQIFQNasdqfmaIT 327
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRpTSGSVLFDGEDITGLPPheiarlgigRT-FQIP-RLFPE-------LT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQKHASPYFT---------PEVLDQALADLD---LADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:cd03219 92 VLENVMVAAQARTGSGLllararreeREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 396 SGLDQKSIEQVVQLLQKCQEKsGQTILLISHH 427
Cdd:cd03219 172 AGLNPEETEELAELIRELRER-GITVLLVEHD 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
258-426 |
6.82e-27 |
|
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: 107.58 E-value: 6.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKL--KERTYF--QHVAQIFQnasdQFMAI---TVK 329
Cdd:cd03255 25 LSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLseKELAAFrrRHIGFVFQ----SFNLLpdlTAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 E--ELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVV 407
Cdd:cd03255 101 EnvELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVM 180
|
170
....*....|....*....
gi 489717269 408 QLLQKCQEKSGQTILLISH 426
Cdd:cd03255 181 ELLRELNKEAGTTIVVVTH 199
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-188 |
6.88e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 13 SYGDREVIRDLSLTLPAGTfSL-LIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMM-----FQeaGEqftm 86
Cdd:COG1134 35 RREEFWALKDVSFEVERGE-SVgIIGRNGAGKSTLLKLIAGILE-----PTSGRVEVNGRVSALLelgagFH--PE---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 87 ATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAAR 166
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ 182
|
170 180
....*....|....*....|..
gi 489717269 167 RFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG1134 183 KKCLARIRELRESGRTVIFVSH 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-248 |
7.18e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.94 E-value: 7.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYGGQLTSGQVS-------LGGRSQ-AM 75
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPLdyskrglLALRQQvAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:PRK13638 82 VFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRFKGEQVdlLTKDEQALLLA----------TEP- 224
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI--LTHGAPGEVFActeameqaglTQPw 239
|
250 260 270
....*....|....*....|....*....|
gi 489717269 225 -IGLH----FPLPENEPAAFV-MKNFAIKQ 248
Cdd:PRK13638 240 lVKLHtqlgLPLCKTETEFFHrMQKCAFRE 269
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
248-426 |
7.81e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 106.35 E-value: 7.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRP-LLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKE--RTYFQHVAQIFQNASDQF 323
Cdd:TIGR01166 2 PGGPeVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQsGAVLIDGEPLDYSRKglLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 MAITVKEELALSQKH--ASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:TIGR01166 82 FAADVDQDVAFGPLNlgLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*
gi 489717269 402 SIEQVVQLLQKCQEkSGQTILLISH 426
Cdd:TIGR01166 162 GREQMLAILRRLRA-EGMTVVISTH 185
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
258-427 |
1.10e-26 |
|
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: 107.82 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE---------RTyFQHVaQIFQNasdqfMaiT 327
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITGFYRpTSGRILFDGRDITGLPPhriarlgiaRT-FQNP-RLFPE-----L--T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQKHASPYFT--------------PEVLDQA---LADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLL 390
Cdd:COG0411 96 VLENVLVAAHARLGRGLlaallrlprarreeREARERAeelLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 391 IDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-186 |
1.24e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.18 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGD--REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG-------- 70
Cdd:PRK13635 2 KEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL-----PEAGTITVGGmvlseetv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ----RSQAMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVA 146
Cdd:PRK13635 77 wdvrRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 147 MDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGK-TII-IT 186
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLsIT 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-189 |
1.33e-26 |
|
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: 112.55 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSY--GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRS-QAMMFQ 78
Cdd:COG4987 331 GPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDlRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 79 EAGEQFTMATPREEIiFAM---ENL-----GKSKTEFADRLKLA--SEFAE-----IDSLLDQKIVTMSGGEKQRVALAV 143
Cdd:COG4987 406 DLRRRIAVVPQRPHL-FDTtlrENLrlarpDATDEELWAALERVglGDWLAalpdgLDTWLGEGGRRLSGGERRRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLkEQGKTII-ITDHL 189
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLlITHRL 530
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
248-427 |
1.40e-26 |
|
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: 105.16 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNAsdQFMAI 326
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDpTSGEILIDGVDLRDLDLESLRKNIAYVPQDP--FLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELalsqkhaspyftpevldqaladldladhmdqvvysLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:cd03228 91 TIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180
....*....|....*....|.
gi 489717269 407 VQLLQKcqEKSGQTILLISHH 427
Cdd:cd03228 136 LEALRA--LAKGKTVIVIAHR 154
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
242-436 |
1.49e-26 |
|
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: 107.25 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 242 KNFaikQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKlKERTYFQHVAQIFQ-NA 319
Cdd:COG4555 9 KKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpDSGSILIDGEDVRK-EPREARRQIGVLPDeRG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 320 SDQFMaiTVKEELAL--SQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSG 397
Cdd:COG4555 85 LYDRL--TVRENIRYfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 398 LDQKSIEQVVQLLQKCQeKSGQTILLISHHFYGISTWCD 436
Cdd:COG4555 163 LDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCD 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-192 |
1.72e-26 |
|
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: 106.65 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREViRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGG----------RSQA 74
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP-----DSGKILLNGkditnlppekRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:cd03299 75 YVPQNYA-LFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 155 DEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDD 192
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEE 192
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-188 |
2.10e-26 |
|
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: 106.37 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMM-------- 76
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-----PTSGSVLFDGEDITGLppheiarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 -----FQEAGEQFTMaTPREEIIFAMENLGKSKTEFADRLKLASEFAE----------IDSLLDQKIVTMSGGEKQRVAL 141
Cdd:cd03219 76 gigrtFQIPRLFPEL-TVLENVMVAAQARTGSGLLLARARREEREAREraeellervgLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 142 AVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
258-396 |
2.40e-26 |
|
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: 103.88 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDqFMAITVKEELALSQ 336
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQL-FPRLTVRENLRLGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 337 KHASPYFTP--EVLDQALADLDLADHMDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:pfam00005 85 LLKGLSKREkdARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
258-427 |
5.13e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.53 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERtYFQHVAQIFQNAS-DQFMaiTVKEELALS 335
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPAlYPDL--TVRENLRFF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 QK--HASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKC 413
Cdd:COG1131 98 ARlyGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL 177
|
170
....*....|....
gi 489717269 414 QEKsGQTILLISHH 427
Cdd:COG1131 178 AAE-GKTVLLSTHY 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-188 |
7.17e-26 |
|
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: 105.01 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQA---------- 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE-----TPTSGEILLDGKDITnlpphkrpvn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:cd03300 76 TVFQNYA-LFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 155 DEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLqKELGITFVFVTH 189
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
230-444 |
8.56e-26 |
|
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: 109.86 E-value: 8.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 230 PLPENEPAAFVMKNFAI---KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKE 305
Cdd:COG4987 325 PAPAPGGPSLELEDVSFrypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSITLGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 306 RTYFQHVAQIFQNAsdQFMAITVKEELALsqkhASPYFTPE----VLDQA-LADL--DLADHMDQVVYS----LSGGQKK 374
Cdd:COG4987 405 DDLRRRIAVVPQRP--HLFDTTLRENLRL----ARPDATDEelwaALERVgLGDWlaALPDGLDTWLGEggrrLSGGERR 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 375 KLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEksGQTILLISHHFYGIStWCDYHLRL-AGR 444
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLE-RMDRILVLeDGR 546
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-188 |
1.53e-25 |
|
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: 109.08 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLggrsqammfqea 80
Cdd:COG4988 334 PPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL------------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 gEQFTMATPREEI--------IFA---MENL--GK---SKTEFADRLKLA--SEFaeIDSL---LDQKI----VTMSGGE 135
Cdd:COG4988 402 -SDLDPASWRRQIawvpqnpyLFAgtiRENLrlGRpdaSDEELEAALEAAglDEF--VAALpdgLDTPLgeggRGLSGGQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489717269 136 KQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKeQGKTIIITDH 188
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITH 530
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-426 |
1.70e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 109.00 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGD----REVIRDLSLTLPAG-TFSLlIGPTGCGKS-TLLKIMaGLYPkYGGQLTSGQVSLGGRSQ----- 73
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGeTLAL-VGESGSGKSvTALSIL-RLLP-DPAAHPSGSILFDGQDLlglse 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 -----------AMMFQEA----------GEQFTmatpreEIIFAMENLGKSKTEfadrlklasefAEIDSLLDQ------ 126
Cdd:COG4172 84 relrrirgnriAMIFQEPmtslnplhtiGKQIA------EVLRLHRGLSGAAAR-----------ARALELLERvgipdp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 127 -KIVT-----MSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLK-EQGKTII-ITDHL-----FDDY 193
Cdd:COG4172 147 eRRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQrELGMALLlITHDLgvvrrFADR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 194 -----QGKVdgVYRfkGEQVDLLTKDEQA---LLLATEPIGLHFPLPENEPAAFVMKN----FAIKQG---RPLLEQK-- 256
Cdd:COG4172 227 vavmrQGEI--VEQ--GPTAELFAAPQHPytrKLLAAEPRGDPRPVPPDAPPLLEARDlkvwFPIKRGlfrRTVGHVKav 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 257 ---ELSIPKGKvTL-ITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAKLKE---RTYFQHVAQIFQnasDQF------ 323
Cdd:COG4172 303 dgvSLTLRRGE-TLgLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRralRPLRRRMQVVFQ---DPFgslspr 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 MAI--TVKEELALSQKHASPYFTPEVLDQALADLDL-ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD- 399
Cdd:COG4172 379 MTVgqIIAEGLRVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDv 458
|
490 500
....*....|....*....|....*....
gi 489717269 400 --QKsieQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG4172 459 svQA---QILDLLRDLQREHGLAYLFISH 484
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-188 |
3.66e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 106.27 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG----------RS 72
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE-----DITSGDLFIGEkrmndvppaeRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 QAMMFQEAG--EQFTMAtprEEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALA-VLVAmDV 149
Cdd:PRK11000 77 VGMVFQSYAlyPHLSVA---ENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGrTLVA-EP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 150 DLFLLDEPFASVDPAAR---RFLIGRLAklKEQGKTIIITDH 188
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRvqmRIEISRLH--KRLGRTMIYVTH 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
258-444 |
4.77e-25 |
|
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: 102.58 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKER---TYFQHVAQIFQNASDQF---MAI--TV 328
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLSRRlrkIRRKEIQMVFQDPMSSLnprMTIgeQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 KEELALSQKHASPYFTPEVLDQALADLDL-ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVV 407
Cdd:cd03257 106 AEPLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQIL 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 408 QLLQKCQEKSGQTILLISHHFYGISTWCDYHLRL-AGR 444
Cdd:cd03257 186 DLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMyAGK 223
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-188 |
4.78e-25 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 102.74 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMM-------- 76
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVR-----PDAGKILIDGQDITHLpmherarl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 -----FQEAgEQFTMATPREEIIFAMENLGK-SKTEFADRL-KLASEFaEIDSLLDQKIVTMSGGEKQRVALAVLVAMDV 149
Cdd:TIGR04406 77 gigylPQEA-SIFRKLTVEENIMAVLEIRKDlDRAEREERLeALLEEF-QISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 150 DLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH 193
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-188 |
7.05e-25 |
|
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: 102.57 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYG----DREVIRDLSLTLPAG-TFSLlIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQ------ 73
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGeSFGL-VGESGSGKSTLLRALAGLERP-----WSGEVTFDGRPVtrrrrk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 ------AMMFQEAgeqFTMATPR---EEIIF-AMENLGKSKTEfaDRLKLASEFAEID-SLLDQKIVTMSGGEKQRVALA 142
Cdd:COG1124 76 afrrrvQMVFQDP---YASLHPRhtvDRILAePLRIHGLPDRE--ERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 143 VLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQ-GKTIIITDH 188
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSH 197
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-188 |
1.06e-24 |
|
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: 101.43 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY----GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ----------LTSGQVSLGG 70
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdllkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQAMMFQEAGEQF--TMaTPREEIIFAMENLGKSKTEFADRLKLASEFAEI---DSLLDQKIVTMSGGEKQRVALAVLV 145
Cdd:cd03257 82 KEIQMVFQDPMSSLnpRM-TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 146 AMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQ-GKTIIITDH 188
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITH 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-192 |
1.19e-24 |
|
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: 101.43 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE--VIRDLSLTLPAG-TFSLLiGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAG 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGeIFGLL-GHNGAGKTTTLKMLTGELRP-----TSGTAYINGYSIRTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 E------QFTMA----TPREEI-IFAMENLGKSKTEFADRLKLASEFaEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:cd03263 75 QslgycpQFDALfdelTVREHLrFYARLKGLPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKeQGKTIIITDHLFDD 192
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDE 194
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-223 |
1.40e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.25 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSYG----DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGR------- 71
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA-----PSSGEITLDGVpvtgpga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQAMMFQEAGeQFTMATPREEIIFAMENLGKSKtefADRLKLASEFAEIDSLLD---QKIVTMSGGEKQRVALAVLVAMD 148
Cdd:COG4525 77 DRGVVFQKDA-LLPWLNVLDNVAFGLRLRGVPK---AERRARAEELLALVGLADfarRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 149 VDLFLLDEPFASVDPAARrfligrlaklkEQGKTIIITdhlfddyqgkvdgVYRFKGEQVDLLTKD-EQALLLATE 223
Cdd:COG4525 153 PRFLLMDEPFGALDALTR-----------EQMQELLLD-------------VWQRTGKGVFLITHSvEEALFLATR 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-188 |
1.84e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.26 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGR--SQAMMF--- 77
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGRIFLDGEdiTHLPMHkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 78 --------QEAGeQFTMATPREEIIFAMENLGKSKTEFADRL-KLASEFaEIDSLLDQKIVTMSGGEKQRVALAVLVAMD 148
Cdd:COG1137 77 rlgigylpQEAS-IFRKLTVEDNILAVLELRKLSKKEREERLeELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 149 VDLFLLDEPFASVDPAArrflIGRL----AKLKEQGKTIIITDH 188
Cdd:COG1137 155 PKFILLDEPFAGVDPIA----VADIqkiiRHLKERGIGVLITDH 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-188 |
1.88e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.00 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 13 SYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGqvslGGRSQAMMFQ--EAGEQF------ 84
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA----GGARVAYVPQrsEVPDSLpltvrd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 --TM-------------ATPREEIIFAMENLGksktefadrlklasefaeIDSLLDQKIVTMSGGEKQRVALAVLVAMDV 149
Cdd:NF040873 77 lvAMgrwarrglwrrltRDDRAAVDDALERVG------------------LADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 150 DLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-191 |
1.94e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYG-----GQLTSGQVSLGGRSQ 73
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYlPQRGrvkvmGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 -AMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:PRK13647 81 vGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 153 LLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFD 191
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVD 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
248-436 |
2.25e-24 |
|
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: 101.42 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEVAKLKERTYFQHVAQIFQN---ASDQF 323
Cdd:COG1124 16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpyaSLHPR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 MaiTVKEELALSQKHASPYFTPEVLDQALADLDL-ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD--- 399
Cdd:COG1124 96 H--TVDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsv 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 400 QKsieQVVQLLQKCQEKSGQTILLISHHFYGISTWCD 436
Cdd:COG1124 174 QA---EILNLLKDLREERGLTYLFVSHDLAVVAHLCD 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-188 |
2.33e-24 |
|
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: 101.22 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE-VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG------------R 71
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI-----EPTSGEIFIDGedireqdpvelrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQAMMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADR----LKLASefAEIDSLLDQKIVTMSGGEKQRVALAVLVAM 147
Cdd:cd03295 76 KIGYVIQQIG-LFPHMTVEENIALVPKLLKWPKEKIRERadelLALVG--LDPAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKLKEQ-GKTIIITDH 188
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTH 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
259-426 |
2.39e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.75 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 259 SIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAITVKEELALS-Q 336
Cdd:PRK13648 31 NIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVGSIVKYDVAFGlE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 337 KHASPY-FTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQE 415
Cdd:PRK13648 111 NHAVPYdEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKS 190
|
170
....*....|.
gi 489717269 416 KSGQTILLISH 426
Cdd:PRK13648 191 EHNITIISITH 201
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-188 |
2.50e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 101.31 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 6 TIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSqamMFQEAGEQF- 84
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPP-----DSGEVLVDGLD---VATTPSRELa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 -TMATPREEIIFAM----ENL----------GKSKTEfaDRLKL--ASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAM 147
Cdd:COG4604 75 kRLAILRQENHINSrltvRELvafgrfpyskGRLTAE--DREIIdeAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH 194
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-192 |
3.04e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.60 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVirDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQ----------A 74
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLP-----PDSGRILWNGQDLtalppaerpvS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEaGEQFTMATPREEIifameNLGkskteFADRLKLASE-------FAE---IDSLLDQKIVTMSGGEKQRVALA-V 143
Cdd:COG3840 75 MLFQE-NNLFPHLTVAQNI-----GLG-----LRPGLKLTAEqraqveqALErvgLAGLLDRLPGQLSGGQRQRVALArC 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 144 LVaMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDD 192
Cdd:COG3840 144 LV-RKRPILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPED 192
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-192 |
4.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYG-----DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLG------GRS 72
Cdd:PRK13634 2 DITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL-----QPTSGTVTIGervitaGKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 Q----------AMMFQEAGEQFTMATPREEIIFAMENLGKSKtefADRLKLASEFAEI----DSLLDQKIVTMSGGEKQR 138
Cdd:PRK13634 77 NkklkplrkkvGIVFQFPEHQLFEETVEKDICFGPMNFGVSE---EDAKQKAREMIELvglpEELLARSPFELSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 139 VALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDD 192
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMED 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-191 |
5.64e-24 |
|
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: 99.95 E-value: 5.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG------------- 70
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-----PTSGSVLIDGtdinklkgkalrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 -RSQ-AMMFQEAG--EQFTMAT--------------------PREEIIFAMENLgksktefaDRLKLAsEFAEidslldQ 126
Cdd:cd03256 76 lRRQiGMIFQQFNliERLSVLEnvlsgrlgrrstwrslfglfPKEEKQRALAAL--------ERVGLL-DKAY------Q 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 127 KIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFD 191
Cdd:cd03256 141 RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVD 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-188 |
5.83e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.15 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGR-------SQ--- 73
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLE-----TPDSGRIVLNGRdlftnlpPRerr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 -AMMFQEAgeqftmA-----TPREEIIFAMENLGKSKTEFADR-LKLASEFaEIDSLLDQKIVTMSGGEKQRVALAVLVA 146
Cdd:COG1118 77 vGFVFQHY------AlfphmTVAENIAFGLRVRPPSKAEIRARvEELLELV-QLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 147 MDVDLFLLDEPFASVDPAARRFL---IGRLakLKEQGKTIIITDH 188
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELrrwLRRL--HDELGGTTVFVTH 192
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
240-426 |
5.96e-24 |
|
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: 99.58 E-value: 5.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFAIKQGR-PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTkLLDY--QGSLTWEGKEVAKLKE---RTYFQHVA 313
Cdd:cd03258 7 VSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCIN-GLERptSGSVLVDGTDLTLLSGkelRKARRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 314 QIFQNAsDQFMAITVKEELALSQKHA--SPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLI 391
Cdd:cd03258 86 MIFQHF-NLLSSRTVFENVALPLEIAgvPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 392 DEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRELGLTIVLITH 199
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-200 |
6.13e-24 |
|
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: 99.19 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLiGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAgeqf 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPP-----SSGTIRIDGQDVLKQPQKL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 tmatpREEIIFAMENLGKSKT----EFADRLKLASEF------AEIDSLL---------DQKIVTMSGGEKQRVALAVLV 145
Cdd:cd03264 71 -----RRRIGYLPQEFGVYPNftvrEFLDYIAWLKGIpskevkARVDEVLelvnlgdraKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 146 AMDVDLFLLDEPFASVDPAAR-RF--LIGRLAKlkeqGKTIIITDHLFDDYQGKVDGV 200
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERiRFrnLLSELGE----DRIVILSTHIVEDVESLCNQV 199
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-168 |
6.74e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.19 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPkyggqlTSGQVSLGGRS----------- 72
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTP------SSGEVRLNGRPlaawspwelar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 -QAMMFQEAGEQFtmATPREEIIfAM--ENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALA-VL--VA 146
Cdd:COG4559 76 rRAVLPQHSSLAF--PFTVEEVV-ALgrAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArVLaqLW 152
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 147 MDVD----LFLLDEPFASVDPA--------ARRF 168
Cdd:COG4559 153 EPVDggprWLFLDEPTSALDLAhqhavlrlARQL 186
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-192 |
6.84e-24 |
|
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: 99.10 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGdrEVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPkyggqlTSGQVSLGG----------RSQ 73
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETP------QSGRVLINGvdvtaappadRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQEaGEQFTMATPREEIifameNLGKS---KTEFADRLKLASEFAE--IDSLLDQKIVTMSGGEKQRVALAVLVAMD 148
Cdd:cd03298 73 SMLFQE-NNLFAHLTVEQNV-----GLGLSpglKLTAEDRQAIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 149 VDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDD 192
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPED 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
258-437 |
6.89e-24 |
|
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: 97.85 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYfQHVAQIFQNASdqfmaitvkeelalsq 336
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIKVLGKDIKKEPEEVK-RRIGYLPEEPS---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 337 khASPYFTPEvldqaladldlaDHMDqvvysLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQeK 416
Cdd:cd03230 84 --LYENLTVR------------ENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELK-K 143
|
170 180
....*....|....*....|.
gi 489717269 417 SGQTILLISHHFYGISTWCDY 437
Cdd:cd03230 144 EGKTILLSSHILEEAERLCDR 164
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-189 |
7.40e-24 |
|
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: 98.91 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLiGPTGCGKSTLLKIMAGLYPKYGGQLT-SGQVSLGGRSQ----------AMMFQEAgEQFTMATPR 90
Cdd:cd03297 16 KIDFDLNEEVTGIF-GASGAGKSTLLRCIAGLEKPDGGTIVlNGTVLFDSRKKinlppqqrkiGLVFQQY-ALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 91 EEIIFAMEnlGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLI 170
Cdd:cd03297 94 ENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180
....*....|....*....|.
gi 489717269 171 GRLAKLKE--QGKTIIITDHL 189
Cdd:cd03297 172 PELKQIKKnlNIPVIFVTHDL 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-188 |
1.03e-23 |
|
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: 98.37 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQ---------AM 75
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKninelrqkvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQeageQFTM---ATPREEIIFA-MENLGKSKtefADRLKLASEFAEIDSLLDQK---IVTMSGGEKQRVALAVLVAMD 148
Cdd:cd03262 81 VFQ----QFNLfphLTVLENITLApIKVKGMSK---AEAEERALELLEKVGLADKAdayPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 149 VDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-201 |
1.10e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQ-----------AMMFQEAGEQFTMATPR 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikqirkkvGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 91 EEIIFAMENLGKSKTEfADRL---KLA----SEfaeidSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDP 163
Cdd:PRK13649 105 KDVAFGPQNFGVSQEE-AEALareKLAlvgiSE-----SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 164 AARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVY 201
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVY 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
248-427 |
1.17e-23 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 99.81 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKlKERTYF--QHVAQIFQNASDQFM 324
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTsGKVTVDGLDTLD-EENLWEirKKVGMVFQNPDNQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 AITVKEELAlsqkhaspyFTPEVL-----------DQALADLDLADHMDQVVYSLSGGQKKKLEI---LLMLlsgQEVLL 390
Cdd:TIGR04520 92 GATVEDDVA---------FGLENLgvpreemrkrvDEALKLVGMEDFRDREPHLLSGGQKQRVAIagvLAMR---PDIII 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 391 IDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-188 |
1.65e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.98 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLggrSQA-----MMFQE 79
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL---AEAredtrLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 80 AgeqftMATPREEIIfamENLGKS-KTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPF 158
Cdd:PRK11247 90 A-----RLLPWKKVI---DNVGLGlKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 159 ASVDPAAR---RFLIGRLakLKEQGKTIIITDH 188
Cdd:PRK11247 162 GALDALTRiemQDLIESL--WQQHGFTVLLVTH 192
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-189 |
1.80e-23 |
|
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: 102.82 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTsgqvsLGGRSQAMMFQEAGEQ 83
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT-----LDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 84 FTMATPREEIIFA---MENLGKSKTEFAD--------RLKLASEFAEIDSLLDQKIVTM----SGGEKQRVALAVLVAMD 148
Cdd:TIGR02868 410 RVSVCAQDAHLFDttvRENLRLARPDATDeelwaaleRVGLADWLRALPDGLDTVLGEGgarlSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 149 VDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
248-426 |
2.37e-23 |
|
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: 102.99 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNasDQFMAI 326
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRILIDGIDLRQIDPASLRRQIGVVLQD--VFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALsqkhASPYFTPEVLDQALADLDLADH-------MDQVVY----SLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:COG2274 564 TIRENITL----GDPDATDEEIIEAARLAGLHDFiealpmgYDTVVGeggsNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQkcQEKSGQTILLISH 426
Cdd:COG2274 640 SALDAETEAIILENLR--RLLKGRTVIIIAH 668
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-179 |
2.67e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.30 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG----------R 71
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE-----RITSGEIWIGGrvvnelepadR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQAMMFQEAGEQFTMaTPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:PRK11650 77 DIAMVFQNYALYPHM-SVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180
....*....|....*....|....*...
gi 489717269 152 FLLDEPFASVDpaarrfligrlAKLKEQ 179
Cdd:PRK11650 156 FLFDEPLSNLD-----------AKLRVQ 172
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-186 |
2.69e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.91 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG--------- 70
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL-----KPQSGEIKIDGitiskenlk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 --RSQ-AMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAM 147
Cdd:PRK13632 80 eiRKKiGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKLKEQG-KTII-IT 186
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLIsIT 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-425 |
4.66e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.25 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLggrsqammfqeAGEQF 84
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQP-----DSGEILL-----------DGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMATPRE------EIIF----------AMEN--LGKSKTE--FADRLKLASEFAEI-DSL-----LDQKIVTMSGGEKQR 138
Cdd:COG1129 69 RFRSPRDaqaagiAIIHqelnlvpnlsVAENifLGREPRRggLIDWRAMRRRARELlARLgldidPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 139 VALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTII-----------ITDH---LFDdyqGKVDGVYRFK 204
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIyishrldevfeIADRvtvLRD---GRLVGTGPVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 205 GeqvdlLTKDEQALLLATEPIGLHFPLPENEPaafvmknfaikqGRPLLEQKELSIP-----------KGKVTLITGPNG 273
Cdd:COG1129 226 E-----LTEDELVRLMVGRELEDLFPKRAAAP------------GEVVLEVEGLSVGgvvrdvsfsvrAGEILGIAGLVG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 274 SGKSSLFKA---MTKLldYQGSLTWEGKEVAKlkeRTYFQHVAQ-------------IFQNASdqfmaitVKEELALS-- 335
Cdd:COG1129 289 AGRTELARAlfgADPA--DSGEIRLDGKPVRI---RSPRDAIRAgiayvpedrkgegLVLDLS-------IRENITLAsl 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 QKHASPYFTP-----EVLDQALADLDL-ADHMDQVVYSLSGG--QKkkleILL--MLLSGQEVLLIDEPLSGLDQKSIEQ 405
Cdd:COG1129 357 DRLSRGGLLDrrrerALAEEYIKRLRIkTPSPEQPVGNLSGGnqQK----VVLakWLATDPKVLILDEPTRGIDVGAKAE 432
|
490 500
....*....|....*....|
gi 489717269 406 VVQLLQKCQEKsGQTILLIS 425
Cdd:COG1129 433 IYRLIRELAAE-GKAVIVIS 451
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-189 |
6.00e-23 |
|
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: 94.80 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRsqammfqeageQF 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP-----DSGEILVDGK-----------EV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMATPREeiifaMENLGksktefadrlklasefaeidslldqkIVT---MSGGEKQRVALAVLVAMDVDLFLLDEPFASV 161
Cdd:cd03216 65 SFASPRD-----ARRAG--------------------------IAMvyqLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180
....*....|....*....|....*....
gi 489717269 162 DPAARRFLIGRLAKLKEQGKTII-ITDHL 189
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIfISHRL 142
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-188 |
8.64e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 101.35 E-value: 8.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYG-DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQAMMFQEAGE 82
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF-----QARSGEILLNGFSLKDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QFTMATPREEIIFA---MENL---GKSKTEfADRLKLASEFAEI-----------DSLLDQKIVTMSGGEKQRVALAVLV 145
Cdd:TIGR01193 548 QFINYLPQEPYIFSgsiLENLllgAKENVS-QDEIWAACEIAEIkddienmplgyQTELSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 146 AMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEqgKTIIITDH 188
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAH 667
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-176 |
9.65e-23 |
|
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: 96.64 E-value: 9.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLypkygGQLTSGQVSLGG----------RSQ 73
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-----ERPDSGTILFGGedatdvpvqeRNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQEAGeQFTMATPREEIIFAME----NLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDV 149
Cdd:cd03296 77 GFVFQHYA-LFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180
....*....|....*....|....*..
gi 489717269 150 DLFLLDEPFASVDPAARRFLIGRLAKL 176
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRL 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-192 |
1.12e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.36 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 13 SYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQAM--------MFQEAGEQF 84
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLArarigvvpQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMatpREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPA 164
Cdd:PRK13536 130 TV---RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180
....*....|....*....|....*...
gi 489717269 165 ARRFLIGRLAKLKEQGKTIIITDHLFDD 192
Cdd:PRK13536 207 ARHLIWERLRSLLARGKTILLTTHFMEE 234
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
7-188 |
1.14e-22 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 95.39 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ----------LTSGQVSLGGRSQAM 75
Cdd:TIGR02673 4 FHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQvriagedvnrLRGRQLPLLRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEageqFTMATPR---EEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:TIGR02673 84 VFQD----FRLLPDRtvyENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 153 LLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATH 195
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-188 |
1.37e-22 |
|
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: 95.58 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYggqltSGQVSLGGRSQAmmfqeageqf 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR-----SGSIRFDGRDIT---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 tmATPREEI-------------IFA----MENL-----GKSKTEFADRL-KLASEFAEIDSLLDQKIVTMSGGEKQRVAL 141
Cdd:cd03224 66 --GLPPHERaragigyvpegrrIFPeltvEENLllgayARRRAKRKARLeRVYELFPRLKERRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 142 AVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQ 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-188 |
1.40e-22 |
|
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: 96.26 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMM---- 76
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR-----PTSGRILFDGRDITGLpphr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 ---------FQEAG--EQFT---------MATPREEIIFAMENLGKSKTEFADRLKLASE---FAEIDSLLDQKIVTMSG 133
Cdd:COG0411 76 iarlgiartFQNPRlfPELTvlenvlvaaHARLGRGLLAALLRLPRARREEREARERAEElleRVGLADRADEPAGNLSY 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 134 GEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLK-EQGKTIIITDH 188
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEH 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-192 |
1.43e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPKYGGQLTSGQVSLGGRSQAMMFQE 79
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 80 AGEQFTMATP----REEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:PRK13537 84 VVPQFDNLDPdftvRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDD 192
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEE 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
248-427 |
1.67e-22 |
|
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: 94.04 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEVAKLKERTYFQHVAqifqnasdqfmai 326
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEILLDGKDLASLSPKELARKIA------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 tvkeelalsqkhaspyftpeVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:cd03214 77 --------------------YVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180
....*....|....*....|.
gi 489717269 407 VQLLQKCQEKSGQTILLISHH 427
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHD 157
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
248-446 |
1.76e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.24 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQnasdQFMA- 325
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLALLPQ----HHLTp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 --ITVKEELALSQkhaSPYFT---------PEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEP 394
Cdd:PRK11231 89 egITVRELVAYGR---SPWLSlwgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489717269 395 LSGLDQKSIEQVVQLLQKCQEKsGQTILLISHHFYGISTWCDYHLRLAGREL 446
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-208 |
1.83e-22 |
|
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: 95.04 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLT---SGQVSLGGRSQAMMFQEAG 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 EQFTMaTPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASV 161
Cdd:cd03269 81 LYPKM-KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 162 DPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRF-KGEQV 208
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLnKGRAV 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-230 |
1.92e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYG-----DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ-------LTSGQVSLGG-RSQ 73
Cdd:PRK13637 5 IENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvdITDKKVKLSDiRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 -AMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEID--SLLDQKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:PRK13637 85 vGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQGK-TIIITDHLFDD-----------YQGKV--DGVYR--FKgeQVDLLtkd 214
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDvakladriivmNKGKCelQGTPRevFK--EVETL--- 239
|
250
....*....|....*.
gi 489717269 215 eqalllatEPIGLHFP 230
Cdd:PRK13637 240 --------ESIGLAVP 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-179 |
2.65e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPkyggqlTSGQVSLGG----------RSQ 73
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKP------TEGQIFIDGedvthrsiqqRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:PRK11432 81 CMVFQSYA-LFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180
....*....|....*....|....*.
gi 489717269 154 LDEPFASVDPAARRFLIGRLAKLKEQ 179
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQ 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-189 |
2.82e-22 |
|
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: 94.21 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSqamMFQEAGEQF 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKP-----DSGEITFDGKS---YQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMATPREEIIFAMENLGKSKTEFADRLKLASEfAEIDSLLD---------QKIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:cd03268 73 RIGALIEAPGFYPNLTARENLRLLARLLGIRK-KRIDEVLDvvglkdsakKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-188 |
3.10e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.49 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGG---------- 70
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGediydpdvdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ---RSQAMM-FQeageqftMATP-----REEIIFAMENLG-KSKTEFADR----LKLASEFAEIDSLLDQKIVTMSGGEK 136
Cdd:COG1117 88 velRRRVGMvFQ-------KPNPfpksiYDNVAYGLRLHGiKSKSELDEIveesLRKAALWDEVKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489717269 137 QRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQgKTIIITDH 188
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTH 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-188 |
3.14e-22 |
|
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: 94.07 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE-----VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGrSQAMMFQE 79
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK-----LSGSVSVPG-SIAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 80 AGEQFtmATPREEIIFAMEnlgKSKTEFADRLKLASEFAEIDSLLD-------QKIVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:cd03250 75 PWIQN--GTIRENILFGKP---FDEERYEKVIKACALEPDLEILPDgdlteigEKGINLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 153 LLDEPFASVDPAARRFLI-----GRLAKlkeqGKTIIITDH 188
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFencilGLLLN----NKTRILVTH 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-189 |
3.24e-22 |
|
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: 95.15 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPKYGGQLT-----SGQVSL-------GGR 71
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgerRGGEDVwelrkriGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQAMMfqeagEQFTMATPREEII----FAM----ENLGKSKTEFADRLkLasEFAEIDSLLDQKIVTMSGGEKQRVALA- 142
Cdd:COG1119 84 SPALQ-----LRFPRDETVLDVVlsgfFDSiglyREPTDEQRERAREL-L--ELLGLAHLADRPFGTLSQGEQRRVLIAr 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489717269 143 VLVAmDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKT--IIITDHL 189
Cdd:COG1119 156 ALVK-DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtlVLVTHHV 203
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-188 |
4.31e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 94.19 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGD--REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQAmmfqeag 81
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY-----KPTSGSVLLDGTDIR------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 eQFTMATPREEIIFAM-----------ENLGKSKTEFAD-RLKLASEFAEIDSL-------LDQKI----VTMSGGEKQR 138
Cdd:cd03245 70 -QLDPADLRRNIGYVPqdvtlfygtlrDNITLGAPLADDeRILRAAELAGVTDFvnkhpngLDLQIgergRGLSGGQRQA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 139 VALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEqGKTIIITDH 188
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITH 197
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-188 |
4.77e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 92.66 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRsqammfqeAGE 82
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP-----TSGRVRLDGA--------DIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QFTMATPREEIIFAMENlgksktefadrlklasefaeiDSLLDQKIV--TMSGGEKQRVALAVLVAMDVDLFLLDEPFAS 160
Cdd:cd03246 68 QWDPNELGDHVGYLPQD---------------------DELFSGSIAenILSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180
....*....|....*....|....*...
gi 489717269 161 VDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
258-427 |
8.29e-22 |
|
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: 93.20 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEG----KEVAKLKERtyfqhVAQIFQNAS-DQfmAITVKEE 331
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGhdvvREPREVRRR-----IGIVFQDLSvDD--ELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 332 LALsqkHASPYFTP-----EVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:cd03265 94 LYI---HARLYGVPgaerrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180
....*....|....*....|.
gi 489717269 407 VQLLQKCQEKSGQTILLISHH 427
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHY 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-168 |
8.45e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPkyggqlTSGQVSLGGR------------ 71
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSP------DSGEVRLNGRpladwspaelar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQAMMFQeageQFTMATP--REEIIfAM--ENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALA-VLV- 145
Cdd:PRK13548 77 RRAVLPQ----HSSLSFPftVEEVV-AMgrAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArVLAq 151
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 146 ----AMDVDLFLLDEPFASVDPA--------ARRF 168
Cdd:PRK13548 152 lwepDGPPRWLLLDEPTSALDLAhqhhvlrlARQL 186
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
230-426 |
1.00e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 230 PLPENEPAAFVMKNFAIK--QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAKLKERT 307
Cdd:PRK11174 341 ELASNDPVTIEAEDLEILspDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 308 YFQHVAQIFQNAsdQFMAITVKEELALSQKHASpyftPEVLDQALADLDLADHMDQVVY-----------SLSGGQKKKL 376
Cdd:PRK11174 421 WRKHLSWVGQNP--QLPHGTLRDNVLLGNPDAS----DEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 377 EILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQkcQEKSGQTILLISH 426
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTH 542
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-188 |
1.14e-21 |
|
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: 97.36 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDR-EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQAMMFQEAG- 81
Cdd:TIGR02857 321 SLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 ----EQFTMATPREEIIFAmeNLGKSKTEFADRLKLAsEFAEIDSLLDQKIVTM--------SGGEKQRVALAVLVAMDV 149
Cdd:TIGR02857 401 vpqhPFLFAGTIAENIRLA--RPDASDAEIREALERA-GLDEFVAALPQGLDTPigeggaglSGGQAQRLALARAFLRDA 477
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 150 DLFLLDEPFASVDPAARRFLIGRLAKLKeQGKTIIITDH 188
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-435 |
1.16e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLT--FSYGD--REVIRDLSLTLPAGTFSLLIGPTGCGKS-TLLKIMAGL------YPKyGGQLTSGQVSLGG 70
Cdd:PRK15134 3 QPLLAIENLSvaFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpsppvvYPS-GDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQ----------AMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRlklasefAEIDSLLDQKIV----------- 129
Cdd:PRK15134 82 SEQtlrgvrgnkiAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAAR-------GEILNCLDRVGIrqaakrltdyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 130 -TMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLK-EQGKTIIITDHLFDDYQGKVDGVYRFK-GE 206
Cdd:PRK15134 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLSIVRKLADRVAVMQnGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 207 QVDllTKDEQAL-----------LLATEPIGLHFPLPENEPAAFVMKN----FAIKQG--------RPLLEQKELSIPKG 263
Cdd:PRK15134 235 CVE--QNRAATLfsapthpytqkLLNSEPSGDPVPLPEPASPLLDVEQlqvaFPIRKGilkrtvdhNVVVKNISFTLRPG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 264 KVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAKLKERTY--FQHVAQI-FQNASDQF-----MAITVKEELALS 335
Cdd:PRK15134 313 ETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLlpVRHRIQVvFQDPNSSLnprlnVLQIIEEGLRVH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 QKHASPYFTPEVLDQALADLDL-ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQ 414
Cdd:PRK15134 393 QPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQ 472
|
490 500
....*....|....*....|.
gi 489717269 415 EKSGQTILLISHHFYGISTWC 435
Cdd:PRK15134 473 QKHQLAYLFISHDLHVVRALC 493
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
250-426 |
1.18e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.29 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 250 RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAITV 328
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsGEIKIDGITISKENLKEIRKKIGIIFQNPDNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 KEELA--LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:PRK13632 102 EDDIAfgLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180
....*....|....*....|
gi 489717269 407 VQLLQKCQEKSGQTILLISH 426
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITH 201
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-223 |
1.40e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.61 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRS--QAMMFQEAGe 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGaeRGVVFQNEG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QFTMATPREEIIFAMENLGKSKTEfadRLKLASEF---AEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFA 159
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQ---RLEIAHQMlkkVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 160 SVDPAARrfligrlaklkEQGKTIIITdhlfddyqgkvdgVYRFKGEQVDLLTKD-EQALLLATE 223
Cdd:PRK11248 158 ALDAFTR-----------EQMQTLLLK-------------LWQETGKQVLLITHDiEEAVFMATE 198
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-197 |
2.28e-21 |
|
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: 92.09 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPKYG-----GQLTSG----QVSLGGRSQAMMFQEageqFTMATPR- 90
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGtirvnGQDVSDlrgrAIPYLRRKIGVVFQD----FRLLPDRn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 91 --EEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRF 168
Cdd:cd03292 95 vyENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 169 LIGRLAKLKEQGKTIIITDH---LFDDYQGKV 197
Cdd:cd03292 175 IMNLLKKINKAGTTVVVATHakeLVDTTRHRV 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-181 |
2.53e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG----------RSQA 74
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLE-----HQTSGHIRFHGtdvsrlhardRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAGeQFTMATPREEIIFAMENLGKSK--TEFADRLKLAS--EFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:PRK10851 78 FVFQHYA-LFRHMTVFDNIAFGLTVLPRRErpNAAAIKAKVTQllEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQGK 181
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELK 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-201 |
4.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQ-----------AMMFQEAGEQFTMATPR 90
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeikpvrkkvGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 91 EEIIFAMENLGKSKTEFAdrlKLASEFAEIDSL----LDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAAR 166
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAE---KIAAEKLEMVGLadefWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 167 RFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVY 201
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVY 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-192 |
4.62e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYG---DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ-------LTSGQVSLGG 70
Cdd:PRK13650 1 MSNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQiiidgdlLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQAMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:PRK13650 81 HKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQ-GKTIIITDHLFDD 192
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
250-426 |
5.36e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 250 RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL----DYQGSLTWEGkevAKLKERTYF---QHVAQIFQNASDQ 322
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddNPNSKITVDG---ITLTAKTVWdirEKVGIVFQNPDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 FMAITVKEELA--LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:PRK13640 97 FVGATVGDDVAfgLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180
....*....|....*....|....*.
gi 489717269 401 KSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITH 202
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
248-426 |
6.09e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.68 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQnaSDQFMA- 325
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDsGEVLVDGLDVATTPSRELAKRLAILRQ--ENHINSr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALSQkhaSPY----FTPE---VLDQALADLDLAD----HMDQvvysLSGGQKKKLEILLMLLSGQEVLLIDEP 394
Cdd:COG4604 90 LTVRELVAFGR---FPYskgrLTAEdreIIDEAIAYLDLEDladrYLDE----LSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 395 LSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG4604 163 LNNLDMKHSVQMMKLLRRLADELGKTVVIVLH 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
244-447 |
7.40e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.11 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 244 FAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQ 322
Cdd:PRK13647 12 FRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 FMAITVKEELA-------LSQKHASpyftpEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:PRK13647 92 VFSSTVWDDVAfgpvnmgLDKDEVE-----RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489717269 396 SGLDQKSIEQVVQLLQKCQeKSGQTILLISHHFYGISTWCDYHLRL-AGRELA 447
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLkEGRVLA 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
240-426 |
9.24e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 91.30 E-value: 9.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFAIKQGR-PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERtyfqhVAQIFQ 317
Cdd:COG1116 13 VSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKpTSGEVLVDGKPVTGPGPD-----RGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 NAsdqfmAI----TVKE--ELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLI 391
Cdd:COG1116 88 EP-----ALlpwlTVLDnvALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 392 DEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLWQETGKTVLFVTH 197
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
258-429 |
9.63e-21 |
|
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: 90.19 E-value: 9.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQ----HVAQ---IFQNasdqfmaITVK 329
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRFDGRDITGLPPHERARagigYVPEgrrIFPE-------LTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELALSQKHASPYFTPEVLDQALaDL--DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVV 407
Cdd:cd03224 94 ENLLLGAYARRRAKRKARLERVY-ELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 408 QLLQKCQEKsGQTILL----------ISHHFY 429
Cdd:cd03224 173 EAIRELRDE-GVTILLveqnarfaleIADRAY 203
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
258-427 |
1.02e-20 |
|
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: 90.26 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYfQHVAQIFQ-NASDQFMaiTVKEEL--- 332
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTsGTAYINGYSIRTDRKAAR-QSLGYCPQfDALFDEL--TVREHLrfy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 333 ----ALSQKHAspyftPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQ 408
Cdd:cd03263 100 arlkGLPKSEI-----KEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD 174
|
170
....*....|....*....
gi 489717269 409 LLQKcqEKSGQTILLISHH 427
Cdd:cd03263 175 LILE--VRKGRSIILTTHS 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-427 |
1.05e-20 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 94.31 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRS----QAMMFQ 78
Cdd:PRK10938 2 SSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeqlQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 79 E----------AGEQFTMATPREEIifameNLGKSKTEFAdrLKLASEFAeIDSLLDQKIVTMSGGEKQRVALAVLVAMD 148
Cdd:PRK10938 82 EwqrnntdmlsPGEDDTGRTTAEII-----QDEVKDPARC--EQLAQQFG-ITALLDRRFKYLSTGETRKTLLCQALMSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 149 VDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVD--GVYR-----FKGEQVDLLTKDEQALLLA 221
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQfaGVLAdctlaETGEREEILQQALVAQLAH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 222 TEPI-GLHFP----------LPENEPaAFVMKNFAIKQG-RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKllD- 288
Cdd:PRK10938 234 SEQLeGVQLPepdepsarhaLPANEP-RIVLNNGVVSYNdRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--Dh 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 289 ---YQGSLT------------WEGKE----VAK---LKERT-----------YFQHVAqIFQNASDQfmaitvkeelalS 335
Cdd:PRK10938 311 pqgYSNDLTlfgrrrgsgetiWDIKKhigyVSSslhLDYRVstsvrnvilsgFFDSIG-IYQAVSDR------------Q 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 QKHAspyftpevlDQALADLDLADHM-DQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD-------QKSIEQVV 407
Cdd:PRK10938 378 QKLA---------QQWLDILGIDKRTaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnrqlvRRFVDVLI 448
|
490 500
....*....|....*....|.
gi 489717269 408 qllqkcqeKSGQTILL-ISHH 427
Cdd:PRK10938 449 --------SEGETQLLfVSHH 461
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
247-427 |
1.21e-20 |
|
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: 90.71 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLK---ERTYFQHVAQIFQ--NAS 320
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQqfNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 321 DQFMAITVKEELALSQKHA----SPYFTPEVLDQALADLD---LADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDE 393
Cdd:cd03256 91 ERLSVLENVLSGRLGRRSTwrslFGLFPKEEKQRALAALErvgLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 394 PLSGLDQKSIEQVVQLL-QKCQEKsGQTILLISHH 427
Cdd:cd03256 171 PVASLDPASSRQVMDLLkRINREE-GITVIVSLHQ 204
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-191 |
1.32e-20 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 90.44 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYG-DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGG----------RSQ 73
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkklrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQE-----------------AGEQFTMAT-----PREEIIFAMENLgksktefaDRLKLAsEFAeidsllDQKIVTM 131
Cdd:TIGR02315 82 GMIFQHynlierltvlenvlhgrLGYKPTWRSllgrfSEEDKERALSAL--------ERVGLA-DKA------YQRADQL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 132 SGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFD 191
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVD 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-188 |
1.52e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG----------RSQA 74
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE-----QPTAGQIMLDGvdlshvppyqRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:PRK11607 95 MMFQSYA-LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 155 DEPFASVDPAAR-RFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK11607 174 DEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTH 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-189 |
2.11e-20 |
|
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: 88.14 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGrSQAMMFQEAGE 82
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL-----KPQQGEITLDG-VPVSDLEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QFTMATPREEIIFA---MENLGKsktefadRLklasefaeidslldqkivtmSGGEKQRVALAVLVAMDVDLFLLDEPFA 159
Cdd:cd03247 75 SLISVLNQRPYLFDttlRNNLGR-------RF--------------------SGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 160 SVDPAARRFLIGRLAKLKEqGKTII-ITDHL 189
Cdd:cd03247 128 GLDPITERQLLSLIFEVLK-DKTLIwITHHL 157
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-425 |
2.39e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDreVI--RDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQA---- 74
Cdd:COG3845 2 MPPALELRGITKRFGG--VVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLY-----QPDSGEILIDGKPVRirsp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 ---------MMFQEageqFTMA---TPREEIIFAMENLGKSK----------TEFADRLKLasefaEIDslLDQKIVTMS 132
Cdd:COG3845 75 rdaialgigMVHQH----FMLVpnlTVAENIVLGLEPTKGGRldrkaarariRELSERYGL-----DVD--PDAKVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 133 GGEKQRVA-LAVLVAmDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHlfddyqgKVDGVYRF-------- 203
Cdd:COG3845 144 VGEQQRVEiLKALYR-GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH-------KLREVMAIadrvtvlr 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 204 KGEQVD-LLTKDEQALLLATEPIGLHFPLPENEPAAfvmknfaiKQGRPLLEQKELSIP--KGKVTL------------- 267
Cdd:COG3845 216 RGKVVGtVDTAETSEEELAELMVGREVLLRVEKAPA--------EPGEVVLEVENLSVRddRGVPALkdvslevrageil 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 268 -ITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQH-VAQI----FQNASdqFMAITVKEELALSQKHAS 340
Cdd:COG3845 288 gIAGVAGNGQSELAEALAGLRPPAsGSIRLDGEDITGLSPRERRRLgVAYIpedrLGRGL--VPDMSVAENLILGRYRRP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 341 PYFTPEVLDQALADlDLADHM-----------DQVVYSLSGG--QKkkleilLML---LSGQ-EVLLIDEPLSGLDQKSI 403
Cdd:COG3845 366 PFSRGGFLDRKAIR-AFAEELieefdvrtpgpDTPARSLSGGnqQK------VILareLSRDpKLLIAAQPTRGLDVGAI 438
|
490 500
....*....|....*....|..
gi 489717269 404 EQVVQLLQKcQEKSGQTILLIS 425
Cdd:COG3845 439 EFIHQRLLE-LRDAGAAVLLIS 459
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
249-426 |
2.83e-20 |
|
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: 87.63 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE--RTYFQHVAQIFQNAsdqfma 325
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLTDLEDelPPLRRRIGMVFQDF------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 itvkeelALsqkhaspYFTPEVLDQaladldladhmdqVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQ 405
Cdd:cd03229 86 -------AL-------FPHLTVLEN-------------IALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180
....*....|....*....|.
gi 489717269 406 VVQLLQKCQEKSGQTILLISH 426
Cdd:cd03229 139 VRALLKSLQAQLGITVVLVTH 159
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-188 |
3.22e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.59 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQAMMfqeag 81
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKM----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 eQFTMATPREEIIFAMEN-------------------LGKSKTEFADRLKLASEFA----EIDSLLDQKIVTMSGGEKQR 138
Cdd:PRK14247 76 -DVIELRRRVQMVFQIPNpipnlsifenvalglklnrLVKSKKELQERVRWALEKAqlwdEVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 139 VALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQgKTIIITDH 188
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-200 |
3.88e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.22 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 18 EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQ-----------AMMFQEAGEQFTM 86
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirpvrkriGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 87 ATPREEIIFAMENLGKSKTEFADR-LKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAA 165
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDEVKNYaHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 166 RRFLIGRLAKLK-EQGKTIIITDHLFDDYQGKVDGV 200
Cdd:PRK13646 181 KRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEV 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-188 |
4.24e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSqamMFQEAGEQF 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP-----DSGEVLWDGEP---LDPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 -----------TMaTPREEII-FAMenL-GKSKTEFADRLK-LASEFaEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:COG4152 74 gylpeerglypKM-KVGEQLVyLAR--LkGLSKAEAKRRADeWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSH 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-262 |
4.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.86 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-----PKY-----GGQLTSGQVSLGGRS 72
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnPNSkitvdGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 QAMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:PRK13640 86 VGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 153 LLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDDYQGK------VDGVYRFKGEQVDLLTKDEqaLLlatEPI 225
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMAdqvlvlDDGKLLAQGSPVEIFSKVE--ML---KEI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 489717269 226 GLHFPlpenepaaFVMKnfaIKQgrpLLEQKELSIPK 262
Cdd:PRK13640 241 GLDIP--------FVYK---LKN---KLKEKGISVPQ 263
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-201 |
4.57e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 10 LTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPKYGGQLTSGQ------VSLGGRSQAMMFQEAG 81
Cdd:PRK13652 9 LCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEpitkenIREVRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 EQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASV 161
Cdd:PRK13652 89 DQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 162 DPAARRFLIGRLAKL-KEQGKTIIITDHLFDDYQGKVDGVY 201
Cdd:PRK13652 169 DPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIY 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-188 |
4.97e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.01 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAmmFQEAGEQF 84
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-----PAAGTIKLDGGDID--DPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMA----------TPREEIIFAMENLGKSKTEFADrlklASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:PRK13539 76 HYLghrnamkpalTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 155 DEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-188 |
5.15e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 88.51 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG-------------R 71
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE-----PDSGTITVDGedltdskkdinklR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQ-AMMFQeageQFTM---ATPREEIIFA-MENLGKSKTEfadrlklASEFAEidSLLDQkiVTM-----------SGGE 135
Cdd:COG1126 77 RKvGMVFQ----QFNLfphLTVLENVTLApIKVKKMSKAE-------AEERAM--ELLER--VGLadkadaypaqlSGGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 136 KQRVALAVLVAMDVDLFLLDEPFASVDPAarrfLIGR----LAKLKEQGKTIIITDH 188
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDPE----LVGEvldvMRDLAKEGMTMVVVTH 194
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
251-427 |
5.35e-20 |
|
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: 87.96 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTyfQHVAQIFQNASdQFMAITVK 329
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVTGVPPER--RNIGMVFQDYA-LFPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELA--LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVV 407
Cdd:cd03259 91 ENIAfgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
|
170 180
....*....|....*....|
gi 489717269 408 QLLQKCQEKSGQTILLISHH 427
Cdd:cd03259 171 EELKELQRELGITTIYVTHD 190
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-179 |
6.53e-20 |
|
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: 90.55 E-value: 6.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLypkygGQLTSGQVSLGG----------------RSQAMMFQEAgEQFT 85
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGL-----ERPDSGRIRLGGevlqdsargiflpphrRRIGYVFQEA-RLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 86 MATPREEIIFAMENLGKSktefADRLKLAS--EFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDP 163
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRA----ERRISFDEvvELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170
....*....|....*.
gi 489717269 164 AARRFLIGRLAKLKEQ 179
Cdd:COG4148 167 ARKAEILPYLERLRDE 182
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-192 |
9.52e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 9.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDRE------VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIM-AGLYPkyggqlTSGQVSLGG--- 70
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMnALLIP------SEGKVYVDGldt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ---------RSQA-MMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVA 140
Cdd:PRK13633 75 sdeenlwdiRNKAgMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489717269 141 LAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDD 192
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEE 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
258-427 |
1.69e-19 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 87.35 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE---RTYFQHVAQIFQnasdQFMAI---TVKE 330
Cdd:TIGR02315 23 LNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITKLRGkklRKLRRRIGMIFQ----HYNLIerlTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 331 ELALSQKHASPY-------FTPEVLDQALADLD---LADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:TIGR02315 99 NVLHGRLGYKPTwrsllgrFSEEDKERALSALErvgLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDP 178
|
170 180
....*....|....*....|....*..
gi 489717269 401 KSIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:TIGR02315 179 KTSKQVMDYLKRINKEDGITVIINLHQ 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
247-447 |
1.91e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKERTYFQHVAQifQNASDQFMA 325
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTRQALQKNLVAYVPQ--SEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALSQ-------KHASPYfTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:PRK15056 95 VLVEDVVMMGRyghmgwlRRAKKR-DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489717269 399 DQKSIEQVVQLLQKCQEKsGQTILLISHHFYGISTWCDYHLRLAGRELA 447
Cdd:PRK15056 174 DVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVKGTVLA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
249-448 |
2.06e-19 |
|
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: 86.79 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQ---HVAQIFQNASdQFM 324
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGLSEAELYRlrrRMGMLFQSGA-LFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 AITVKEELA--LSQKHASPyfTPEVLDQALADLD---LADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:cd03261 91 SLTVFENVAfpLREHTRLS--EEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489717269 400 QKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCDYHLRLAGRELAF 448
Cdd:cd03261 169 PIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-188 |
2.18e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.20 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRS-------- 72
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNiyspdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 ------QAMMFQEAGEqFTMATPREEIIFAME--NLGKSKTEFADR----LKLASEFAEIDSLLDQKIVTMSGGEKQRVA 140
Cdd:PRK14267 81 ievrreVGMVFQYPNP-FPHLTIYDNVAIGVKlnGLVKSKKELDERvewaLKKAALWDEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 141 LAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQgKTIIITDH 188
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTH 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-436 |
3.24e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAGEQF 84
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-----TKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMATPREEI-----IFAMENL--GKSKT---------EFADRLKLASEFAEIDSL---LDQKIVTMSGGEKQRVALAVLV 145
Cdd:PRK09700 81 GIGIIYQELsvideLTVLENLyiGRHLTkkvcgvniiDWREMRVRAAMMLLRVGLkvdLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 146 AMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH-------LFDDYQGKVDGVYRFKGEQVDLLTKDEQAL 218
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHklaeirrICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 219 LLATEpigLHFPLPENEPAA--------FVMKNFaIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ 290
Cdd:PRK09700 241 MVGRE---LQNRFNAMKENVsnlahetvFEVRNV-TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 291 -GSLTWEGKEvakLKERTYFQHV----AQIFQNASDQ--FMAITVKEELALSQ-------KHASPYFTP----EVLDQAL 352
Cdd:PRK09700 317 gGEIRLNGKD---ISPRSPLDAVkkgmAYITESRRDNgfFPNFSIAQNMAISRslkdggyKGAMGLFHEvdeqRTAENQR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 353 ADLDLADH-MDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEkSGQTILLISHHFYGI 431
Cdd:PRK09700 394 ELLALKCHsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEI 472
|
....*
gi 489717269 432 STWCD 436
Cdd:PRK09700 473 ITVCD 477
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-447 |
3.51e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.57 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVS-LGGrsqammfqeageqfT 85
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGAR-----KIQQGRVEvLGG--------------D 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 86 MATP--REEI---IFAM---------------ENL-------GKSKTEFADRlklasefaeIDSLLD------------Q 126
Cdd:NF033858 65 MADArhRRAVcprIAYMpqglgknlyptlsvfENLdffgrlfGQDAAERRRR---------IDELLRatglapfadrpaG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 127 KivtMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARR-F--LIGRLAKLKEQGKTIIIT---------DHL--FDD 192
Cdd:NF033858 136 K---LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqFweLIDRIRAERPGMSVLVATaymeeaerfDWLvaMDA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 193 yqGKVdgvyrfkgeqvdLLTKDEQALLLATEP-------IGLhfpLPENE---PAAFVMKNF-AIKQGRPLLEQKEL--- 258
Cdd:NF033858 213 --GRV------------LATGTPAELLARTGAdtleaafIAL---LPEEKrrgHQPVVIPPRpADDDDEPAIEARGLtmr 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 259 ------------SIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVaklkertyfqhvaqifqNASDQ--- 322
Cdd:NF033858 276 fgdftavdhvsfRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGEAWLFGQPV-----------------DAGDIatr 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 ----FMA--------ITVKEELALsqkHASPYFTPEV-----LDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSG 385
Cdd:NF033858 339 rrvgYMSqafslygeLTVRQNLEL---HARLFHLPAAeiaarVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 386 QEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTIlLISHHFYGISTWCDyhlRL----AGRELA 447
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDGVTI-FISTHFMNEAERCD---RIslmhAGRVLA 477
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-200 |
3.55e-19 |
|
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: 85.88 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE----VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYGGQLTSG----QVSLGGRSQAM 75
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATVDGfdvvKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGV 200
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRV 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-157 |
4.04e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQ-VSLGgrsqamMFQEAGEQ 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtVKIG------YFDQHQEE 389
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 84 FTM-ATPREEIIFAMEnlGKSKTEFADRLK--LaseFAEIDslLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEP 157
Cdd:COG0488 390 LDPdKTVLDELRDGAP--GGTEQEVRGYLGrfL---FSGDD--AFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-188 |
4.79e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAGEQ- 83
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISP-----TSGTLLFEGEDISTLKPEIYRQq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 84 --FTMATP-------REEIIFAMENLGKSKTEFADRLKLAsEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:PRK10247 83 vsYCAQTPtlfgdtvYDNLIFPWQIRNQQPDPAIFLDDLE-RFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 155 DEPFASVDPAARRF---LIGRLAklKEQGKTIIITDH 188
Cdd:PRK10247 162 DEITSALDESNKHNvneIIHRYV--REQNIAVLWVTH 196
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
230-441 |
5.30e-19 |
|
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: 89.27 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 230 PLPENEPAAFVMKN--FAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKER 306
Cdd:TIGR02857 313 PVTAAPASSLEFSGvsVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 307 TYFQHVAQIFQNAsdQFMAITVKEELALSQKHASPYFTPEVLDQA-LADL--DLADHMDQVVYS----LSGGQKKKLEIL 379
Cdd:TIGR02857 393 SWRDQIAWVPQHP--FLFAGTIAENIRLARPDASDAEIREALERAgLDEFvaALPQGLDTPIGEggagLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489717269 380 LMLLSGQEVLLIDEPLSGLDQKSIEQVVQ-LLQKCQeksGQTILLISHHFyGISTWCDYHLRL 441
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEaLRALAQ---GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-194 |
5.53e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYGGQLTSGqVSLGGRSQ--------AMM 76
Cdd:PRK13644 4 LENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVSG-IDTGDFSKlqgirklvGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 FQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDE 156
Cdd:PRK13644 83 FQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 157 PFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQ 194
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH 200
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
240-426 |
6.19e-19 |
|
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: 84.96 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFaikQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKERtyFQHVAQIFQn 318
Cdd:cd03268 6 LTKTY---GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQKNIEA--LRRIGALIE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 ASDQFMAITVKEELALSQK-HASPYftpEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSG 397
Cdd:cd03268 80 APGFYPNLTARENLRLLARlLGIRK---KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180
....*....|....*....|....*....
gi 489717269 398 LDQKSIEQVVQLLQKCQeKSGQTILLISH 426
Cdd:cd03268 157 LDPDGIKELRELILSLR-DQGITVLISSH 184
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
258-427 |
6.25e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.89 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ---GSLTWEGKEVAKLK--ERTY------FQHVAQIfqnasdqfMAI 326
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtsGSILLDGEDILELSpdERARagiflaFQYPVEI--------PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEEL--ALSQKHASPYFTPEV---LDQALADLDLADHMDQ--VVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:COG0396 93 SVSNFLrtALNARRGEELSAREFlklLKEKMKELGLDEDFLDryVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180
....*....|....*....|....*...
gi 489717269 400 QKSIEQVVQLLQKCQEKsGQTILLISHH 427
Cdd:COG0396 173 IDALRIVAEGVNKLRSP-DRGILIITHY 199
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-188 |
7.08e-19 |
|
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: 84.33 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMMFQEAGEQF 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR-----PDSGEVRWNGTPLAEQRDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMA----------TPREEIIFAMENLGKSKTEFADRLklasEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:TIGR01189 76 LYLghlpglkpelSALENLHFWAAIHGGAQRTIEDAL----AAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 155 DEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-188 |
7.22e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.70 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG----------RSQA 74
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE-----TPDSGRIMLDGqdithvpaenRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:PRK09452 90 TVFQSYA-LFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 155 DEPFASVDPAARRFLIGRLAKLKEQ-GKTIIITDH 188
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTH 203
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
249-427 |
8.52e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWE-GKEVAKLKERTyfqhvaqifqnASDQFMAI 326
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTsGTVRRAgGARVAYVPQRS-----------EVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQ-KHASPYFTP-----EVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:NF040873 73 TVRDLVAMGRwARRGLWRRLtrddrAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 489717269 401 KSIEQVVQLLQKCQEKsGQTILLISHH 427
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHD 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
248-426 |
9.03e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.84 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEvakLKERTYFQ---HVAQIFQNASDQF 323
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMV---LSEETVWDvrrQVGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 MAITVKEELALS-QKHASPYFT-PEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:PRK13635 95 VGATVQDDVAFGlENIGVPREEmVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180
....*....|....*....|....*
gi 489717269 402 SIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITH 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-189 |
1.11e-18 |
|
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: 84.08 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAGEQF 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-----LAGRVLLNGGPLDFQRDSIARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 ----------TMATPREEIIFAMENLGKSKTEFA-DRLKLAsefaeidSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:cd03231 76 lylghapgikTTLSVLENLRFWHADHSDEQVEEAlARVGLN-------GFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 154 LDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-188 |
1.19e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRS-QAMMFQEAG 81
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP-----AHGHVWLDGEHiQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 EQFTM-----ATPREEIIFAMENLGKS---------KTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAM 147
Cdd:PRK10253 81 RRIGLlaqnaTTPGDITVQELVARGRYphqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-166 |
1.26e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyGGQLTSGQVSLGGRSQA---------- 74
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS--PAFSASGEVLLNGRRLTalpaeqrrig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEA--------GEQFTMATPReeiifamenlGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALA-VLV 145
Cdd:COG4136 80 ILFQDDllfphlsvGENLAFALPP----------TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLrALL 149
|
170 180
....*....|....*....|.
gi 489717269 146 AmDVDLFLLDEPFASVDPAAR 166
Cdd:COG4136 150 A-EPRALLLDEPFSKLDAALR 169
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-185 |
1.38e-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: 84.59 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG-----------R 71
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFY-----DVDSGRILIDGhdvrdytlaslR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQ-AMMFQEAgEQFTmATPREEIIFAMENLGKSKTEFADRLKLASEFaeIDSL---LDQKI----VTMSGGEKQRVALAV 143
Cdd:cd03251 76 RQiGLVSQDV-FLFN-DTVAENIAYGRPGATREEVEEAARAANAHEF--IMELpegYDTVIgergVKLSGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIII 185
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVI 193
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
248-427 |
1.59e-18 |
|
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: 84.75 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL--DYQGSLTWEGKE-----VAKLKERtyFQHVAQIFQnas 320
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLppTYGNDVRLFGERrggedVWELRKR--IGLVSPALQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 321 DQFMA-ITVkEELALSQKHAS----PYFTPEVLDQA---LADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLID 392
Cdd:COG1119 89 LRFPRdETV-LDVVLSGFFDSiglyREPTDEQRERArelLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 393 EPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
249-428 |
1.66e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEV---AKLKERTYFqhVAQIFQNASDQFM 324
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTgdfSKLQGIRKL--VGIVFQNPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 AITVKEELALSQKHA--SPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:PRK13644 92 GRTVEEDLAFGPENLclPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180
....*....|....*....|....*.
gi 489717269 403 IEQVVQLLQKCQEKsGQTILLISHHF 428
Cdd:PRK13644 172 GIAVLERIKKLHEK-GKTIVYITHNL 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
246-427 |
1.67e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 246 IKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKER-----TYFQHVAQIFQna 319
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARpDAGEVLWQGEPIRRQRDEyhqdlLYLGHQPGIKT-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 320 sdqfmAITVKEELALSQKHASPYfTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:PRK13538 88 -----ELTALENLRFYQRLHGPG-DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|....*....
gi 489717269 400 QKSIEQVVQLL-QKCQEksGQTILLISHH 427
Cdd:PRK13538 162 KQGVARLEALLaQHAEQ--GGMVILTTHQ 188
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-191 |
1.74e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPkyggqlTSGQVSLGGR----------- 71
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKP------SSGRILFDGKpidysrkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 ---SQAMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMD 148
Cdd:PRK13636 80 lreSVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 149 VDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFD 191
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDID 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-191 |
1.76e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 10 LTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG--------------RSQA 74
Cdd:PRK13639 7 LKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL-----KPTSGEVLIKGepikydkksllevrKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:PRK13639 82 IVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 155 DEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFD 191
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVD 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-234 |
2.44e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.76 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSY---GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGG-------QLTSGQVSLGG 70
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQAMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:PRK13642 81 RKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQGK-TIIITDHLFDDYQGKVDGVYRFKGEQVDLLTKDEqalLLATE----PI 225
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSE---LFATSedmvEI 237
|
....*....
gi 489717269 226 GLHFPLPEN 234
Cdd:PRK13642 238 GLDVPFSSN 246
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-188 |
2.56e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.93 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLypkygGQLTSGQVSLGGRSqammFQEAGEQF 84
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL-----ARPDAGEVLWQGEP----IRRQRDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 tmatpREEIIF------------AMENLgksktEFADRL-KLASEFAEIDSL--------LDQKIVTMSGGEKQRVALAV 143
Cdd:PRK13538 73 -----HQDLLYlghqpgikteltALENL-----RFYQRLhGPGDDEALWEALaqvglagfEDVPVRQLSAGQQRRVALAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
242-400 |
2.58e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.30 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 242 KNFAIK-QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD----YQGSLTWEGKEVAKLKerTYFQHVAQIF 316
Cdd:COG4136 5 ENLTITlGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsASGEVLLNGRRLTALP--AEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 317 QNASdQFMAITVKEELAL--------SQKHAspyftpeVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEV 388
Cdd:COG4136 83 QDDL-LFPHLSVGENLAFalpptigrAQRRA-------RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170
....*....|..
gi 489717269 389 LLIDEPLSGLDQ 400
Cdd:COG4136 155 LLLDEPFSKLDA 166
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
258-427 |
3.08e-18 |
|
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: 84.43 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVA---KLKERTYFQHVAQIFQNASDQFMAITVKEELA 333
Cdd:TIGR04521 26 LTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKpTSGTVTIDGRDITakkKKKLKDLRKKVGLVFQFPEHQLFEETVYKDIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 334 -------LSQKhaspyftpEVLDQALADLDLA----DHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:TIGR04521 106 fgpknlgLSEE--------EAEERVKEALELVgldeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177
|
170 180
....*....|....*....|....*
gi 489717269 403 IEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:TIGR04521 178 RKEILDLFKRLHKEKGLTVILVTHS 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-188 |
3.16e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPkyggqlTSGQVSLGGRS-QAMMFQEAGE 82
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGtLTP------TAGTVLVAGDDvEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QftMATPREEIIFAMENLGKSKTEF--------------ADR--LKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVA 146
Cdd:PRK09536 78 R--VASVPQDTSLSFEFDVRQVVEMgrtphrsrfdtwteTDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 147 MDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
268-437 |
3.22e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 268 ITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAITVKEELAlsqkhaspyFTPE 346
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTVEQDIA---------FGPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 347 VL-----------DQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQE 415
Cdd:PRK13652 106 NLgldeetvahrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170 180
....*....|....*....|..
gi 489717269 416 KSGQTILLISHHFYGISTWCDY 437
Cdd:PRK13652 186 TYGMTVIFSTHQLDLVPEMADY 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-191 |
3.28e-18 |
|
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: 84.23 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGG----------------RSQAMMFQEAGeQ 83
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP-----TSGKVLIDGqdiaamsrkelrelrrKKISMVFQSFA-L 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 84 FTMATPREEIIFAMENLGKSKTEfadRLKLASEFAEIDSL---LDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFAS 160
Cdd:cd03294 114 LPHRTVLENVAFGLEVQGVPRAE---REERAAEALELVGLegwEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 161 VDPAARRFLIGRLAKL-KEQGKTIIITDHLFD 191
Cdd:cd03294 191 LDPLIRREMQDELLRLqAELQKTIVFITHDLD 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-206 |
3.30e-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: 83.61 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFS-----LLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQAMmfqEAGEQFTMATPREEIIFA 96
Cdd:cd03237 12 EFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYI---KADYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 97 MENLGKSKTEFADRLKlasefaeIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRF---LIGRL 173
Cdd:cd03237 89 FYTHPYFKTEIAKPLQ-------IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMaskVIRRF 161
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 174 AKLKEqgKTIIITDH--LFDDYQGkvDGVYRFKGE 206
Cdd:cd03237 162 AENNE--KTAFVVEHdiIMIDYLA--DRLIVFEGE 192
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-191 |
3.92e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.75 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 19 VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIM-AGLYPKYGG--------------------------QLTSG----QVS 67
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnALLLPDTGTiewifkdeknkkktkekekvleklviQKTRFkkikKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 68 LGGRSQAMMFQEAGEQFTMATPREEIIFAMENLGKSKTEfadRLKLASEFAEI----DSLLDQKIVTMSGGEKQRVALAV 143
Cdd:PRK13651 102 EIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEE---AKKRAAKYIELvgldESYLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFD 191
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-191 |
4.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.29 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDR-----EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGG-------- 70
Cdd:PRK13645 6 DIILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikev 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ----RSQAMMFQEAGEQFTMATPREEIIFAMENLGKSKTE-------FADRLKLASEFAEidslldQKIVTMSGGEKQRV 139
Cdd:PRK13645 86 krlrKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEaykkvpeLLKLVQLPEDYVK------RSPFELSGGQKRRV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489717269 140 ALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFD 191
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMD 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-192 |
4.05e-18 |
|
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: 83.28 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPKYGGQLTSG-QVSLGGRSQAMMFQEAGeQFTMATPREEIIFAM 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGkQITEPGPDRMVVFQNYS-LLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 98 E--NLGKSKTEfadRLKLASEFAEIDSL---LDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGR 172
Cdd:TIGR01184 80 DrvLPDLSKSE---RRAIVEEHIALVGLteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180
....*....|....*....|.
gi 489717269 173 LAKL-KEQGKTIIITDHLFDD 192
Cdd:TIGR01184 157 LMQIwEEHRVTVLMVTHDVDE 177
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
243-436 |
4.82e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.13 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 243 NFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEV---AK--LKERtyfQHVAQIF 316
Cdd:PRK13636 12 NYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKPIdysRKglMKLR---ESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 317 QNASDQFMAITVKEE-------LALSQKHASpyftpEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVL 389
Cdd:PRK13636 89 QDPDNQLFSASVYQDvsfgavnLKLPEDEVR-----KRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 390 LIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCD 436
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCD 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
14-200 |
7.04e-18 |
|
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: 84.78 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 14 YGDREVirDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQAM-----------MFQEAgE 82
Cdd:TIGR02142 9 LGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppekrrigyVFQEA-R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QFTMATPREEIIFAMENL-GKSKTEFADRLklaSEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASV 161
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRArPSERRISFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 162 DPAARRFLIGRLAKL-KEQGKTIIITDHLFDDYQGKVDGV 200
Cdd:TIGR02142 163 DDPRKYEILPYLERLhAEFGIPILYVSHSLQEVLRLADRV 202
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
249-427 |
7.06e-18 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 82.69 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY---QGSLTWEGKEVAKLK--ERTY------FQHVAQI-- 315
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYevtSGTILFKGQDLLELEpdERARaglflaFQYPEEIpg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 316 ------FQNASDQFMAITVKEELALSQKHaspyftpEVLDQALADLDLADHMDQ--VVYSLSGGQKKKLEILLMLLSGQE 387
Cdd:TIGR01978 92 vsnlefLRSALNARRSARGEEPLDLLDFE-------KLLKEKLALLDMDEEFLNrsVNEGFSGGEKKRNEILQMALLEPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 388 VLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISHH 427
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLREP-DRSFLIITHY 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-188 |
7.33e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 85.96 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSY--GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSqamMFQE 79
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP-----PTAGSVRLDGAD---LSQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 80 AGEQF----------------TMAtpreeiifamENLgksktefadrlklaSEFAEIDsllDQKIV-------------- 129
Cdd:COG4618 400 DREELgrhigylpqdvelfdgTIA----------ENI--------------ARFGDAD---PEKVVaaaklagvhemilr 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 130 --------------TMSGGEKQRVALA-------VLVamdvdlfLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG4618 453 lpdgydtrigeggaRLSGGQRQRIGLAralygdpRLV-------VLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
241-440 |
7.58e-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: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 241 MKNFAIK-QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMT-KLLDYQGSLTWegkevaklKERTYFQHVAQifqn 318
Cdd:cd03221 3 LENLSKTyGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTW--------GSTVKIGYFEQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 asdqfmaitvkeelalsqkhaspyftpevldqaladldladhmdqvvysLSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:cd03221 71 -------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 399 DQKSIEQVVQLLQKCQeksgQTILLISHHFYGISTWCD--YHLR 440
Cdd:cd03221 102 DLESIEALEEALKEYP----GTVILVSHDRYFLDQVATkiIELE 141
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-192 |
7.59e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 81.44 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTF------SYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlypKYGGQLTSGQVSLGGRSQamm 76
Cdd:cd03213 2 VTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG---RRTGLGVSGEVLINGRPL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 fqeageqfTMATPREEIIFAM------------ENLgksktEFAdrlklasefAEIDSLldqkivtmSGGEKQRVALAVL 144
Cdd:cd03213 76 --------DKRSFRKIIGYVPqddilhptltvrETL-----MFA---------AKLRGL--------SGGERKRVSIALE 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 145 VAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH--------LFDD 192
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpsseifeLFDK 181
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-188 |
8.78e-18 |
|
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: 81.42 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlYPKYggQLTSGQVSLGG----------RSQA 74
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKY--EVTEGEILFKGeditdlppeeRARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 ---MMFQEageqftmatPrEEIifamenlgksktefaDRLKLASEFAEIDslldqkiVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:cd03217 78 gifLAFQY---------P-PEI---------------PGVKNADFLRYVN-------EGFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-199 |
9.56e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.01 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG-------RS 72
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV-----RLASGKISILGqptrqalQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 QAMMFQEAGEQFTMATPR--EEIIFA-----MENLGKSKTEfaDRLKLASEFAEIDSL--LDQKIVTMSGGEKQRVALAV 143
Cdd:PRK15056 78 NLVAYVPQSEEVDWSFPVlvEDVVMMgryghMGWLRRAKKR--DRQIVTAALARVDMVefRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH------LFDDYQGKVDG 199
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHnlgsvtEFCDYTVMVKG 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-192 |
1.06e-17 |
|
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: 81.93 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 16 DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyGGQLTSGQVSLGG--RSQAMMFQEAG--EQFTMATP-- 89
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNGqpRKPDQFQKCVAyvRQDDILLPgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 90 --REEIIFAMENLGKSKTEFADRLKLASEFAEID----SLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDP 163
Cdd:cd03234 97 tvRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDlaltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 164 AARRFLIGRLAKLKEQGKTIIITDH--------LFDD 192
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHqprsdlfrLFDR 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
248-427 |
1.16e-17 |
|
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: 85.10 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNAsdQFMAI 326
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDpLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDA--HLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQKHASPYFTPEVLDQA-LADL--DLADHMDQVVY----SLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:TIGR02868 424 TVRENLRLARPDATDEELWAALERVgLADWlrALPDGLDTVLGeggaRLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 489717269 400 QKSIEQVVQLLQKCQekSGQTILLISHH 427
Cdd:TIGR02868 504 AETADELLEDLLAAL--SGRTVVLITHH 529
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
249-442 |
1.21e-17 |
|
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: 81.00 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLK-----ERTYFQHVAQIFQnasdq 322
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPpLAGRVLLNGGPLDFQRdsiarGLLYLGHAPGIKT----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 fmAITVKEELalsqKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:cd03231 87 --TLSVLENL----RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 403 IEQVVQLL-QKCQekSGQTILLISHHFYGISTWCDYHLRLA 442
Cdd:cd03231 161 VARFAEAMaGHCA--RGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-399 |
1.53e-17 |
|
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: 84.99 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 6 TIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQvslgGRSQAMMFQEAGEQF 84
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP----GIKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TmATPREEIIFAMENLGKSKTEF-----------ADRLKLASEFAE------------IDSLL------------DQKIV 129
Cdd:TIGR03719 82 T-KTVRENVEEGVAEIKDALDRFneisakyaepdADFDKLAAEQAElqeiidaadawdLDSQLeiamdalrcppwDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 130 TMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKeqGKTIIIT-DHLFDD---------------- 192
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAVThDRYFLDnvagwileldrgrgip 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 193 YQG-----------------KVDGVYRF-------------KGEQV----------DLLTKDEQAlllATEPIGLHFPLP 232
Cdd:TIGR03719 239 WEGnysswleqkqkrleqeeKEESARQKtlkrelewvrqspKGRQAkskarlaryeELLSQEFQK---RNETAEIYIPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 233 EN------EpAAFVMKNFAikqGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMT-KLLDYQGSLTWeGKEVaklke 305
Cdd:TIGR03719 316 PRlgdkviE-AENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITgQEQPDSGTIEI-GETV----- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 306 rtyfqHVAQIFQNASDQFMAITVKEELAlsqkhaspyftpEVLDQaladLDLADH---------------MDQ--VVYSL 368
Cdd:TIGR03719 386 -----KLAYVDQSRDALDPNKTVWEEIS------------GGLDI----IKLGKReipsrayvgrfnfkgSDQqkKVGQL 444
|
490 500 510
....*....|....*....|....*....|.
gi 489717269 369 SGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-188 |
1.54e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 23 LSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkygGQltsGQVSLGGRS------------QAMMFQEAGEQFTMA--- 87
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP---GQ---GEILLNGRPlsdwsaaelarhRAYLSQQQSPPFAMPvfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 88 ---------TPREEIIFAMENLgksktefADRLKLasefaeiDSLLDQKIVTMSGGEKQRVALAVlVAMDVD-------- 150
Cdd:COG4138 89 ylalhqpagASSEAVEQLLAQL-------AEALGL-------EDKLSRPLTQLSGGEWQRVRLAA-VLLQVWptinpegq 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSH 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-188 |
1.57e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.68 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 13 SYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQL-TSGQVSLGGRSQAMMF-QEAG---EQFTM- 86
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLiVDGLKVNDPKVDERLIrQEAGmvfQQFYLf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 87 --ATPREEIIFA-MENLGKSKtefADRLKLASEfaeidsLLDqKI----------VTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:PRK09493 90 phLTALENVMFGpLRVRGASK---EEAEKQARE------LLA-KVglaerahhypSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 154 LDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-186 |
1.61e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.75 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKI---MAGLYPKYggqLTSGQVSLGG------- 70
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPEV---TITGSIVYNGhniyspr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 -------RSQAMMFQEAGEqFTMaTPREEIIFAMENLGKSKTEFADR-----LKLASEFAEIDSLLDQKIVTMSGGEKQR 138
Cdd:PRK14239 79 tdtvdlrKEIGMVFQQPNP-FPM-SIYENVVYGLRLKGIKDKQVLDEaveksLKGASIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 139 VALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIIT 186
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
254-426 |
1.71e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 254 EQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTW-EGKEVAKLKERTYFQHVAQIFQNASDQfMAITVKEEL 332
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWlDGEHIQHYASKEVARRIGLLAQNATTP-GDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 333 ALSQKHASPYFT------PEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:PRK10253 103 ARGRYPHQPLFTrwrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180
....*....|....*....|
gi 489717269 407 VQLLQKCQEKSGQTILLISH 426
Cdd:PRK10253 183 LELLSELNREKGYTLAAVLH 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
258-427 |
1.75e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.34 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLK--ERTyfqhVAQIFQnasDQ--FMAITVKEEL 332
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPpDSGRILWNGQDLTALPpaERP----VSMLFQ---ENnlFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 333 AL----------SQKHAspyftpevLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:COG3840 93 GLglrpglkltaEQRAQ--------VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180
....*....|....*....|....*
gi 489717269 403 IEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:COG3840 165 RQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
247-426 |
1.78e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPL----LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEV-AKLKE---RTYFQHVAQIFQ 317
Cdd:PRK13646 13 QKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITItHKTKDkyiRPVRKRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 NASDQFMAITVKEELALSQKHASPYFTpEVLDQA---LADLDLA-DHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDE 393
Cdd:PRK13646 93 FPESQLFEDTVEREIIFGPKNFKMNLD-EVKNYAhrlLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 394 PLSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSH 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
262-427 |
1.83e-17 |
|
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: 80.80 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 262 KGKVTLITGPNGSGKSSLFKAMTklldyqGSLTWEGKEVaKLKERTYF------------QHVAQIFQNASdQFMAITVK 329
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIA------GLEKPDGGTI-VLNGTVLFdsrkkinlppqqRKIGLVFQQYA-LFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQL 409
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170
....*....|....*...
gi 489717269 410 LQKCQEKSGQTILLISHH 427
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHD 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-436 |
1.89e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.47 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-----------LY------------------- 54
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 55 --PKYGGQLTSGQVSLGGRSQ----------AMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRlklASEFAEIDS 122
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDFWNLSDklrrrirkriAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGR---AVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 123 LlDQKIV----TMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDDYQGKV 197
Cdd:TIGR03269 158 L-SHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 198 D-GVYRFKGEQVDLLTKDE-QALLLATepiglhFPLPENEPaafvmknfAIKQGRPLLEQKELS---------------- 259
Cdd:TIGR03269 237 DkAIWLENGEIKEEGTPDEvVAVFMEG------VSEVEKEC--------EVEVGEPIIKVRNVSkryisvdrgvvkavdn 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 260 ----IPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTW---------------EGKEVAK------LKERTYFQHvAQ 314
Cdd:TIGR03269 303 vsleVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvdmtkpgpDGRGRAKryigilHQEYDLYPH-RT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 315 IFQNASDQfMAITVKEELALSQkhaspyfTPEVLDQALADLDLADH-MDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDE 393
Cdd:TIGR03269 382 VLDNLTEA-IGLELPDELARMK-------AVITLKMVGFDEEKAEEiLDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489717269 394 PLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCD 436
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-192 |
1.97e-17 |
|
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: 80.88 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDREVIRDLSLTLPAG-TFSLLiGPTGCGKSTLLKIMAGLYPKYGGQLT---------SGQVSlggRSQAMM 76
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGeIFGLL-GPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrePREVR---RRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 FQEAGEqftmatprEEIIFAMENL-------GKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQR--VALAVLVAM 147
Cdd:cd03265 79 FQDLSV--------DDELTGWENLyiharlyGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRleIARSLVHRP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489717269 148 DVdLFlLDEPFASVDPAARRFLIGRLAKLK-EQGKTIIITDHLFDD 192
Cdd:cd03265 151 EV-LF-LDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEE 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
258-426 |
2.59e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.66 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEV-----AKLKERtyfQHVAQIFQNASDQFMAITVKEE 331
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGEPIkydkkSLLEVR---KTVGIVFQNPDDQLFAPTVEED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 332 LAlsqkhaspyFTP--------EV---LDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:PRK13639 100 VA---------FGPlnlglskeEVekrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180
....*....|....*....|....*.
gi 489717269 401 KSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:PRK13639 171 MGASQIMKLLYDLNKE-GITIIISTH 195
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
208-444 |
2.80e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.09 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 208 VDLLTKDEQALLLATEPIGLHFPLPENEPAAFVMKNFAIK--QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTK 285
Cdd:COG4178 332 VDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLRtpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 286 LLDY-QGSLTW-EGKEVAKLKERTYFQHVaqifqnasdqfmaiTVKEelALSQKHASPYFTPEVLDQALADL---DLADH 360
Cdd:COG4178 412 LWPYgSGRIARpAGARVLFLPQRPYLPLG--------------TLRE--ALLYPATAEAFSDAELREALEAVglgHLAER 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 361 MDQVV---YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQkcQEKSGQTILLISHHfygiSTWCDY 437
Cdd:COG4178 476 LDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGHR----STLAAF 549
|
250
....*....|
gi 489717269 438 H---LRLAGR 444
Cdd:COG4178 550 HdrvLELTGD 559
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-188 |
2.92e-17 |
|
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: 80.70 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDR----EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPkyggqlTSGQVSLGG--------- 70
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRP------TSGSVLVDGtdltllsgk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ------RSQAMMFQEAGeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVL 144
Cdd:cd03258 76 elrkarRRIGMIFQHFN-LLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 145 VAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITH 199
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
249-432 |
3.13e-17 |
|
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: 79.71 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERtYFQHVAQI-FQNASDQfmAI 326
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRpDSGEVRWNGTPLAEQRDE-PHENILYLgHLPGLKP--EL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQK-HASPYFTPEvldQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQ 405
Cdd:TIGR01189 89 SALENLHFWAAiHGGAQRTIE---DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|....*..
gi 489717269 406 VVQLLQKCQEKSGqTILLISHHFYGIS 432
Cdd:TIGR01189 166 LAGLLRAHLARGG-IVLLTTHQDLGLV 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-184 |
3.64e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.17 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSY-----GDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKimaGLYPKYggQLTSGQVslggrsq 73
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLK---CIYGNY--LPDSGSI------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 amMFQEAGEQFTMAT--PRE-------EIIF----------------AMENL---GKSKTEfadrlklASEFAEidSLLD 125
Cdd:COG4778 69 --LVRHDGGWVDLAQasPREilalrrrTIGYvsqflrviprvsaldvVAEPLlerGVDREE-------ARARAR--ELLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 126 Q-KI---------VTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTII 184
Cdd:COG4778 138 RlNLperlwdlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
3.75e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.95 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQL-------TSGQVSLGGRSQAM 75
Cdd:PRK13648 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaiTDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:PRK13648 88 VFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIIT-----------DHLFDDYQGKVdgvyrFKGEQVDLLTKDEQALLlateP 224
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISithdlseameaDHVIVMNKGTV-----YKEGTPTEIFDHAEELT----R 238
|
....*...
gi 489717269 225 IGLHFPLP 232
Cdd:PRK13648 239 IGLDLPFP 246
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
248-426 |
3.92e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGK--EVAKLKERTYFQHVAQIFQNASDQFM 324
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 AITVKEELALSQKH---ASPYFTPEVlDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:PRK13638 92 YTDIDSDIAFSLRNlgvPEAEITRRV-DEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180
....*....|....*....|....*
gi 489717269 402 SIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:PRK13638 171 GRTQMIAIIRRIVAQ-GNHVIISSH 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-425 |
4.47e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 13 SYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAGEQFTM-ATPRE 91
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPP-----DSGTLEIGGNPCARLTPAKAHQLGIyLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 92 EIIFA----MEN--LGKSKTEFADRlKLASEFAEIDSLL--DQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDP 163
Cdd:PRK15439 95 PLLFPnlsvKENilFGLPKRQASMQ-KMKQLLAALGCQLdlDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 164 AARRFLIGRLAKLKEQGKTIIITDH-LFDDYQ--GKV----DGVYRFKGEqVDLLTKDE--QAL------LLATEPIGLH 228
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHkLPEIRQlaDRIsvmrDGTIALSGK-TADLSTDDiiQAItpaareKSLSASQKLW 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 229 FPLPENEPAAfvmknfaiKQGRPLLEQKELS----------IPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEG 297
Cdd:PRK15439 253 LELPGNRRQQ--------AAGAPVLTVEDLTgegfrnisleVRAGEILGLAGVVGAGRTELAETLYGLRPARgGRIMLNG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 298 KEVAKLKERTYFQ----HVAQIFQnASDQFMAITVKEELALSQKHASPYFTPE-----VLDQALADLDLA-DHMDQVVYS 367
Cdd:PRK15439 325 KEINALSTAQRLArglvYLPEDRQ-SSGLYLDAPLAWNVCALTHNRRGFWIKParenaVLERYRRALNIKfNHAEQAART 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 368 LSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLIS 425
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFIS 460
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-188 |
4.66e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQ--VSLggrsqaMMFQEA 80
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedISL------LPLHAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 GEQFTMATPREEIIF----AMENLGK--------SKTEFADRLK-LASEFaEIDSLLDQKIVTMSGGEKQRVALAVLVAM 147
Cdd:PRK10895 76 ARRGIGYLPQEASIFrrlsVYDNLMAvlqirddlSAEQREDRANeLMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
257-427 |
5.40e-17 |
|
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: 79.52 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 257 ELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKerTYFQHVAQIFQNaSDQFMAITVKEELALS 335
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEpASGSIKVNDQSHTGLA--PYQRPVSMLFQE-NNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 QKHASPY--FTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQK- 412
Cdd:TIGR01277 95 LHPGLKLnaEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQl 174
|
170
....*....|....*
gi 489717269 413 CQEKSgQTILLISHH 427
Cdd:TIGR01277 175 CSERQ-RTLLMVTHH 188
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-192 |
6.10e-17 |
|
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: 79.68 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 14 YGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG-----------RSQAMMFQEAGE 82
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL-----QPTSGEVRVAGlvpwkrrkkflRRIGVVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD 162
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 163 PAA----RRFLigrLAKLKEQGKTIIITDHLFDD 192
Cdd:cd03267 186 VVAqeniRNFL---KEYNRERGTTVLLTSHYMKD 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-188 |
6.99e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.73 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlYPKYggQLTSGQVSLGG----------RSQA 74
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKY--EVTSGSILLDGedilelspdeRARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 ---MMFQE----AG---EQF--TMATP-REEIIFAMENLGKSKtEFADRLKLASEFAEIDslLDqkiVTMSGGEKQRVAL 141
Cdd:COG0396 78 gifLAFQYpveiPGvsvSNFlrTALNArRGEELSAREFLKLLK-EKMKELGLDEDFLDRY--VN---EGFSGGEKKRNEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 142 AVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
249-399 |
8.71e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.77 E-value: 8.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFmAIT 327
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTpSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLAF-PFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKE--ELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLE---ILLMLLSGQE----VLLIDEPLSGL 398
Cdd:COG4559 92 VEEvvALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQlarVLAQLWEPVDggprWLFLDEPTSAL 171
|
.
gi 489717269 399 D 399
Cdd:COG4559 172 D 172
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
258-426 |
8.95e-17 |
|
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: 78.73 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKE--RTYFQHVAQIFQNAsDQFMAITVKEELAL 334
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKLTDDKKniNELRQKVGMVFQQF-NLFPHLTVLENITL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 SQKHASPYFTPEVLDQALADLD---LADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQ 411
Cdd:cd03262 100 APIKVKGMSKAEAEERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMK 179
|
170
....*....|....*
gi 489717269 412 KCQEkSGQTILLISH 426
Cdd:cd03262 180 DLAE-EGMTMVVVTH 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
253-426 |
9.32e-17 |
|
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: 79.05 E-value: 9.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKErtyfqHVAQIFQNASdQFMAITVKE- 330
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGEPVTGPGP-----DRGYVFQQDA-LLPWLTVLDn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 331 -ELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQL 409
Cdd:cd03293 94 vALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE 173
|
170
....*....|....*..
gi 489717269 410 LQKCQEKSGQTILLISH 426
Cdd:cd03293 174 LLDIWRETGKTVLLVTH 190
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-188 |
9.54e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLT-FSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkYGgqltSGQVSL--GGRsqaMMF- 77
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP-YG----SGRIARpaGAR---VLFl 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 78 -Q----------------EAGEQFtmatPREEIIFAME--NLGKskteFADRLklaSEFAEIDSLLdqkivtmSGGEKQR 138
Cdd:COG4178 432 pQrpylplgtlreallypATAEAF----SDAELREALEavGLGH----LAERL---DEEADWDQVL-------SLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489717269 139 VALAVLVAMDVDLFLLDEPFASVDPAARRFLigrLAKLKEQ--GKTIIITDH 188
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAAL---YQLLREElpGTTVISVGH 542
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
5-188 |
1.04e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 79.23 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlYPKYggQLTSGQVSLGGRS-QAMMFQE---A 80
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-HPSY--EVTSGTILFKGQDlLELEPDErarA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 GEQFTMATPRE--------------EIIFAMENLGKSKT-EFADRLKLASEFAEID-SLLDQKI-VTMSGGEKQRVALAV 143
Cdd:TIGR01978 78 GLFLAFQYPEEipgvsnleflrsalNARRSARGEEPLDLlDFEKLLKEKLALLDMDeEFLNRSVnEGFSGGEKKRNEILQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
258-427 |
1.11e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGK-VTLItGPNGSGKSSLFKAM--TKLLDyQGSLTWEGKEVAKLKERTYFQHVAQIFQN-----ASDqfMaiTVK 329
Cdd:COG1101 27 LTIEEGDfVTVI-GSNGAGKSTLLNAIagSLPPD-SGSILIDGKDVTKLPEYKRAKYIGRVFQDpmmgtAPS--M--TIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELAL-SQKHASPYFTPEVLDQ---------ALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:COG1101 101 ENLALaYRRGKRRGLRRGLTKKrrelfrellATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
170 180
....*....|....*....|....*...
gi 489717269 400 QKSIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:COG1101 181 PKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-188 |
1.11e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ-LTSGQVSLGGRSQAMMFQEA 80
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEiLLDAQPLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 --GEQFTMA---TPREeiIFAMEN------LGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDV 149
Cdd:PRK10575 89 ylPQQLPAAegmTVRE--LVAIGRypwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 150 DLFLLDEPFASVDPAAR---RFLIGRLAklKEQGKTIIITDH 188
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQvdvLALVHRLS--QERGLTVIAVLH 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-188 |
1.11e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLT-------------SGQVSLGGRSQ 73
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdfsktpsDKAIRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQeageQFTM---ATPREEIIFA-MENLGKSKTE-------FADRLKLAsEFAEIDSLldqkivTMSGGEKQRVALA 142
Cdd:PRK11124 85 GMVFQ----QYNLwphLTVQQNLIEApCRVLGLSKDQalaraekLLERLRLK-PYADRFPL------HLSGGQQQRVAIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489717269 143 VLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH 199
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
231-446 |
1.12e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 231 LPENEPAAFVMKNFAIK-QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTK---------LLDYQGSLTWEGKEV 300
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRvPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRhqppsegeiLLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 301 AKlkertyfqHVAQIFQNASdQFMAITVKEELALSQkhaSPYFTP---------EVLDQALADLDLADHMDQVVYSLSGG 371
Cdd:PRK10575 84 AR--------KVAYLPQQLP-AAEGMTVRELVAIGR---YPWHGAlgrfgaadrEKVEEAISLVGLKPLAHRLVDSLSGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 372 QKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCDYHLRLAGREL 446
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
258-436 |
1.33e-16 |
|
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: 78.91 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERtyfqHVAQI---FQNASDQFMAITVKEELA 333
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGLVPWKRRKK----FLRRIgvvFGQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 334 LsqkHASPYFTPEV-----LDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQ 408
Cdd:cd03267 118 L---LAAIYDLPPArfkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180
....*....|....*....|....*...
gi 489717269 409 LLQKCQEKSGQTILLISHHFYGISTWCD 436
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALAR 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
258-427 |
1.98e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLdyqgsLTWEGKEVAKLKERTYFQHVAQI-------FQNASDQFMAITVKE 330
Cdd:PRK13633 31 LEVKKGEFLVILGRNGSGKSTIAKHMNALL-----IPSEGKVYVDGLDTSDEENLWDIrnkagmvFQNPDNQIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 331 ELAlsqkhaspyFTPEVL-----------DQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:PRK13633 106 DVA---------FGPENLgippeeirervDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180
....*....|....*....|....*...
gi 489717269 400 QKSIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHY 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-431 |
2.02e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 81.37 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 35 LIGPTGCGKSTLLKIMAG-LYP----------------KYGG--------QLTSGQVSLGGRSQamMFQEAGEQFTmATP 89
Cdd:COG1245 104 ILGPNGIGKSTALKILSGeLKPnlgdydeepswdevlkRFRGtelqdyfkKLANGEIKVAHKPQ--YVDLIPKVFK-GTV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 90 REeIIFAMENLGKSKtEFADRLklasefaEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD-----PA 164
Cdd:COG1245 181 RE-LLEKVDERGKLD-ELAEKL-------GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlNV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 165 ARrfLIGRLAklkEQGKTIIITDH------LFDDY----QGKvDGVY--------------------------RFKGEQV 208
Cdd:COG1245 252 AR--LIRELA---EEGKYVLVVEHdlaildYLADYvhilYGE-PGVYgvvskpksvrvginqyldgylpeenvRIRDEPI 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 209 DLLTKDEQAllLATEPIGLHFPlpenepaAFVMK--NFAikqgrplLEQKELSIPKGKVTLITGPNGSGKSSlfkaMTKL 286
Cdd:COG1245 326 EFEVHAPRR--EKEEETLVEYP-------DLTKSygGFS-------LEVEGGEIREGEVLGIVGPNGIGKTT----FAKI 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 287 LdyQGSLTWEGKEVAKLKERTYF-QHVaqifqnASDQFMaiTVKEEL--ALSQKHASPYFTPEVLDQaladLDLADHMDQ 363
Cdd:COG1245 386 L--AGVLKPDEGEVDEDLKISYKpQYI------SPDYDG--TVEEFLrsANTDDFGSSYYKTEIIKP----LGLEKLLDK 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 364 VVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDqksIEQ---VVQLLQKCQEKSGQTILLISHHFYGI 431
Cdd:COG1245 452 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD---VEQrlaVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-188 |
2.18e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.95 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGqvslggrsqammfqeageqf 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 tmatpreeiifamenlgkSKTEFAdrlklasefaeidsLLDQkivtMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPA 164
Cdd:cd03221 61 ------------------STVKIG--------------YFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180
....*....|....*....|....
gi 489717269 165 ARRFLIGRlakLKEQGKTIIITDH 188
Cdd:cd03221 105 SIEALEEA---LKEYPGTVILVSH 125
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-437 |
2.26e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.39 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 35 LIGPTGCGKSTLLKIMAG-LYPKYGG------------------------QLTSGQVSLGGRSQamMFQEAGEQFTmATP 89
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGeLIPNLGDyeeepswdevlkrfrgtelqnyfkKLYNGEIKVVHKPQ--YVDLIPKVFK-GKV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 90 REEIIFAMENlGKSKtEFADRLklasefaEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD-----PA 164
Cdd:PRK13409 181 RELLKKVDER-GKLD-EVVERL-------GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrlNV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 165 ARrfLIGRLAKlkeqGKTIIITDHlfD----DY--------QGKvDGVY--------------------------RFKGE 206
Cdd:PRK13409 252 AR--LIRELAE----GKYVLVVEH--DlavlDYladnvhiaYGE-PGAYgvvskpkgvrvgineylkgylpeenmRIRPE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 207 QVDLLTKDEQAllLATEPIGLHFPlpenepaafvmkNFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTkl 286
Cdd:PRK13409 323 PIEFEERPPRD--ESERETLVEYP------------DLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLA-- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 287 ldyqGSLTW-EGKEVAKLKERTYFQHVaqifqnASDQFMaiTVKEELA-LSQKHASPYFTPEVLDQaladLDLADHMDQV 364
Cdd:PRK13409 387 ----GVLKPdEGEVDPELKISYKPQYI------KPDYDG--TVEDLLRsITDDLGSSYYKSEIIKP----LQLERLLDKN 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 365 VYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDqksIEQ---VVQLLQKCQEKSGQTILLISHHFYGIstwcDY 437
Cdd:PRK13409 451 VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD---VEQrlaVAKAIRRIAEEREATALVVDHDIYMI----DY 519
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
249-426 |
2.40e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.83 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQNASdqFMAIT 327
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTsGTLLFEGEDISTLKPEIYRQQVSYCAQTPT--LFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQ--KHASPyfTPEVLDQALADLDLADHM-DQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIE 404
Cdd:PRK10247 97 VYDNLIFPWqiRNQQP--DPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|..
gi 489717269 405 QVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
249-427 |
2.85e-16 |
|
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: 77.18 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY---QGSLTWEGKEVAKLK--ERtyfqhvaqifqnasdqf 323
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevtEGEILFKGEDITDLPpeER----------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 maitVKEELALSQKhaSPYFTPEVldqaladlDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSI 403
Cdd:cd03217 75 ----ARLGIFLAFQ--YPPEIPGV--------KNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180
....*....|....*....|....
gi 489717269 404 EQVVQLLQKCQEKsGQTILLISHH 427
Cdd:cd03217 141 RLVAEVINKLREE-GKSVLIITHY 163
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-188 |
3.23e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.09 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQL------------TSGQVSLGGR 71
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrdKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQ--------AMMFQEAgEQFTMATPREEIIFA-MENLGKSKTEFADRLKLASEFAEIDSLLDQKI-VTMSGGEKQRVAL 141
Cdd:PRK10619 85 NQlrllrtrlTMVFQHF-NLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 142 AVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTH 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
247-426 |
3.37e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.40 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERtyfqHVAQ-------IFQN 318
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERpTSGQVLVNGQDLSRLKRR----EIPYlrrrigvVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 A---SDQfmaiTVKEELALS------QKHASPYFTPEVLDQaladLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVL 389
Cdd:COG2884 88 FrllPDR----TVYENVALPlrvtgkSRKEIRRRVREVLDL----VGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 390 LIDEPLSGLDQKSIEQVVQLLQKCQeKSGQTILLISH 426
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATH 195
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-188 |
3.74e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIM-------------AGLYPKYGGQLTSGQVSLGG 70
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdsgqlniAGHQFDFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQAMMFQeageQFTM---ATPREEIIFA-MENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVA 146
Cdd:COG4161 82 QKVGMVFQ----QYNLwphLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 147 MDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTH 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-191 |
4.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE-----VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYG----GQLTSGQVSLGGRSQ- 73
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGtiqvGDIYIGDKKNNHELIt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 -----------------AMMFQEAGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEID-SLLDQKIVTMSGGE 135
Cdd:PRK13631 102 npyskkiknfkelrrrvSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 136 KQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFD 191
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
238-445 |
4.88e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.77 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 238 AFVMKNFAIK-QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKeVAKLKERTY-------- 308
Cdd:PRK14258 7 AIKVNNLSFYyDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGR-VEFFNQNIYerrvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 309 -FQHVAQIFQNASdqFMAITVKEELALSQKHASpyFTPEV-----LDQALADLDLADHMDQVVY----SLSGGQKKKLEI 378
Cdd:PRK14258 86 lRRQVSMVHPKPN--LFPMSVYDNVAYGVKIVG--WRPKLeiddiVESALKDADLWDEIKHKIHksalDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 379 LLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCDYHLRLAGRE 445
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-192 |
5.55e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.93 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYgDREVIRdLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPKyggqltSGQVSLGG----------RSQ 73
Cdd:PRK10771 2 LKLTDITWLY-HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGfLTPA------SGSLTLNGqdhtttppsrRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQEaGEQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:PRK10771 74 SMLFQE-NNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 154 LDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDHLFDD 192
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLED 192
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
258-426 |
5.57e-16 |
|
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: 76.94 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLL--DyQGSLTWEGKEVAKLKERTYFQHVAQI---FQNA---SDqfmaITVK 329
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLrpD-SGEILVDGQDITGLSEKELYELRRRIgmlFQGGalfDS----LTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELALS-QKHASpyFTPEVLDQ----ALADLDLADHMDQVVYSLSGGQKKKLEI--LLMLLSgqEVLLIDEPLSGLDQKS 402
Cdd:COG1127 101 ENVAFPlREHTD--LSEAEIRElvleKLELVGLPGAADKMPSELSGGMRKRVALarALALDP--EILLYDEPTAGLDPIT 176
|
170 180
....*....|....*....|....
gi 489717269 403 IEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG1127 177 SAVIDELIRELRDELGLTSVVVTH 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
253-426 |
5.64e-16 |
|
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: 76.84 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGK-------------EVAKLKERtyfqhVAQIFQNA 319
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEvlldgkdiydldvDVLELRRR-----VGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 320 SdqFMAITVKEELALSQKH---ASPYFTPEVLDQALADLDLADHMD--QVVYSLSGGQKKKLEILLMLLSGQEVLLIDEP 394
Cdd:cd03260 91 N--PFPGSIYDNVAYGLRLhgiKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 395 LSGLDQKSIEQVVQLLQKCQEKSgqTILLISH 426
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEY--TIVIVTH 198
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
258-428 |
7.62e-16 |
|
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: 75.99 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLK--ERTyfqhVAQIFQNaSDQFMAITVKEELAL 334
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVDVTAAPpaDRP----VSMLFQE-NNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 SQkhaSP--YFTPE---VLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQL 409
Cdd:cd03298 94 GL---SPglKLTAEdrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170
....*....|....*....
gi 489717269 410 LQKCQEKSGQTILLISHHF 428
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQP 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-188 |
8.41e-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: 76.50 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 8 DHLTFSYGD-REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQAMMFQEAGEQFTM 86
Cdd:cd03253 4 ENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY-----DVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 87 ATPREEIIF--------AMENLGKSKTEFADRLKLASEFAEI-------DSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:cd03253 79 VVPQDTVLFndtigyniRYGRPDATDEEVIEAAKAAQIHDKImrfpdgyDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKLKeQGKTIIITDH 188
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAH 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-188 |
8.80e-16 |
|
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: 76.32 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDRE----VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLypkygGQLTSGQVSLGGRSQAMMFQEA 80
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-----DRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 geqftMATPREE---IIF----------AMENLgksktefADRLKLASE---FAEIDSLLDQkiV-----------TMSG 133
Cdd:COG4181 84 -----RARLRARhvgFVFqsfqllptltALENV-------MLPLELAGRrdaRARARALLER--VglghrldhypaQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 134 GEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTH 205
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-184 |
9.05e-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: 74.50 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREV-IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLtsgqVSLGGRSQAMMFQEAgeQ 83
Cdd:cd03223 1 IELENLSLATPDGRVlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMPEGEDLLFLPQRP--Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 84 FTMATPREEIIFAmenlgkskteFADRLklasefaeidslldqkivtmSGGEKQRVALAVLVAMDVDLFLLDEPFASVDP 163
Cdd:cd03223 75 LPLGTLREQLIYP----------WDDVL--------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|.
gi 489717269 164 AARRFLigrLAKLKEQGKTII 184
Cdd:cd03223 125 ESEDRL---YQLLKELGITVI 142
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-188 |
9.11e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.21 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 17 REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVsLGGRSQAMMFQEAgeqFTM-ATPREEIIF 95
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF-----EISEGRV-WAERSIAYVPQQA---WIMnATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 96 AMEnlgksktEFADRL-------KLASEFAEIDSLLDQKI----VTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDP- 163
Cdd:PTZ00243 744 FDE-------EDAARLadavrvsQLEADLAQLGGGLETEIgekgVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAh 816
|
170 180
....*....|....*....|....*....
gi 489717269 164 ----AARRFLIGRLAklkeqGKTIIITDH 188
Cdd:PTZ00243 817 vgerVVEECFLGALA-----GKTRVLATH 840
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
249-426 |
1.12e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.73 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMT-KLLDYQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFmAIT 327
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSF-PFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKE--ELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEI--LLMLLSGQE----VLLIDEPLSGLD 399
Cdd:PRK13548 93 VEEvvAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLarVLAQLWEPDgpprWLLLDEPTSALD 172
|
170 180
....*....|....*....|....*..
gi 489717269 400 QKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK13548 173 LAHQHHVLRLARQLAHERGLAVIVVLH 199
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
258-426 |
1.13e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.31 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMT-KLLDYQGSLTWEGKEVAKLKErtyfqhvAQI--------FQNASdQFMAITV 328
Cdd:COG4674 31 LYVDPGELRVIIGPNGAGKTTLMDVITgKTRPDSGSVLFGGTDLTGLDE-------HEIarlgigrkFQKPT-VFEELTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 KE--ELALSQKH---ASPYF--TPEV---LDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:COG4674 103 FEnlELALKGDRgvfASLFArlTAEErdrIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGM 182
|
170 180
....*....|....*....|....*...
gi 489717269 399 DQKSIEQVVQLLQKCQEKsgQTILLISH 426
Cdd:COG4674 183 TDAETERTAELLKSLAGK--HSVVVVEH 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-188 |
1.18e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.74 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGG----------- 70
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGknlyapdvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ---RSQAMMFQEAgEQFTMATpREEIIFAMENLGKSKT--EFADR-LKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVL 144
Cdd:PRK14243 88 evrRRIGMVFQKP-NPFPKSI-YDNIAYGARINGYKGDmdELVERsLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 145 VAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQgKTIIITDH 188
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTH 208
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-198 |
1.56e-15 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 75.51 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMMFQEAGEQF 84
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRP-----TSGEIIFDGHPWTRKDLHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMATPREEIIFAMENLgKSKTefadrLKLASEFAEIDSLLD---------QKIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:TIGR03740 76 IESPPLYENLTARENL-KVHT-----TLLGLPDSRIDEVLNivdltntgkKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVD 198
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLAD 192
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
258-437 |
1.63e-15 |
|
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: 77.05 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKlKERTYFQHVAQIFQNAS-DQfmAITVKEELALs 335
Cdd:TIGR01188 14 FKVREGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASvDE--DLTGRENLEM- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 qkHASPYFTPEVLDQALAD-----LDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLL 410
Cdd:TIGR01188 90 --MGRLYGLPKDEAEERAEellelFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180
....*....|....*....|....*..
gi 489717269 411 QKCQEkSGQTILLISHHFYGISTWCDY 437
Cdd:TIGR01188 168 RALKE-EGVTILLTTHYMEEADKLCDR 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-189 |
1.70e-15 |
|
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: 75.34 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGG------RSQ-A 74
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrkslRSMiG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 MMFQEAG-------EQFTMATP---REEIIFAMENLGksKTEFADRLK--LASEFAEIDSLLdqkivtmSGGEKQRVALA 142
Cdd:cd03254 81 VVLQDTFlfsgtimENIRLGRPnatDEEVIEAAKEAG--AHDFIMKLPngYDTVLGENGGNL-------SQGERQLLAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 143 VLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL 198
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
244-426 |
1.83e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 78.67 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 244 FAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQnasDQ 322
Cdd:COG1132 347 FSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTsGRILIDGVDIRDLTLESLRRQIGVVPQ---DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 FM-AITVKEELALSQKHAspyfTPEVLDQAL--ADLD-----LADHMDQVV----YSLSGGQKKKLEILLMLLSGQEVLL 390
Cdd:COG1132 424 FLfSGTIRENIRYGRPDA----TDEEVEEAAkaAQAHefieaLPDGYDTVVgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 391 IDEPLSGLD-------QKSIEQVVQllqkcqeksGQTILLISH 426
Cdd:COG1132 500 LDEATSALDtetealiQEALERLMK---------GRTTIVIAH 533
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
247-426 |
2.04e-15 |
|
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: 75.41 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASdQFMA 325
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDIREQDPVELRRKIGYVIQQIG-LFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALSQK--HASPYFTPEVLDQALADLDL--ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:cd03295 90 MTVEENIALVPKllKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPI 169
|
170 180
....*....|....*....|....*
gi 489717269 402 SIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:cd03295 170 TRDQLQEEFKRLQQELGKTIVFVTH 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
233-426 |
2.18e-15 |
|
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: 75.00 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 233 ENEPAAFVMKNFAIKqgrpLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWE----GKEVAKLKERTY 308
Cdd:cd03234 7 WDVGLKAKNWNKYAR----ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQilfnGQPRKPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 309 FQHVAQifqnaSDQFMA-ITVKEEL------ALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLM 381
Cdd:cd03234 83 VAYVRQ-----DDILLPgLTVRETLtytailRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 382 LLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQeKSGQTILLISH 426
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIH 201
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
250-427 |
2.72e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.45 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 250 RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ---GSLTWEGKEVAKL--KERTY------FQHVAQIFQN 318
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKileGDILFKGESILDLepEERAHlgiflaFQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 ASDQFMaitvkeELALSQKHAS---PYFTP-EVLDQALADLDLADhMDQVVYS------LSGGQKKKLEILLMLLSGQEV 388
Cdd:CHL00131 100 SNADFL------RLAYNSKRKFqglPELDPlEFLEIINEKLKLVG-MDPSFLSrnvnegFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 389 LLIDEPLSGLD---QKSIEQVVQLLQkcqeKSGQTILLISHH 427
Cdd:CHL00131 173 AILDETDSGLDidaLKIIAEGINKLM----TSENSIILITHY 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
258-426 |
2.75e-15 |
|
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: 74.37 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKLKERT---YFQHVAQIFQNaSDQFMAITVKEELA 333
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQD-FRLLPDRNVYENVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 334 LSQK--HASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQ 411
Cdd:cd03292 101 FALEvtGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK 180
|
170
....*....|....*
gi 489717269 412 KCQeKSGQTILLISH 426
Cdd:cd03292 181 KIN-KAGTTVVVATH 194
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
10-188 |
2.81e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 10 LTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ----------LTSGQVSLGGRSQAMMFQe 79
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEilfdgenipaMSRSRLYTVRKRMSMLFQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 80 AGEQFTMATPREEIIFAME---NLGKSKTEFADRLKLasEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDE 156
Cdd:PRK11831 92 SGALFTDMNVFDNVAYPLRehtQLPAPLLHSTVMMKL--EAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 157 PFASVDPaarrFLIGRLAKLKEQ-----GKTIIITDH 188
Cdd:PRK11831 170 PFVGQDP----ITMGVLVKLISElnsalGVTCVVVSH 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
248-426 |
2.95e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKL-KER-TYFQHVAQI-FQNASD-- 321
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGPgAERgVVFQNEGLLpWRNVQDnv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 322 ----QFMAITVKEELALSQkhaspyftpevldQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSG 397
Cdd:PRK11248 92 afglQLAGVEKMQRLEIAH-------------QMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180
....*....|....*....|....*....
gi 489717269 398 LDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
248-426 |
3.16e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 75.28 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKL-KERtyfqhvAQIFQNasDQFMA 325
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPsSGEITLDGVPVTGPgADR------GVVFQK--DALLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 -ITVKEELAL---------SQKHAspyftpeVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:COG4525 90 wLNVLDNVAFglrlrgvpkAERRA-------RAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG4525 163 GALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
248-439 |
3.75e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKlkERTYFQHVAQIFQNASDQFMAI 326
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQSIKK--DLCTYQKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEElALSQKHASPyfTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:PRK13540 90 TLREN-CLYDIHFSP--GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 407 VQLLQKcQEKSGQTILLISHHFYGI--STWCDYHL 439
Cdd:PRK13540 167 ITKIQE-HRAKGGAVLLTSHQDLPLnkADYEEYHL 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
258-426 |
3.98e-15 |
|
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: 76.30 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYF----QHVAQIFQNASdQFMAITVKEEL 332
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRpDEGEIVLNGRTLFDSRKGIFLppekRRIGYVFQEAR-LFPHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 333 ALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQK 412
Cdd:TIGR02142 97 RYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLER 176
|
170
....*....|....
gi 489717269 413 CQEKSGQTILLISH 426
Cdd:TIGR02142 177 LHAEFGIPILYVSH 190
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
258-426 |
4.53e-15 |
|
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: 75.86 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ----GSLTWEGKEVAKLKERTY----FQHVAQIFQNAsdqfMA---- 325
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitsGEILFDGEDLLKLSEKELrkirGREIQMIFQDP----MTslnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 -ITVKE---ELALSQKHASPyftPEVLDQALADLDL------ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:COG0444 102 vMTVGDqiaEPLRIHGGLSK---AEARERAIELLERvglpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPT 178
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 396 SGLD---QKsieQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG0444 179 TALDvtiQA---QILNLLKDLQRELGLAILFITH 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
253-450 |
7.51e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 7.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLdyQGSLTWE------GKEVAKLKE-----RTYFQHVAQIFQnasd 321
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI--TGDKSAGshiellGRTVQREGRlardiRKSRANTGYIFQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 322 QFMAI---TVKEELALSQKHASP-------YFTPEVLD---QALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEV 388
Cdd:PRK09984 94 QFNLVnrlSVLENVLIGALGSTPfwrtcfsWFTREQKQralQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489717269 389 LLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHfygistwCDYHLRLAGRELAFVQ 450
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQ-------VDYALRYCERIVALRQ 228
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-441 |
9.31e-15 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 77.18 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 124 LDQKIVTMSGGEKQRVALAVLVAMDVD--LFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHlfdDYQ------- 194
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH---DEQmisladr 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 195 --------GKVDGVYRFKGEQVDLLTKDEQ--ALLLATEpigLHFPLPENEPA--AFVMKNFAIKQGrplLEQKELSIPK 262
Cdd:PRK00635 547 iidigpgaGIFGGEVLFNGSPREFLAKSDSltAKYLRQE---LTIPIPEKRTNslGTLTLSKATKHN---LKDLTISLPL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFK-----AMTKLL--DYQGSLTWEGKEVAKL----------KER----TY---FQHVAQIFQN 318
Cdd:PRK00635 621 GRLTVVTGVSGSGKSSLINdtlvpAVEEFIeqGFCSNLSIQWGAISRLvhitrdlpgrSQRsiplTYikaFDDLRELFAE 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 ---------------------------------ASDQFMAI----------------------TVKEELALSQKHASPYF 343
Cdd:PRK00635 701 qprskrlgltkshfsfntplgacaecqglgsitTTDNRTSIpcpsclgkrflpqvlevrykgkNIADILEMTAYEAEKFF 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 344 --TPEVLD--QALADLDLaDH--MDQVVYSLSGGQKKKLEILLMLLSG---QEVLLIDEPLSGLDQKSIEQVVQLLQKCQ 414
Cdd:PRK00635 781 ldEPSIHEkiHALCSLGL-DYlpLGRPLSSLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLT 859
|
410 420
....*....|....*....|....*..
gi 489717269 415 EKsGQTILLISHHFYGISTwCDYHLRL 441
Cdd:PRK00635 860 HQ-GHTVVIIEHNMHVVKV-ADYVLEL 884
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
258-427 |
9.53e-15 |
|
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: 73.00 E-value: 9.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGkVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEVAKLKErTYFQHVAQIFQnasdQFM---AITVKEELA 333
Cdd:cd03264 21 LTLGPG-MYGLLGPNGAGKTTLMRILATLTpPSSGTIRIDGQDVLKQPQ-KLRRRIGYLPQ----EFGvypNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 334 -------LSQKHAspyftPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDqksIEQV 406
Cdd:cd03264 95 yiawlkgIPSKEV-----KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD---PEER 166
|
170 180
....*....|....*....|.
gi 489717269 407 VQLLQKCQEKSGQTILLISHH 427
Cdd:cd03264 167 IRFRNLLSELGEDRIVILSTH 187
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
240-426 |
1.04e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFAIKQgrpLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEV--AKLKERTYFQHVAQIF 316
Cdd:PRK09493 7 VSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsGDLIVDGLKVndPKVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 317 QnasdQFM---AITVKEELALSQKHASPYFTPEVLDQA---LADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLL 390
Cdd:PRK09493 84 Q----QFYlfpHLTALENVMFGPLRVRGASKEEAEKQArelLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 391 IDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTH 194
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-189 |
1.43e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRSQAMMFQEAGEQ 83
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 84 FTMATPREEII-----FAMENLGKSKTEFA-----DRLKLAsEFAE-----IDSLLDQKIVTMSGGEKQRVALA-VLVAM 147
Cdd:PRK10790 416 GVAMVQQDPVVladtfLANVTLGRDISEEQvwqalETVQLA-ELARslpdgLYTPLGEQGNNLSVGQKQLLALArVLVQT 494
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 148 DvDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:PRK10790 495 P-QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRL 535
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-193 |
1.52e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.59 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 36 IGPTGCGKSTLLKIMAGL---------------Y-PKYGGQLTSGQVslggrsQAMMFQEAGEQFTMATPREEIIfamen 99
Cdd:COG1245 372 VGPNGIGKTTFAKILAGVlkpdegevdedlkisYkPQYISPDYDGTV------EEFLRSANTDDFGSSYYKTEII----- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 100 lgksktefaDRLKLasefaeiDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD-----PAARrfLIGRLA 174
Cdd:COG1245 441 ---------KPLGL-------EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlAVAK--AIRRFA 502
|
170 180
....*....|....*....|.
gi 489717269 175 klKEQGKTIIITDH--LFDDY 193
Cdd:COG1245 503 --ENRGKTAMVVDHdiYLIDY 521
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-188 |
1.72e-14 |
|
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: 76.14 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY--GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGrSQAMMFQEAGE 82
Cdd:TIGR00957 637 ITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK-----VEGHVHMKG-SVAYVPQQAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QftMATPREEIIFamenlGKSKTE--FADRLKLASEFAEIDSL-------LDQKIVTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:TIGR00957 711 Q--NDSLRENILF-----GKALNEkyYQQVLEACALLPDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 154 LDEPFASVDPAARRFL----IGRLAKLKeqGKTIIITDH 188
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHIfehvIGPEGVLK--NKTRILVTH 820
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-192 |
2.05e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG----------------RSQAMMFQEAGEQFT 85
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALL-----KPSSGTITIAGyhitpetgnknlkklrKKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 86 MATPREEIIFAMENLGKSKTEFADR-LKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPA 164
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGFSEDEAKEKaLKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180
....*....|....*....|....*...
gi 489717269 165 ARRFLIGRLAKLKEQGKTIIITDHLFDD 192
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDD 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
258-429 |
2.11e-14 |
|
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: 72.32 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLkeRTY------FQHVAQ---IFQNasdqfmaIT 327
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGEDITGL--PPHriarlgIGYVPEgrrIFPS-------LT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQKHASPYF-TPEVLDQALaDL--DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIE 404
Cdd:COG0410 95 VEENLLLGAYARRDRAeVRADLERVY-ELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 405 QVVQLLQKCQEkSGQTILL----------ISHHFY 429
Cdd:COG0410 174 EIFEIIRRLNR-EGVTILLveqnarfaleIADRAY 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-186 |
2.31e-14 |
|
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: 73.55 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLT--FSYGDREV--IRDLSLTLPAG-TFSLlIGPTGCGKSTLLKIMAGLYPKYGgqLTSGQVSLGGR-----SQ- 73
Cdd:COG0444 2 LEVRNLKvyFPTRRGVVkaVDGVSFDVRRGeTLGL-VGESGSGKSTLARAILGLLPPPG--ITSGEILFDGEdllklSEk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 ----------AMMFQEA----------GEQFTmatpreEIIFAMENLGKsktefADRLKLASEFAEI------DSLLDQK 127
Cdd:COG0444 79 elrkirgreiQMIFQDPmtslnpvmtvGDQIA------EPLRIHGGLSK-----AEARERAIELLERvglpdpERRLDRY 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 128 IVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQ-GKTII-IT 186
Cdd:COG0444 148 PHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILfIT 208
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-164 |
2.60e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYP---KYGGQLTSGQVSLGG----------- 70
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTGDVTLNGeplaaidaprl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 -RSQAMMFQEAGEQFTMATprEEIIF--------AMENLGKSKTEFADRlklASEFAEIDSLLDQKIVTMSGGEKQRVAL 141
Cdd:PRK13547 82 aRLRAVLPQAAQPAFAFSA--REIVLlgrypharRAGALTHRDGEIAWQ---ALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 142 AVLVAM---------DVDLFLLDEPFASVDPA 164
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLA 188
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
245-427 |
2.76e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 245 AIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKER---TYFQHvaqifQNAs 320
Cdd:PRK13539 10 CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPpAAGTIKLDGGDIDDPDVAeacHYLGH-----RNA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 321 dqfM--AITVKEELALSQKHASPyfTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:PRK13539 84 ---MkpALTVAENLEFWAAFLGG--EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*....
gi 489717269 399 DQKSIEQVVQLLQKCQEKSGqtILLISHH 427
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGG--IVIAATH 185
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
257-426 |
3.78e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.94 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 257 ELSIPKGKVTLITGPNGSGKSSLFKAMTKLldYQ---GSLTWEGKEVAKLKE---------RTyFQHVaQIFQNasdqfm 324
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGF--YKptgGTILLRGQHIEGLPGhqiarmgvvRT-FQHV-RLFRE------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 aITVKEELALSQKH--ASPYF-----TP-------EVLDQALADLD---LADHMDQVVYSLSGGQKKKLEILLMLLSGQE 387
Cdd:PRK11300 95 -MTVIENLLVAQHQqlKTGLFsgllkTPafrraesEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 388 VLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-188 |
3.78e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQAmMFQE 79
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW-----DPQQGEILLNGQPIA-DYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 80 AGEQFTM-----------ATPREEIIFAMENlgKSKTEFADRL------KLASEFAEIDSLLDQKIVTMSGGEKQRVALA 142
Cdd:PRK11160 410 AALRQAIsvvsqrvhlfsATLRDNLLLAAPN--ASDEALIEVLqqvgleKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 143 VLVAMDVDLFLLDEPFASVDPAARRFLigrLAKLKE--QGKTIIITDH 188
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQI---LELLAEhaQNKTVLMITH 532
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
258-436 |
3.84e-14 |
|
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: 71.16 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEVAKLKERT--YFQHVAQIFQNASDQFMAITVKEELAL 334
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPDSGEVLFDGKPLDIAARNRigYLPEERGLYPKMKVIDQLVYLAQLKGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 SQKHASPYftpevLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQ 414
Cdd:cd03269 101 KKEEARRR-----IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELA 175
|
170 180
....*....|....*....|..
gi 489717269 415 EKsGQTILLISHHFYGISTWCD 436
Cdd:cd03269 176 RA-GKTVILSTHQMELVEELCD 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
248-431 |
4.28e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNAsDQFMAi 326
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDpQQGEILLNGQPIADYSEAALRQAISVVSQRV-HLFSA- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQKHAspyfTPEVLDQALADLDLADHMDQVV----------YSLSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:PRK11160 429 TLRDNLLLAAPNA----SDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 397 GLDQKSIEQVVQLLQK-CQEKsgqTILLISHHFYGI 431
Cdd:PRK11160 505 GLDAETERQILELLAEhAQNK---TVLMITHRLTGL 537
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-188 |
4.29e-14 |
|
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: 71.42 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 6 TIDHLTFSYGDR---EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG-----------R 71
Cdd:cd03249 2 EFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFY-----DPTSGEILLDGvdirdlnlrwlR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 72 SQ-AMMFQEAgeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAE-----IDSLLDQKIVTMSGGEKQRVALAVLV 145
Cdd:cd03249 77 SQiGLVSQEP--VLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMslpdgYDTLVGERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 146 AMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEqGKTIIITDH 188
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-188 |
4.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRS---QAMMFQEAG 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNiyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 EQFTMATPR---------EEIIFAMENLG-KSKTEFAD----RLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAM 147
Cdd:PRK14258 88 RQVSMVHPKpnlfpmsvyDNVAYGVKIVGwRPKLEIDDivesALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGK-TIIITDH 188
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSH 209
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-163 |
4.60e-14 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 74.40 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 19 VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSgqvslgGRSQAMMFQEAGEQFTMATPREEIIFAMe 98
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK------PAKGKLFYVPQRPYMTLGTLRDQIIYPD- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 99 nlgkSKTEFADRLKLASEFAEI----------------DSLLDQKIVtMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD 162
Cdd:TIGR00954 540 ----SSEDMKRRGLSDKDLEQIldnvqlthilereggwSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
.
gi 489717269 163 P 163
Cdd:TIGR00954 615 V 615
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
241-426 |
5.01e-14 |
|
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: 70.27 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 241 MKNFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY---QGSLTWEGKevaKLKERTYFQHVAQIFQ 317
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLINGR---PLDKRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 NasDQFMA-ITVKEELALSqkhaspyftpevldqalADLDladhmdqvvySLSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:cd03213 90 D--DILHPtLTVRETLMFA-----------------AKLR----------GLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 397 GLDQKSIEQVVQLLQK-CQEksGQTILLISH 426
Cdd:cd03213 141 GLDSSSALQVMSLLRRlADT--GRTIICSIH 169
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
248-427 |
5.16e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.49 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLldyqgsltW---EGKEVAKLKERTYFqhvaqifqnasdqfm 324
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL--------WpwgSGRIGMPEGEDLLF--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 aitvkeelaLSQKhasPYFTPEVLdqaladldladhMDQVVYS----LSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:cd03223 69 ---------LPQR---PYLPLGTL------------REQLIYPwddvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*..
gi 489717269 401 KSIEQVVQLLQkcqeKSGQTILLISHH 427
Cdd:cd03223 125 ESEDRLYQLLK----ELGITVISVGHR 147
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
253-427 |
5.17e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.35 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGK-----EVAKLKE-RTYFQHVAQIFQNASDQFMAI 326
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipaNLKKIKEvKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELAL------SQKHASPYFTPEVLDqaLADLDlADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:PRK13645 107 TIEKDIAFgpvnlgENKQEAYKKVPELLK--LVQLP-EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180
....*....|....*....|....*..
gi 489717269 401 KSIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHN 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
258-436 |
7.90e-14 |
|
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: 68.99 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAklkertyfqhvaqifqnasdqfmaitvkeelalsq 336
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVDGKEVS----------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 337 kHASPYftpevldqaladlDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEK 416
Cdd:cd03216 66 -FASPR-------------DARRAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ 131
|
170 180
....*....|....*....|
gi 489717269 417 sGQTILLISHHFYGISTWCD 436
Cdd:cd03216 132 -GVAVIFISHRLDEVFEIAD 150
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
263-422 |
8.24e-14 |
|
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: 69.98 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFKAMTKLLDY----QGSLTWEGKEVAKLKErtYFQHVAqIFQNASDQFMA-ITVKE--ELALS 335
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTEGnvsvEGDIHYNGIPYKEFAE--KYPGEI-IYVSEEDVHFPtLTVREtlDFALR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 QKHaspyftpevldqaladldladhmDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQE 415
Cdd:cd03233 110 CKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAD 166
|
....*..
gi 489717269 416 KSGQTIL 422
Cdd:cd03233 167 VLKTTTF 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-192 |
8.42e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.89 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 17 REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRS---------QAM-MFQEAGEQFTM 86
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP-----TSGTVLVGGKDietnldavrQSLgMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 87 ATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAAR 166
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180
....*....|....*....|....*.
gi 489717269 167 RFLIGRLAKLKeQGKTIIITDHLFDD 192
Cdd:TIGR01257 1098 RSIWDLLLKYR-SGRTIIMSTHHMDE 1122
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-188 |
9.74e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYGGQLTSGQV---SLGGRSQAMMF--Q 78
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEKGEILFERQSikkDLCTYQKQLCFvgH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 79 EAGEQFTMaTPREEIIFAMeNLGKSKTEFADRLKLASefaeIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPF 158
Cdd:PRK13540 82 RSGINPYL-TLRENCLYDI-HFSPGAVGITELCRLFS----LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|
gi 489717269 159 ASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
250-427 |
1.09e-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: 70.19 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 250 RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLldYQ---GSLTWEGKEVAKLKERTYFQHVAQIFQNAsdQFMAI 326
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF--YQpqgGQVLLDGKPISQYEHKYLHSKVSLVGQEP--VLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQKHASPYFTPEVLDQALADlDLADHMDQVVYS--------LSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:cd03248 103 SLQDNIAYGLQSCSFECVKEAAQKAHAH-SFISELASGYDTevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180
....*....|....*....|....*....
gi 489717269 399 DQKSIEQVVQLLQKCQEKsgQTILLISHH 427
Cdd:cd03248 182 DAESEQQVQQALYDWPER--RTVLVIAHR 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-191 |
1.11e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.81 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyGGQLTSGQVSLGGRSqammFQEA 80
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT--GDKSAGSHIELLGRT----VQRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 G-----------------EQFTMATPreeiIFAMEN-----LGKS---KTEFA-------DRLKLASEFAEIDSLLDQKI 128
Cdd:PRK09984 75 GrlardirksrantgyifQQFNLVNR----LSVLENvligaLGSTpfwRTCFSwftreqkQRALQALTRVGMVHFAHQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489717269 129 VTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQ-GKTIIITDHLFD 191
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVD 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-189 |
1.19e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 9 HLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRS-------------QAM 75
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSifnyrdvlefrrrVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEAgEQFTMATPREEIIFAMENLGKSKTEF----ADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:PRK14271 106 LFQRP-NPFPMSIMDNVLAGVRAHKLVPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
241-443 |
1.19e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.18 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 241 MKNFAIKQG-RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQN 318
Cdd:PRK09536 6 VSDLSVEFGdTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEALSARAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 ASDQFmAITVKEELALSQKHASPYFTP------EVLDQALADLDLADHMDQVVYSLSGGQKKKleILLMLLSGQE--VLL 390
Cdd:PRK09536 86 TSLSF-EFDVRQVVEMGRTPHRSRFDTwtetdrAAVERAMERTGVAQFADRPVTSLSGGERQR--VLLARALAQAtpVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 391 IDEPLSGLDqksIEQVVQLLQKCQE--KSGQTILLISHHFYGISTWCDYHLRLAG 443
Cdd:PRK09536 163 LDEPTASLD---INHQVRTLELVRRlvDDGKTAVAAIHDLDLAARYCDELVLLAD 214
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
262-428 |
1.20e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 262 KGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMaITVKEELALSQ-KHAS 340
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFA-MPVFQYLALHQpAGAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 341 PYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLL--------SGQeVLLIDEPLSGLDqksIEQVV---QL 409
Cdd:COG4138 100 SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinpEGQ-LLLLDEPMNSLD---VAQQAaldRL 175
|
170 180
....*....|....*....|
gi 489717269 410 LQK-CQekSGQTILLISHHF 428
Cdd:COG4138 176 LRElCQ--QGITVVMSSHDL 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
258-426 |
1.23e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAITVKEELALSQ 336
Cdd:PRK13642 28 FSITKGEWVSIIGQNGSGKSTTARLIDGLFEeFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDVAFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 337 KHASPYFTPEV--LDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQ 414
Cdd:PRK13642 108 ENQGIPREEMIkrVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIK 187
|
170
....*....|..
gi 489717269 415 EKSGQTILLISH 426
Cdd:PRK13642 188 EKYQLTVLSITH 199
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
258-427 |
1.28e-13 |
|
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: 69.88 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLL--DyQGSLTWEGKEVAKL--KER-----TYFQHVAQIFQNasdqfmaITV 328
Cdd:cd03218 21 LSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkpD-SGKILLDGQDITKLpmHKRarlgiGYLPQEASIFRK-------LTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 KEEL--ALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:cd03218 93 EENIlaVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI 172
|
170 180
....*....|....*....|.
gi 489717269 407 VQLLQKCQEKsGQTILLISHH 427
Cdd:cd03218 173 QKIIKILKDR-GIGVLITDHN 192
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
258-426 |
1.32e-13 |
|
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: 69.59 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKL--KERtyfqHVAQIFQNASdQFMAITVKEELA- 333
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTDLppKDR----DIAMVFQNYA-LYPHMTVYDNIAf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 334 -LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQK 412
Cdd:cd03301 96 gLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKR 175
|
170
....*....|....
gi 489717269 413 CQEKSGQTILLISH 426
Cdd:cd03301 176 LQQRLGTTTIYVTH 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
257-437 |
1.50e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 257 ELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSL---------TWEGKEVAKLKERtyfqhVAQIFQNASDQFMAI 326
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVtvgdivvssTSKQKEIKPVRKK-----VGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQKH--ASPYFTPEVLDQALADLDLADHM-DQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSI 403
Cdd:PRK13643 101 TVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 404 EQVVQLLQKCQEkSGQTILLISHHFYGISTWCDY 437
Cdd:PRK13643 181 IEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADY 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-425 |
1.56e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLT-SGQ-VSLGGRSQAmmfQ 78
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKeVTFNGPKSS---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 79 EAG-----------EQFTMAtpreEIIFamenLGKSKTEFADRLKLASEFAEIDSLL---------DQKIVTMSGGEKQR 138
Cdd:PRK10762 78 EAGigiihqelnliPQLTIA----ENIF----LGREFVNRFGRIDWKKMYAEADKLLarlnlrfssDKLVGELSIGEQQM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 139 VALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH----LF---DDYQGKVDGvyRFKGEQ-VDL 210
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHrlkeIFeicDDVTVFRDG--QFIAEReVAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 211 LTKDEQALLLATEPIGLHFPLPENEPaafvmknfaikqGRPLLEQKELSIP----------KGKVTLITGPNGSGKSSLF 280
Cdd:PRK10762 228 LTEDSLIEMMVGRKLEDQYPRLDKAP------------GEVRLKVDNLSGPgvndvsftlrKGEILGVSGLMGAGRTELM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 281 KAMTKLL-DYQGSLTWEGKEVaklKERTYFQHVAQ-IFQNASDQ-----FMAITVKEELALSqkhASPYFTPEV--LDQA 351
Cdd:PRK10762 296 KVLYGALpRTSGYVTLDGHEV---VTRSPQDGLANgIVYISEDRkrdglVLGMSVKENMSLT---ALRYFSRAGgsLKHA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 352 LADLDLAD----------HMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTI 421
Cdd:PRK10762 370 DEQQAVSDfirlfniktpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSI 448
|
....
gi 489717269 422 LLIS 425
Cdd:PRK10762 449 ILVS 452
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
251-427 |
1.89e-13 |
|
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: 69.04 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKeVAklkertYfqhVAQI--FQNAsdqfmaiT 327
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEkLSGSVSVPGS-IA------Y---VSQEpwIQNG-------T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQKhaspyFTPEVLDQAL------ADLDLADHMDQVV-----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:cd03250 82 IRENILFGKP-----FDEERYEKVIkacalePDLEILPDGDLTEigekgINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 397 GLD----QKSIEQVVQ-LLQKcqeksGQTILLISHH 427
Cdd:cd03250 157 AVDahvgRHIFENCILgLLLN-----NKTRILVTHQ 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-188 |
1.97e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 23 LSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqlTSGQVSLGGRS------------QAMMFQEAGEQFTMAtpr 90
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP------GSGSIQFAGQPleawsaaelarhRAYLSQQQTPPFAMP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 91 eeiIFAMENL-GKSKTEFADRLKLASEFAE---IDSLLDQKIVTMSGGEKQRVALAVlVAMDVD--------LFLLDEPF 158
Cdd:PRK03695 86 ---VFQYLTLhQPDKTRTEAVASALNEVAEalgLDDKLGRSVNQLSGGEWQRVRLAA-VVLQVWpdinpagqLLLLDEPM 161
|
170 180 190
....*....|....*....|....*....|
gi 489717269 159 ASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
258-426 |
1.98e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 70.92 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKvTL-ITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE---RTYFQHVAQIFQN--AS-DQFMaiTVK 329
Cdd:COG4608 39 FDIRRGE-TLgLVGESGCGKSTLGRLLLRLEEpTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDpyASlNPRM--TVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELA---LSQKHASPyftPEVLDQALADLDL----ADHMDQVVYSLSGGQKKKLEIL--LMLlsGQEVLLIDEPLSGLDq 400
Cdd:COG4608 116 DIIAeplRIHGLASK---AERRERVAELLELvglrPEHADRYPHEFSGGQRQRIGIAraLAL--NPKLIVCDEPVSALD- 189
|
170 180
....*....|....*....|....*..
gi 489717269 401 KSIE-QVVQLLQKCQEKSGQTILLISH 426
Cdd:COG4608 190 VSIQaQVLNLLEDLQDELGLTYLFISH 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-188 |
2.44e-13 |
|
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: 69.44 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYG--DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQAMMFQEAG- 81
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 --EQFTM--ATPREEIIFAMENLGKSKTEFADRLKLASEFAE-----IDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:cd03252 81 vlQENVLfnRSIRDNIALADPGMSMERVIEAAKLAGAHDFISelpegYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 153 LLDEPFASVDPAARRFLIGRLAKLKEqGKTIIITDH 188
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAH 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
223-427 |
2.54e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.06 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 223 EPIGLHFPLPENEPAAFVMKNFA--IKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLldYQ---GSLTWEG 297
Cdd:TIGR00958 465 PLTGTLAPLNLEGLIEFQDVSFSypNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL--YQptgGQVLLDG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 298 KEVAKLKERTYFQHVAQIFQNAsdQFMAITVKEELALSQKHASPYFTPEVLDQALADlDLADHMDQVVYS--------LS 369
Cdd:TIGR00958 543 VPLVQYDHHYLHRQVALVGQEP--VLFSGSVRENIAYGLTDTPDEEIMAAAKAANAH-DFIMEFPNGYDTevgekgsqLS 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 370 GGQKKKLEILLMLLSGQEVLLIDEPLSGLDQksieQVVQLLQKCQEKSGQTILLISHH 427
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHR 673
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
247-426 |
2.56e-13 |
|
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: 69.18 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKERTYFQHVAQIFQNA---SDq 322
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASLRRQIGLVSQDVflfND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 fmaiTVKEELALSQKHASPYFTPEVLDQALAD---LDLADHMDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:cd03251 91 ----TVAENIAYGRPGATREEVEEAARAANAHefiMELPEGYDTVIgergVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQKCQEksGQTILLISH 426
Cdd:cd03251 167 SALDTESERLVQAALERLMK--NRTTFVIAH 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
228-427 |
3.38e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 228 HFPLPENEPAAFVMKNFAIKQG---RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTK-LLDYQGSLTWEGKEVAKL 303
Cdd:COG2401 18 SSVLDLSERVAIVLEAFGVELRvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVDVPDNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 304 KERTYFQHVAQIFqnasdqfmaiTVKEELALsqkhaspyftpevldqaLADLDLADhmdqvVYS-------LSGGQKKKL 376
Cdd:COG2401 98 REASLIDAIGRKG----------DFKDAVEL-----------------LNAVGLSD-----AVLwlrrfkeLSTGQKFRF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489717269 377 EILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHH 427
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH 196
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-189 |
3.55e-13 |
|
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: 71.29 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 9 HLTFSYG--DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ-LTSG-------------QVSLGGRs 72
Cdd:TIGR02203 335 NVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQiLLDGhdladytlaslrrQVALVSQ- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 QAMMFQE---------AGEQFTMATPREEIifAMENLgkskTEFADRLKLAsefaeIDSLLDQKIVTMSGGEKQRVALAV 143
Cdd:TIGR02203 414 DVVLFNDtianniaygRTEQADRAEIERAL--AAAYA----QDFVDKLPLG-----LDTPIGENGVLLSGGQRQRLAIAR 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRL 528
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
258-426 |
5.24e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.83 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTkLLDY--QGSLTWEGKEVAKLKE---RTYFQHVAQIFQN----ASDqfmaiTV 328
Cdd:PRK11153 26 LHIPAGEIFGVIGASGAGKSTLIRCIN-LLERptSGRVLVDGQDLTALSEkelRKARRQIGMIFQHfnllSSR-----TV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 KEELALSQKHASpyfTPEVLDQA----LADL-DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSI 403
Cdd:PRK11153 100 FDNVALPLELAG---TPKAEIKArvteLLELvGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
|
170 180
....*....|....*....|...
gi 489717269 404 EQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK11153 177 RSILELLKDINRELGLTIVLITH 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-432 |
6.99e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 70.66 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMA-----GLyPKYGGQLTSGQVSLGGRSQAM--- 75
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI-PKNCQILHVEQEVVGDDTTALqcv 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 ---------MFQEagEQFTMATPREEIIFAMENLGKSKTEFADRLKLASE-FAEIDSLLDQ------------------- 126
Cdd:PLN03073 256 lntdiertqLLEE--EAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQrLEEIYKRLELidaytaearaasilaglsf 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 127 -------KIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKeqgKTIIITDHL---------- 189
Cdd:PLN03073 334 tpemqvkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAreflntvvtd 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 190 --------FDDYQGKVDGVYRFKGEQVDLLTK----------------DE-----------QALLLATEPIG-------- 226
Cdd:PLN03073 411 ilhlhgqkLVTYKGDYDTFERTREEQLKNQQKafesnersrshmqafiDKfrynakraslvQSRIKALDRLGhvdavvnd 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 227 ----LHFPLPENEPAA----FVMKNFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGk 298
Cdd:PLN03073 491 pdykFEFPTPDDRPGPpiisFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS- 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 299 evAKLKERTYFQHVAQIFQNASDQFmaitvkeelaLSQKHASPYFTPEVLDQALADLDLADHMD-QVVYSLSGGQKKKLE 377
Cdd:PLN03073 570 --AKVRMAVFSQHHVDGLDLSSNPL----------LYMMRCFPGVPEQKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVA 637
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 378 ILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQeksgQTILLISHHFYGIS 432
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ----GGVLMVSHDEHLIS 688
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
268-426 |
7.34e-13 |
|
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: 69.06 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 268 ITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKerTYFQHVAQIFQNASdQFMAITVKEELALS---QKHASPYF 343
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPdSGSIMLDGEDVTNVP--PHLRHINMVFQSYA-LFPHMTVEENVAFGlkmRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 344 TPEVLDqALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILL 423
Cdd:TIGR01187 78 KPRVLE-ALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
...
gi 489717269 424 ISH 426
Cdd:TIGR01187 157 VTH 159
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
258-426 |
7.91e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.34 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTkLLDY--QGSLTWEGKEVAKLKE---RTYFQHVAQIFQnasdQF---MAITVK 329
Cdd:COG1135 26 LTIEKGEIFGIIGYSGAGKSTLIRCIN-LLERptSGSVLVDGVDLTALSErelRAARRKIGMIFQ----HFnllSSRTVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELALSQKHASpyfTPEVLDQA----LADL-DLADHMDQvvY--SLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:COG1135 101 ENVALPLEIAG---VPKAEIRKrvaeLLELvGLSDKADA--YpsQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180
....*....|....*....|....
gi 489717269 403 IEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG1135 176 TRSILDLLKDINRELGLTIVLITH 199
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
243-427 |
8.36e-13 |
|
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: 67.64 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 243 NFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQnasD 321
Cdd:cd03254 9 NFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSLRSMIGVVLQ---D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 322 QFM-AITVKEELALSqkhaSPYFTPEVLDQALADL-------DLADHMDQVV----YSLSGGQKKKLEILLMLLSGQEVL 389
Cdd:cd03254 86 TFLfSGTIMENIRLG----RPNATDEEVIEAAKEAgahdfimKLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 390 LIDEPLSGLDQKSIEQVVQLLQKCQEksGQTILLISHH 427
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHR 197
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
248-426 |
8.89e-13 |
|
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: 67.23 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKG-KVTLItGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQNASdqFMA 325
Cdd:cd03245 15 QEIPALDNVSLTIRAGeKVAII-GRVGSGKSTLLKLLAGLYKPTsGSVLLDGTDIRQLDPADLRRNIGYVPQDVT--LFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALSQKHASpyfTPEVLDQA-LADLD--LADH---MDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:cd03245 92 GTLRDNITLGAPLAD---DERILRAAeLAGVTdfVNKHpngLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQkcQEKSGQTILLISH 426
Cdd:cd03245 169 SAMDMNSEERLKERLR--QLLGDKTLIIITH 197
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-188 |
9.49e-13 |
|
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: 66.19 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTLLKimAGLYpkyggqltsgqvslggrsqammfqeageqftmATPREEIIFAMEN 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--------------------------------ASGKARLISFLPK 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 100 LGKSKTEFADRLKLASEFAeIDSL-LDQKIVTMSGGEKQRVALAVLVAMDVD--LFLLDEPFASVDPAARRFLIGRLAKL 176
Cdd:cd03238 57 FSRNKLIFIDQLQFLIDVG-LGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL 135
|
170
....*....|..
gi 489717269 177 KEQGKTIIITDH 188
Cdd:cd03238 136 IDLGNTVILIEH 147
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
248-427 |
1.04e-12 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 70.28 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKG-KVTLItGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNAsdQFMA 325
Cdd:TIGR03375 476 QETPALDNVSLTIRPGeKVAII-GRIGSGKSTLLKLLLGLYQpTEGSVLLDGVDIRQIDPADLRRNIGYVPQDP--RLFY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALsqkhASPYFTPEVLDQALAD---LDLADH----MDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEP 394
Cdd:TIGR03375 553 GTLRDNIAL----GAPYADDEEILRAAELagvTEFVRRhpdgLDMQIgergRSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 395 LSGLDQKSIEQVVQLLQkcQEKSGQTILLISHH 427
Cdd:TIGR03375 629 TSAMDNRSEERFKDRLK--RWLAGKTLVLVTHR 659
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-191 |
1.07e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 10 LTFSYGDREV-IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQAMMFQEAGEQFTMAT 88
Cdd:PRK10522 328 VTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY-----QPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 89 PREEIIFAmENLGKSKTEFAD--------RLKLASEFaeidSLLDQKIVT--MSGGEKQRVALAVLVAMDVDLFLLDEPF 158
Cdd:PRK10522 403 FTDFHLFD-QLLGPEGKPANPalvekwleRLKMAHKL----ELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 159 ASVDPAARRFLIGR-LAKLKEQGKTII-IT--DHLFD 191
Cdd:PRK10522 478 ADQDPHFRREFYQVlLPLLQEMGKTIFaIShdDHYFI 514
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-250 |
1.10e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.08 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 35 LIGPTGCGKSTLLKIMAGLYPKygGQLTSGQVSLGGRSQAMMFQEAGEQFTMA--------TPREEIIF-AMENLGKSKT 105
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPIDAKEMRAISAYVQQddlfiptlTVREHLMFqAHLRMPRRVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 106 EFADRLKLaSEFAEIDSLLD-QKIVT--------MSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL 176
Cdd:TIGR00955 134 KKEKRERV-DEVLQALGLRKcANTRIgvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 177 KEQGKTIIITDH--------LFDDY----QGKVdgVYRFKGEQ-VDLLTKdeqalllatepigLHFPLPENE-PAAFVMK 242
Cdd:TIGR00955 213 AQKGKTIICTIHqpsselfeLFDKIilmaEGRV--AYLGSPDQaVPFFSD-------------LGHPCPENYnPADFYVQ 277
|
....*...
gi 489717269 243 NFAIKQGR 250
Cdd:TIGR00955 278 VLAVIPGS 285
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-182 |
1.16e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.79 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY---------GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG----- 70
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLE-----SPSQGNVSWRGeplak 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 --RSQA--------MMFQEAgeqFTMATPREEI--IFA--MENL-GKSKTEFADRLKLASEFAEID-SLLDQKIVTMSGG 134
Cdd:PRK10419 79 lnRAQRkafrrdiqMVFQDS---ISAVNPRKTVreIIRepLRHLlSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 135 EKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKT 182
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGT 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
258-426 |
1.34e-12 |
|
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: 68.59 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTwegkevakLKERTYFQHVAQI------------FQNASdQFM 324
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERpDSGRIR--------LGGEVLQDSARGIflpphrrrigyvFQEAR-LFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 AITVKEELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIE 404
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180
....*....|....*....|..
gi 489717269 405 QVVQLLQKCQEKSGQTILLISH 426
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSH 192
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
258-426 |
1.37e-12 |
|
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: 66.88 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKerTYFQHVAQIFQNASdQFMAITVKEELA--L 334
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETpTSGEILLDGKDITNLP--PHKRPVNTVFQNYA-LFPHLTVFENIAfgL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 SQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQ 414
Cdd:cd03300 98 RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQ 177
|
170
....*....|..
gi 489717269 415 EKSGQTILLISH 426
Cdd:cd03300 178 KELGITFVFVTH 189
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
263-426 |
1.37e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFKAMT----KLLDYQGSLTWEGKEVAKLKERTYFQHVAQifqnaSDQFM-AITVKEELALS-- 335
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAfrspKGVKGSGSVLLNGMPIDAKEMRAISAYVQQ-----DDLFIpTLTVREHLMFQah 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 ---QKHASPYFTPEVLDQALADLDLADHMDQV------VYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:TIGR00955 126 lrmPRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180
....*....|....*....|.
gi 489717269 407 VQLLQK-CQekSGQTILLISH 426
Cdd:TIGR00955 206 VQVLKGlAQ--KGKTIICTIH 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
236-426 |
1.40e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.42 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 236 PAAFVMKNFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL-----DYQGSLTWEGKEVA--KLKERty 308
Cdd:PRK10418 2 PQQIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVApcALRGR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 309 fqHVAQIFQNASDQF-----MAITVKEELALSQKHAspyfTPEVLDQALADLDLADH---MDQVVYSLSGGQKKKLEILL 380
Cdd:PRK10418 80 --KIATIMQNPRSAFnplhtMHTHARETCLALGKPA----DDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489717269 381 MLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTH 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
237-427 |
1.80e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 237 AAFVMKNFA-IKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVA--KLKERT----- 307
Cdd:PRK10895 2 ATLTAKNLAkAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISllPLHARArrgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 308 YFQHVAQIFQNAS--DQFMAI-TVKEELALSQKHaspyftpEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLS 384
Cdd:PRK10895 82 YLPQEASIFRRLSvyDNLMAVlQIRDDLSAEQRE-------DRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 385 GQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEkSGQTILLISHH 427
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHN 196
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
249-428 |
1.99e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.43 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD------YQGSLTWEGKEVAKLKERTYFQH-VAQIFQNASD 321
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrYSGDVLLGGRSIFNYRDVLEFRRrVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 322 QFMAIT------VKEELALSQKHASPYFTPEVLDQALADLdLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:PRK14271 113 FPMSIMdnvlagVRAHKLVPRKEFRGVAQARLTEVGLWDA-VKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 396 SGLDQKSIEQVVQLLQKCQEKsgQTILLISHHF 428
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADR--LTVIIVTHNL 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
240-428 |
2.08e-12 |
|
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: 66.59 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLK-ERtyfQHVAQIFQ 317
Cdd:cd03299 2 KVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpDSGKILLNGKDITNLPpEK---RDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 NASdQFMAITVKEELALSQKHASpYFTPEV---LDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEP 394
Cdd:cd03299 79 NYA-LFPHMTVYKNIAYGLKKRK-VDKKEIerkVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 395 LSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHF 428
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDF 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
248-426 |
2.35e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.06 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAI 326
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELA--LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIE 404
Cdd:PRK13650 98 TVEDDVAfgLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180
....*....|....*....|..
gi 489717269 405 QVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITH 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
247-436 |
3.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.78 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGrplLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL----------DYQGSLTWEGKEVAKLKERtyfqhVAQIF 316
Cdd:PRK13641 20 KKG---LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpssgtitiaGYHITPETGNKNLKKLRKK-----VSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 317 QNASDQFMAITVKEELALSQKH--ASPYFTPEVLDQALADLDLADH-MDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDE 393
Cdd:PRK13641 92 QFPEAQLFENTVLKDVEFGPKNfgFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 394 PLSGLDQKSIEQVVQLLQKCQeKSGQTILLISHHFYGISTWCD 436
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYAD 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
258-428 |
3.57e-12 |
|
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: 65.62 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLK--ERT-----YFQHVAQIFQnasdqfmAITVK 329
Cdd:TIGR03410 21 LEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKsGSIRLDGEDITKLPphERAragiaYVPQGREIFP-------RLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELAL------SQKHASPYFTPE---VLDQALA----DLdladhmdqvvyslSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:TIGR03410 94 ENLLTglaalpRRSRKIPDEIYElfpVLKEMLGrrggDL-------------SGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 397 GLdQKS----IEQVVQLLQKcqeKSGQTILLISHHF 428
Cdd:TIGR03410 161 GI-QPSiikdIGRVIRRLRA---EGGMAILLVEQYL 192
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
258-426 |
3.65e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.09 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY------QGSLTWEGKEVAKLKERTYFQHVAQIFQnASDQFMAITVKEE 331
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearvSGEVYLDGQDIFKMDVIELRRRVQMVFQ-IPNPIPNLSIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 332 LALSQK----HASPYFTPEVLDQAL--ADL--DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSI 403
Cdd:PRK14247 103 VALGLKlnrlVKSKKELQERVRWALekAQLwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENT 182
|
170 180
....*....|....*....|...
gi 489717269 404 EQVVQLLqkCQEKSGQTILLISH 426
Cdd:PRK14247 183 AKIESLF--LELKKDMTIVLVTH 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-185 |
3.74e-12 |
|
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: 64.76 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYgdreVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLggrsqammfqeAGEQF 84
Cdd:cd03215 5 LEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-----PASGEITL-----------DGKPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMATPREEIifameNLGkskteFA----DRLK--LASEFAEID-----SLLdqkivtmSGGEKQRVALAVLVAMDVDLFL 153
Cdd:cd03215 65 TRRSPRDAI-----RAG-----IAyvpeDRKRegLVLDLSVAEnialsSLL-------SGGNQQKVVLARWLARDPRVLI 127
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 154 LDEPFASVDPAARRFLIGRLAKLKEQGKTIII 185
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLL 159
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-162 |
4.06e-12 |
|
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: 66.42 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 19 VIRDLSLTLPAGTFSLLIGPTGCGKSTLLK-IMAGLYPKYGGQLTSGQVSLGGRSQAMMfqeageqftMATPREEIIFAM 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEGKIKHSGRISFSSQFSWIM---------PGTIKENIIFGV 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 98 ---ENLGKSKTEFADRLKLASEFAEID-SLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD 162
Cdd:cd03291 123 sydEYRYKSVVKACQLEEDITKFPEKDnTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
250-446 |
4.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.84 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 250 RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-------YQGSLTWEGKEVAKLKERTYFQHVAQIFQNAsDQ 322
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQP-NP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 FMAITVKEELA-------LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:PRK14246 102 FPHLSIYDNIAyplkshgIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQKCqeKSGQTILLISHHFYGISTWCDYHLRLAGREL 446
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-189 |
4.80e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.40 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 19 VIRDLSLTLPAGTFSLLIGPTGCGKSTLLK-IMAGLYPKYGGQLTSGQVSLGGRSQAMMfqeageqftMATPREEIIFAM 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEGKIKHSGRISFSPQTSWIM---------PGTIKDNIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 98 ENLGKSKTEFADRLKLA---SEFAEID-SLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGR- 172
Cdd:TIGR01271 512 SYDEYRYTSVIKACQLEediALFPEKDkTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESc 591
|
170
....*....|....*..
gi 489717269 173 LAKLKEQGKTIIITDHL 189
Cdd:TIGR01271 592 LCKLMSNKTRILVTSKL 608
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-162 |
5.96e-12 |
|
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: 65.18 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 10 LTFSY---GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQAMMFQEAGEQFTM 86
Cdd:cd03248 17 VTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFY-----QPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 87 ATPREEIIFA---MENL--GKSKTEFADRLKLA---------SEFA-EIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:cd03248 92 LVGQEPVLFArslQDNIayGLQSCSFECVKEAAqkahahsfiSELAsGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170
....*....|.
gi 489717269 152 FLLDEPFASVD 162
Cdd:cd03248 172 LILDEATSALD 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-225 |
5.99e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlYPKY--------GGQLTSGQVSLGGRS 72
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRAtsgrivfdGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 QAMMFQEAGEQFTMATPREEIifAMENLGKSKTEFADRLKLASE-FAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENL--AMGGFFAERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRFKGEQVDLltKDEQALLLATEPI 225
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVL--EDTGDALLANEAV 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-182 |
6.08e-12 |
|
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: 65.60 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY---------GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLypkygGQLTSGQVSLGG----- 70
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL-----EKPAQGTVSFRGqdlyq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 --RSQA--------MMFQEAGEQFTMATPREEIIF-AMENLGKSKTefADRLKLASEFAEI----DSLLDQKIVTMSGGE 135
Cdd:TIGR02769 78 ldRKQRrafrrdvqLVFQDSPSAVNPRMTVRQIIGePLRHLTSLDE--SEQKARIAELLDMvglrSEDADKLPRQLSGGQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 136 KQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKT 182
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGT 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-162 |
6.46e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYGGQLTSGQVSLGGRSQAMMFQE 79
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIKRNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 80 ----AGEQFTMATP---REEIIFAMEnlgksktefadRLKLAsefaeidSLLDQKIVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:PRK09544 81 tlplTVNRFLRLRPgtkKEDILPALK-----------RVQAG-------HLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170
....*....|
gi 489717269 153 LLDEPFASVD 162
Cdd:PRK09544 143 VLDEPTQGVD 152
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
227-432 |
6.56e-12 |
|
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: 63.87 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 227 LHFPLPENEPAAFVMKNFAIKQGRplleqkelsipkgKVTLItGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE 305
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGE-------------KIALL-GRSGSGKSTLLQLLTGDLKpQQGEITLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 306 rtyfqhvaqifqNASDQfmaITVkeelaLSQKhaspyftPEVLDQALadldladhMDQVVYSLSGGQKKKLEILLMLLSG 385
Cdd:cd03247 72 ------------ALSSL---ISV-----LNQR-------PYLFDTTL--------RNNLGRRFSGGERQRLALARILLQD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 386 QEVLLIDEPLSGLDQKSIEQVVQLLQKCQEksGQTILLISHHFYGIS 432
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIE 161
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
253-426 |
8.34e-12 |
|
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: 64.79 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKL-KERTYfqhvaqIFQNASdQFMAITVKE 330
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGKQITEPgPDRMV------VFQNYS-LLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 331 ELALSQKHASPYF-TPE---VLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:TIGR01184 74 NIALAVDRVLPDLsKSErraIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|.
gi 489717269 407 V-QLLQKCQEkSGQTILLISH 426
Cdd:TIGR01184 154 QeELMQIWEE-HRVTVLMVTH 173
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
66-279 |
1.00e-11 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 67.35 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 66 VSLGGRS----QAMMFQEAGE--QFTMATPREEIIfAMENLgkskTEFADRLKLASEFAeIDSL-LDQKIVTMSGGEKQR 138
Cdd:TIGR00630 423 VTVGGKSiadvSELSIREAHEffNQLTLTPEEKKI-AEEVL----KEIRERLGFLIDVG-LDYLsLSRAAGTLSGGEAQR 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 139 VALAV-----LVAMdvdLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH-----LFDDY-------QGKVDGVY 201
Cdd:TIGR00630 497 IRLATqigsgLTGV---LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHdedtiRAADYvidigpgAGEHGGEV 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 202 RFKGEQVDLLTKDEQ--ALLLATEpigLHFPLPEN----EPAAFVMKNFAIKQgrplLEQKELSIPKGKVTLITGPNGSG 275
Cdd:TIGR00630 574 VASGTPEEILANPDSltGQYLSGR---KKIEVPAErrpgNGKFLTLKGARENN----LKNITVSIPLGLFTCITGVSGSG 646
|
....
gi 489717269 276 KSSL 279
Cdd:TIGR00630 647 KSTL 650
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
253-426 |
1.11e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.07 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVA--KLKERTYFQHVAQIFQNASDQFMAITVK 329
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELAlsqkhaspyFTP--------EVLDQ-----ALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:PRK13637 103 KDIA---------FGPinlglseeEIENRvkramNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190
....*....|....*....|....*....|
gi 489717269 397 GLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSH 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-425 |
1.17e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGRSQAmmFQEA 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNY-----QPDAGSILIDGQEMR--FAST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 GEQFT--MATPREEI-----IFAMEN--LGK--SKTEFADRLKLASEFAE--------IDSllDQKIVTMSGGEKQRVAL 141
Cdd:PRK11288 74 TAALAagVAIIYQELhlvpeMTVAENlyLGQlpHKGGIVNRRLLNYEAREqlehlgvdIDP--DTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 142 AVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRFK-GEQVDllTKDEQALL- 219
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKdGRYVA--TFDDMAQVd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 220 ---LATEPIG------LHFPLPENEPAAFVMKNFaikQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAM---TKLl 287
Cdd:PRK11288 230 rdqLVQAMVGreigdiYGYRPRPLGEVRLRLDGL---KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLygaTRR- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 288 dYQGSLTWEGKEVaklKERTYFQHVAQ-------------IFQNASdqfmaitVKEELALS-QKHASPYFTpeVLDQ--- 350
Cdd:PRK11288 306 -TAGQVYLDGKPI---DIRSPRDAIRAgimlcpedrkaegIIPVHS-------VADNINISaRRHHLRAGC--LINNrwe 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 351 -ALADLDLAD------HMDQVVYSLSGGQKKKLeILLMLLS-GQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTIL 422
Cdd:PRK11288 373 aENADRFIRSlniktpSREQLIMNLSGGNQQKA-ILGRWLSeDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVL 450
|
...
gi 489717269 423 LIS 425
Cdd:PRK11288 451 FVS 453
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
258-426 |
1.30e-11 |
|
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: 64.10 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNAsdQFMAITVKEELALSQ 336
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIGLVSQEP--VLFDGTIAENIRYGK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 337 KHASPYFTPEVLDQALAD---LDLADHMDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSiEQVVQ- 408
Cdd:cd03249 102 PDATDEEVEEAAKKANIHdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES-EKLVQe 180
|
170
....*....|....*...
gi 489717269 409 LLQKCQEksGQTILLISH 426
Cdd:cd03249 181 ALDRAMK--GRTTIVIAH 196
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
253-448 |
1.32e-11 |
|
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: 64.35 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTklldyqGSLTWEGKEVAKLKERTYF--QHVAQIFQNASDQFMAITVKE 330
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLA------GVLKPDEGDIEIELDTVSYkpQYIKADYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 331 elalsqKHASPYFTPEVLDQaladLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDqksIEQ---VV 407
Cdd:cd03237 89 ------FYTHPYFKTEIAKP----LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD---VEQrlmAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 408 QLLQKCQEKSGQTILLISHHFYGIstwcDYhlrLAGRELAF 448
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEHDIIMI----DY---LADRLIVF 189
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
258-426 |
1.42e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLldYQ---GSLTWEGKEVA--------KLKERTYFQHvaqifqnasdqFM-- 324
Cdd:COG3845 26 LTVRPGEIHALLGENGAGKSTLMKILYGL--YQpdsGEILIDGKPVRirsprdaiALGIGMVHQH-----------FMlv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 -AITVKEELALSQKHASPYFTPevLDQALADL-DLADHM------DQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:COG3845 93 pNLTVAENIVLGLEPTKGGRLD--RKAARARIrELSERYgldvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190
....*....|....*....|....*....|
gi 489717269 397 GLDQKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:COG3845 171 VLTPQEADELFEILRRLAAE-GKSIIFITH 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-157 |
1.46e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 15 GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGG--QLTSGqVSLGgrsqaMMFQE------------- 79
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeaRPAPG-IKVG-----YLPQEpqldpektvrenv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 80 ---AGEQFTMATPREEIifaMENLGkskTEFADRLKLASEFAE------------IDSLL------------DQKIVTMS 132
Cdd:PRK11819 92 eegVAEVKAALDRFNEI---YAAYA---EPDADFDALAAEQGElqeiidaadawdLDSQLeiamdalrcppwDAKVTKLS 165
|
170 180
....*....|....*....|....*
gi 489717269 133 GGEKQRVALAVLVAMDVDLFLLDEP 157
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
253-426 |
1.59e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.42 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY------QGSLTWEGKEV-------AKLKERtyfqhVAQIFQNA 319
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrvEGKVTFHGKNLyapdvdpVEVRRR-----IGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 320 SDqfMAITVKEELALSQK-HASPYFTPEVLDQAL--ADL--DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEP 394
Cdd:PRK14243 101 NP--FPKSIYDNIAYGARiNGYKGDMDELVERSLrqAALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 395 LSGLDQKSIEQVVQLLQKCQEKsgQTILLISH 426
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQ--YTIIIVTH 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
248-426 |
1.65e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKLK--ERTYFQHVAQ-IFQnasDQF 323
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRGEPLAKLNraQRKAFRRDIQmVFQ---DSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 MAI----TVKEELALSQKHASPYFTPEVLDQALADLDLAD----HMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:PRK10419 100 SAVnprkTVREIIREPLRHLLSLDKAERLARASEMLRAVDlddsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-215 |
1.81e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHL--TFSYG---DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGG--------- 70
Cdd:COG1101 2 LELKNLskTFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP-----PDSGSILIDGkdvtklpey 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 -RSQ--AMMFQE--AG--------EQFTMATPReeiifamenlGKSKT-----------EFADRLKlasefaeidSL--- 123
Cdd:COG1101 77 kRAKyiGRVFQDpmMGtapsmtieENLALAYRR----------GKRRGlrrgltkkrreLFRELLA---------TLglg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 124 ----LDQKIVTMSGGekQRVALAVLVAM--DVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGK--TIIITDHLFD--DY 193
Cdd:COG1101 138 lenrLDTKVGLLSGG--QRQALSLLMATltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNltTLMVTHNMEQalDY 215
|
250 260 270
....*....|....*....|....*....|
gi 489717269 194 --------QGKVdgVYRFKGEQVDLLTKDE 215
Cdd:COG1101 216 gnrlimmhEGRI--ILDVSGEEKKKLTVED 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
250-426 |
2.03e-11 |
|
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: 62.23 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 250 RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEVAKLKERTYFQHVAQIFQNasDQFMAITV 328
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLrPTSGRVRLDGADISQWDPNELGDHVGYLPQD--DELFSGSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 KEELalsqkhaspyftpevldqaladldladhmdqvvysLSGGQKKKLeILLMLLSGQEVLLI-DEPLSGLDQ---KSIE 404
Cdd:cd03246 93 AENI-----------------------------------LSGGQRQRL-GLARALYGNPRILVlDEPNSHLDVegeRALN 136
|
170 180
....*....|....*....|..
gi 489717269 405 QVVQLLQkcqeKSGQTILLISH 426
Cdd:cd03246 137 QAIAALK----AAGATRIVIAH 154
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-194 |
2.19e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlYPKYggQLTSGQVslggrsqamMFQeaGEQF 84
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAY--KILEGDI---------LFK--GESI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMATPREEI---IF-----AMENLGKSKTEFadrLKLA-------SEFAEID-----SLLDQK--IVTM----------- 131
Cdd:CHL00131 74 LDLEPEERAhlgIFlafqyPIEIPGVSNADF---LRLAynskrkfQGLPELDpleflEIINEKlkLVGMdpsflsrnvne 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 132 --SGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHlfddYQ 194
Cdd:CHL00131 151 gfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH----YQ 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-425 |
2.27e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYP--KYGGQLTSGQVSLGGRSQAMMfQEAG- 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDT-ERAGi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 ---EQFTMATPREEIifaMEN--LGKSKTEFADRLKLASEFAEIDSLLDQ----------KIVTMSGGEKQRVALAVLVA 146
Cdd:TIGR02633 81 viiHQELTLVPELSV---AENifLGNEITLPGGRMAYNAMYLRAKNLLRElqldadnvtrPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 147 MDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRFK-GEQVDllTKDEQAL------- 218
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRdGQHVA--TKDMSTMseddiit 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 219 ---------LLATEP--IGLHFPLPENEPAAFVMkNFAIKQgrplLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL 287
Cdd:TIGR02633 236 mmvgreitsLYPHEPheIGDVILEARNLTCWDVI-NPHRKR----VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 288 D--YQGSLTWEGKEVA-KLKERTYFQHVAQIFQNASDQ----FMAITVKEELALSQKhaspYFTPEVLDQAlADLDLAD- 359
Cdd:TIGR02633 311 PgkFEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKRHgivpILGVGKNITLSVLKS----FCFKMRIDAA-AELQIIGs 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 360 ----------HMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLL-QKCQEksGQTILLIS 425
Cdd:TIGR02633 386 aiqrlkvktaSPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInQLAQE--GVAIIVVS 460
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-188 |
2.36e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.82 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 9 HLTFSYGDREVI--RDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPkyggqlTSGQVSLGG--------------- 70
Cdd:PRK11153 8 SKVFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRP------TSGRVLVDGqdltalsekelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQAMMFQeageQFTMATPR---EEIIFAMENLGKSKTEFADRlklASEFAEIDSLLDQKIV---TMSGGEKQRVALAVL 144
Cdd:PRK11153 82 RQIGMIFQ----HFNLLSSRtvfDNVALPLELAGTPKAEIKAR---VTELLELVGLSDKADRypaQLSGGQKQRVAIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 145 VAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITH 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-157 |
2.43e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 8 DHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQ-VSLGGRSQammFQEA--GEQf 84
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtVKLAYVDQ---SRDAldPNK- 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 85 tmaTPREEIIFAMENLGKSKTEFADRLKLAS-EFAEIDSlldQKIV-TMSGGEKQRVALAVLVAMDVDLFLLDEP 157
Cdd:PRK11819 404 ---TVWEEISGGLDIIKVGNREIPSRAYVGRfNFKGGDQ---QKKVgVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
212-427 |
2.78e-11 |
|
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: 66.19 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 212 TKDEQALLlATEPI-----------GLHFPLPENEPAAFV----MKNFAI---KQGRPLLEQKELSIPKGKVTLITGPNG 273
Cdd:TIGR01257 888 TREERALE-KTEPLteemedpehpeGINDSFFERELPGLVpgvcVKNLVKifePSGRPAVDRLNITFYENQITAFLGHNG 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 274 SGKSSLFKAMTKLLD-YQGSLTWEGKEVaklkeRTYFQHVAQIFQNASDQ---FMAITVKEE-LALSQKHASPYFTPEV- 347
Cdd:TIGR01257 967 AGKTTTLSILTGLLPpTSGTVLVGGKDI-----ETNLDAVRQSLGMCPQHnilFHHLTVAEHiLFYAQLKGRSWEEAQLe 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 348 LDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKcqEKSGQTILLISHH 427
Cdd:TIGR01257 1042 MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK--YRSGRTIIMSTHH 1119
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-426 |
3.34e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKS-TLLKIMAgLYPKYGGQLTSGQVSLGGRSQ---------------------AMMF 77
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGLVQCDKMLLRRRSRqvielseqsaaqmrhvrgadmAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 78 QEAGEQ----FTMATPREEIIFAMENLGKSKT-EFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:PRK10261 111 QEPMTSlnpvFTVGEQIAESIRLHQGASREEAmVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 153 LLDEPFASVD---PAARRFLIGRLAKLKEQGKTIIITDH-LFDDYQGKVDGVYRfkGEQVDLLTKDE----------QAL 218
Cdd:PRK10261 191 IADEPTTALDvtiQAQILQLIKVLQKEMSMGVIFITHDMgVVAEIADRVLVMYQ--GEAVETGSVEQifhapqhpytRAL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 219 LLATEPIGL--------HFPL---PENEPAAFVMKNFAIKQGRPLLEQKEL--------------------------SIP 261
Cdd:PRK10261 269 LAAVPQLGAmkgldyprRFPLislEHPAKQEPPIEQDTVVDGEPILQVRNLvtrfplrsgllnrvtrevhavekvsfDLW 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 262 KGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKL---KERTYFQHVAQIFQN--AS---DQFMAITVKEEL 332
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLspgKLQALRRDIQFIFQDpyASldpRQTVGDSIMEPL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 333 ---ALSQKHASPYFTPEVLDQALAdldLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQL 409
Cdd:PRK10261 429 rvhGLLPGKAAAARVAWLLERVGL---LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
|
490
....*....|....*..
gi 489717269 410 LQKCQEKSGQTILLISH 426
Cdd:PRK10261 506 LLDLQRDFGIAYLFISH 522
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
258-451 |
3.92e-11 |
|
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: 63.43 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQ----HVAQIFQNasdqfMAI----TV 328
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQS-----FALlphrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 KEELA--LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQV 406
Cdd:cd03294 120 LENVAfgLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 407 VQLLQKCQEKSGQTILLISHHFygistwcDYHLRLAGReLAFVQD 451
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDL-------DEALRLGDR-IAIMKD 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-188 |
3.94e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQL-TSGQVSLGGR-----SQAMMFQ 78
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkVDGKVLYFGKdifqiDAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 79 EAGEQFTMATP------REEIIFAMENLG-KSKTEFA----DRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAM 147
Cdd:PRK14246 91 EVGMVFQQPNPfphlsiYDNIAYPLKSHGiKEKREIKkiveECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 148 DVDLFLLDEPFASVDPAARRFLIGRLAKLKEQgKTIIITDH 188
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSH 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
257-426 |
4.54e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 257 ELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGkEVAKLKERTYF---------QHVAQIFQnASDQFMAIT 327
Cdd:PRK14267 24 DLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEG-EVRLFGRNIYSpdvdpievrREVGMVFQ-YPNPFPHLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQKHASPYFTPEVLDQ---------ALADlDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:PRK14267 102 IYDNVAIGVKLNGLVKSKKELDErvewalkkaALWD-EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANI 180
|
170 180
....*....|....*....|....*...
gi 489717269 399 DQKSIEQVVQLLQKCqeKSGQTILLISH 426
Cdd:PRK14267 181 DPVGTAKIEELLFEL--KKEYTIVLVTH 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
258-426 |
4.82e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.72 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTkLLDY--QGSLTWEG-----------KEVAKLKertyfQHVAQIFQnasdQFM 324
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLN-LLEMprSGTLNIAGnhfdfsktpsdKAIRELR-----RNVGMVFQ----QYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 A---ITVKEEL--------ALSQKHASpyftpEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDE 393
Cdd:PRK11124 93 LwphLTVQQNLieapcrvlGLSKDQAL-----ARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 394 PLSGLDQKSIEQVVQLLQKCQEkSGQTILLISH 426
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAE-TGITQVIVTH 199
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-188 |
5.09e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.56 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHL--TFSYGDREVI--RDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPkyggqlTSGQVSLGG--------- 70
Cdd:COG1135 2 IELENLskTFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLeRP------TSGSVLVDGvdltalser 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 ------RSQAMMFQeageQF---TMATPREEIIFAMENLGKSKTEFADRlklasefaeIDSLLDqkIV-----------T 130
Cdd:COG1135 76 elraarRKIGMIFQ----HFnllSSRTVAENVALPLEIAGVPKAEIRKR---------VAELLE--LVglsdkadaypsQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 131 MSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITH 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
258-426 |
6.17e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 63.58 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGK-VTLItGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLK--ERtyfqHVAQIFQNAsdqfmAI----TVK 329
Cdd:COG3842 26 LSIEPGEfVALL-GPSGCGKTTLLRMIAGFETpDSGRILLDGRDVTGLPpeKR----NVGMVFQDY-----ALfphlTVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELA--LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKkkleillmllsgQ------------EVLLIDEPL 395
Cdd:COG3842 96 ENVAfgLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQ------------QrvalaralapepRVLLLDEPL 163
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG3842 164 SALDAKLREEMREELRRLQRELGITFIYVTH 194
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-188 |
6.45e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.36 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSY---GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG------- 70
Cdd:TIGR00958 475 LEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY-----QPTGGQVLLDGvplvqyd 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 -----RSQAMMFQEAgeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAE-----IDSLLDQKIVTMSGGEKQRVA 140
Cdd:TIGR00958 550 hhylhRQVALVGQEP--VLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMefpngYDTEVGEKGSQLSGGQKQRIA 627
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 141 LAVLVAMDVDLFLLDEPFASVDPAARRFLigrLAKLKEQGKTIIITDH 188
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLL---QESRSRASRTVLLIAH 672
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-188 |
6.95e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.27 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSYGDREV--IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGG--------- 70
Cdd:PRK11176 339 KGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY-----DIDEGEILLDGhdlrdytla 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 --RSQ-AMMFQE---------------AGEQFTmatpREEIifamenlgksktEFADRLKLASEFAE-IDSLLDQKI--- 128
Cdd:PRK11176 414 slRNQvALVSQNvhlfndtianniayaRTEQYS----REQI------------EEAARMAYAMDFINkMDNGLDTVIgen 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 129 -VTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQgKTIIITDH 188
Cdd:PRK11176 478 gVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAH 537
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-192 |
7.10e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 17 REV--IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPkyggqlTSGQVSLGGRsqammfqeageqftmaTPREE- 92
Cdd:COG4586 33 REVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP------TSGEVRVLGY----------------VPFKRr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 93 --------IIF-----------AMENL-------GKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQR--VALAVL 144
Cdd:COG4586 91 kefarrigVVFgqrsqlwwdlpAIDSFrllkaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAAALL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489717269 145 VAMDVdLFlLDEPFASVDPAA----RRFligrLAKL-KEQGKTIIITDHLFDD 192
Cdd:COG4586 171 HRPKI-LF-LDEPTIGLDVVSkeaiREF----LKEYnRERGTTILLTSHDMDD 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-215 |
7.35e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.51 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGdrevIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQA------ 74
Cdd:PRK10070 29 LSKEQILEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 -----MMFQEAGEQFTMaTPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDV 149
Cdd:PRK10070 105 rkkiaMVFQSFALMPHM-TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 150 DLFLLDEPFASVDPAARRFLIGRLAKLK-EQGKTIIITDHLFDDYQGKVDGVYRFK-GEQVDLLTKDE 215
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQnGEVVQVGTPDE 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-185 |
7.39e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkyggQLTSGQVSLGGR-----SQAM-----------MFQEAgEQFT 85
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLT-----RPQKGRIVLNGRvlfdaEKGIclppekrrigyVFQDA-RLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 86 MATPREEIIFAMENlgKSKTEFADRLKLASefaeIDSLLDQKIVTMSGGEKQRVAL--AVLVAmdVDLFLLDEPFASVDP 163
Cdd:PRK11144 90 HYKVRGNLRYGMAK--SMVAQFDKIVALLG----IEPLLDRYPGSLSGGEKQRVAIgrALLTA--PELLLMDEPLASLDL 161
|
170 180
....*....|....*....|..
gi 489717269 164 AARRFLIGRLAKLKEQGKTIII 185
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPIL 183
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
23-192 |
7.50e-11 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 64.21 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 23 LSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYGGQLTSGQ-VSLGGRSQ-AMMFQEAGEQFTMATPREEIIFAMEN 99
Cdd:TIGR01194 361 IDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYiPQEGEILLDGAaVSADSRDDyRDLFSAIFADFHLFDDLIGPDEGEHA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 100 LGKSKTEFADRLKLASEfAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGR-LAKLKE 178
Cdd:TIGR01194 441 SLDNAQQYLQRLEIADK-VKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEElLPDLKR 519
|
170
....*....|....
gi 489717269 179 QGKTIIITDHlfDD 192
Cdd:TIGR01194 520 QGKTIIIISH--DD 531
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
248-437 |
7.95e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQkELSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEV---AKLKE-RTYFQHVAQIFQNASDQ 322
Cdd:PRK13649 19 EGRALFDV-NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDTLItstSKNKDiKQIRKKVGLVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 FMAITVKEELA-------LSQKHAspyftpevldQALADLDLA------DHMDQVVYSLSGGQKKKLEILLMLLSGQEVL 389
Cdd:PRK13649 98 LFEETVLKDVAfgpqnfgVSQEEA----------EALAREKLAlvgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 390 LIDEPLSGLDQKSIEQVVQLLQKCQEkSGQTILLISHHFYGISTWCDY 437
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADF 214
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-188 |
8.17e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.00 E-value: 8.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 35 LIGPTGCGKSTLLKIMAG-LYP------------------------KYGGQLTSGQVSLGGRSQAMmfQEAGEQFTMATp 89
Cdd:cd03236 31 LVGPNGIGKSTALKILAGkLKPnlgkfddppdwdeildefrgselqNYFTKLLEGDVKVIVKPQYV--DLIPKAVKGKV- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 90 rEEIIFAMENLGKsKTEFADRLklasefaEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD-----PA 164
Cdd:cd03236 108 -GELLKKKDERGK-LDELVDQL-------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqrlNA 178
|
170 180
....*....|....*....|....
gi 489717269 165 ARrfLIGRLAklkEQGKTIIITDH 188
Cdd:cd03236 179 AR--LIRELA---EDDNYVLVVEH 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
249-426 |
1.01e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL--LDyQGSLTWEGKEVAKL-KERtyfQHVAQIFQNASdQFMA 325
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFetPD-SGRIMLDGQDITHVpAEN---RHVNTVFQSYA-LFPH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALS---QKHASPYFTPEVLDqALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:PRK09452 101 MTVFENVAFGlrmQKTPAAEITPRVME-ALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
170 180
....*....|....*....|....
gi 489717269 403 IEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK09452 180 RKQMQNELKALQRKLGITFVFVTH 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
258-426 |
1.14e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.43 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAklkertyFQHVAQI---------FQNasdqfmaIT 327
Cdd:COG4152 22 FTVPKGEIFGLLGPNGAGKTTTIRIILGILApDSGEVLWDGEPLD-------PEDRRRIgylpeerglYPK-------MK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELA-------LSQKHAspyftPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:COG4152 88 VGEQLVylarlkgLSKAEA-----KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180
....*....|....*....|....*.
gi 489717269 401 KSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:COG4152 163 VNVELLKDVIRELAAK-GTTVIFSSH 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
251-429 |
1.30e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEvAKLKERT----YFQHVAQIFQNASdqfma 325
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKT-ATRGDRSrfmaYLGHLPGLKADLS----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 itVKEEL----ALSQKHASPyfTPevlDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:PRK13543 99 --TLENLhflcGLHGRRAKQ--MP---GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
170 180
....*....|....*....|....*...
gi 489717269 402 SIEQVVQLLQkCQEKSGQTILLISHHFY 429
Cdd:PRK13543 172 GITLVNRMIS-AHLRGGGAALVTTHGAY 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
263-426 |
1.45e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.49 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFmAITVKEELALSQ-KHASP 341
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF-AMPVFQYLTLHQpDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 342 YFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLL--------SGQeVLLIDEPLSGLDqksIEQVV---QLL 410
Cdd:PRK03695 101 EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinpAGQ-LLLLDEPMNSLD---VAQQAaldRLL 176
|
170
....*....|....*..
gi 489717269 411 QK-CQekSGQTILLISH 426
Cdd:PRK03695 177 SElCQ--QGIAVVMSSH 191
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
5-189 |
1.47e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.27 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDReVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRSQ---AMMFQEAG 81
Cdd:PRK13541 2 LSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpycTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 EQFTMaTPREEIIFAMENLGKSKTEFAdrlklASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASV 161
Cdd:PRK13541 81 LKLEM-TVFENLKFWSEIYNSAETLYA-----AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180
....*....|....*....|....*...
gi 489717269 162 DPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-425 |
1.47e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ-LTSGQ-VSLGGRSQA------MMFQEageqFTMATPREei 93
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSiLFQGKeIDFKSSKEAlengisMVHQE----LNLVLQRS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 94 ifAMEN--LGK--SKTEFADRLKLASE----FAEIDSLLD--QKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDP 163
Cdd:PRK10982 90 --VMDNmwLGRypTKGMFVDQDKMYRDtkaiFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 164 AARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVYRFKGEQ------VDLLTKDEQALLLATEPIGLHFPLPENEPA 237
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQwiatqpLAGLTMDKIIAMMVGRSLTQRFPDKENKPG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 238 AFVM--KNF-AIKQgrPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVaklKERTYFQHVA 313
Cdd:PRK10982 248 EVILevRNLtSLRQ--PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKsAGTITLHGKKI---NNHNANEAIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 314 Q-------------IFQNASDQFMAI-----TVKEELALSQKHASPYFTPEVLDQalADLDLADHMDQvVYSLSGGQKKK 375
Cdd:PRK10982 323 HgfalvteerrstgIYAYLDIGFNSLisnirNYKNKVGLLDNSRMKSDTQWVIDS--MRVKTPGHRTQ-IGSLSGGNQQK 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 489717269 376 LEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLIS 425
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIIS 448
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-188 |
1.67e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 17 REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkygGQLTSGQVSLggrsqammfqeAGEQFtmatPREEIIfa 96
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---GTPVAGCVDV-----------PDNQF----GREASL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 97 MENLGKS-----KTEFADRLKLASEFaeidsLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIG 171
Cdd:COG2401 103 IDAIGRKgdfkdAVELLNAVGLSDAV-----LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170
....*....|....*...
gi 489717269 172 RLAKL-KEQGKTIIITDH 188
Cdd:COG2401 178 NLQKLaRRAGITLVVATH 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
216-428 |
1.68e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 216 QALLLATEPIGLHFPLPENEPAAFVMKN----FAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQg 291
Cdd:PLN03232 592 EELLLSEERILAQNPPLQPGAPAISIKNgyfsWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 292 sltwEGKEVAKLKERTYFQHVAQIFqNAsdqfmaiTVKEELALSQKHASPYFTPEVLDQALA-DLDLADHMDQVV----- 365
Cdd:PLN03232 671 ----ETSSVVIRGSVAYVPQVSWIF-NA-------TVRENILFGSDFESERYWRAIDVTALQhDLDLLPGRDLTEigerg 738
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 366 YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKcQEKSGQTILLISH--HF 428
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNqlHF 802
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-191 |
2.41e-10 |
|
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: 62.51 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDRE-----VIRDLSLTLPAG--TFslLIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGRSQAMM 76
Cdd:COG4615 327 TLELRGVTYRYPGEDgdegfTLGPIDLTIRRGelVF--IVGGNGSGKSTLAKLLTGLYRP-----ESGEILLDGQPVTAD 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 FQEA-GEQFTmatpreeIIFA----MENL----GKSKTEFAD----RLKLasefAEIDSLLDQKIVT--MSGGEKQRVAL 141
Cdd:COG4615 400 NREAyRQLFS-------AVFSdfhlFDRLlgldGEADPARARelleRLEL----DHKVSVEDGRFSTtdLSQGQRKRLAL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 142 AVLVAMDVDLFLLDEPFASVDPAARRF----LigrLAKLKEQGKTII-IT--DHLFD 191
Cdd:COG4615 469 LVALLEDRPILVFDEWAADQDPEFRRVfyteL---LPELKARGKTVIaIShdDRYFD 522
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
244-426 |
2.89e-10 |
|
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: 60.32 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 244 FAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQ----- 317
Cdd:cd03253 8 FAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSsGSILIDGQDIREVTLDSLRRAIGVVPQdtvlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 NAsdqfmaiTVKEELALSQKHASPyftPEVLDQALAdldlADHMDQVV-----YS---------LSGGQKKKLEILLMLL 383
Cdd:cd03253 88 ND-------TIGYNIRYGRPDATD---EEVIEAAKA----AQIHDKIMrfpdgYDtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 384 SGQEVLLIDEPLSGLDQKSiEqvvQLLQKCQEK--SGQTILLISH 426
Cdd:cd03253 154 KNPPILLLDEATSALDTHT-E---REIQAALRDvsKGRTTIVIAH 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
258-426 |
3.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWE------GKEVAKLKerTYFQHVAQIFQNASDQFMAITVKE 330
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIGervitaGKKNKKLK--PLRKKVGIVFQFPEHQLFEETVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 331 ELAlsqkhaspyFTP--------EVLDQALADLDL----ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:PRK13634 106 DIC---------FGPmnfgvseeDAKQKAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180
....*....|....*....|....*...
gi 489717269 399 DQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
251-426 |
3.20e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.96 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNA---SDqfmai 326
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQVALVSQNVhlfND----- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELAL-SQKHASPYFTPEVLDQALAdLDLADHMDQVV--------YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSG 397
Cdd:PRK11176 432 TIANNIAYaRTEQYSREQIEEAARMAYA-MDFINKMDNGLdtvigengVLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 398 LDQKS---IEQVVQLLQKcqeksGQTILLISH 426
Cdd:PRK11176 511 LDTESeraIQAALDELQK-----NRTSLVIAH 537
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-188 |
3.57e-10 |
|
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: 59.65 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 12 FSYG-DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQL--------TSGQVSLGGRSQAMMFQEAGE 82
Cdd:cd03290 8 FSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 83 QFTM-ATPREEIIFAMENlgkSKTEFADRLKLASEFAEIDSL-------LDQKIVTMSGGEKQRVALAVLVAMDVDLFLL 154
Cdd:cd03290 88 PWLLnATVEENITFGSPF---NKQRYKAVTDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 155 DEPFASVDPAARRFLI--GRLAKLKEQGKTIIITDH 188
Cdd:cd03290 165 DDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTH 200
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
258-426 |
3.62e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTkLLDY--QGSLTWEGKEV---AKLKERTYF---QHVAQIFQNaSDQFMAITVK 329
Cdd:COG4161 23 LECPSGETLVLLGPSGAGKSSLLRVLN-LLETpdSGQLNIAGHQFdfsQKPSEKAIRllrQKVGMVFQQ-YNLWPHLTVM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EEL--------ALSQKHASpyftpEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:COG4161 101 ENLieapckvlGLSKEQAR-----EKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180
....*....|....*....|....*
gi 489717269 402 SIEQVVQLLQKCQEkSGQTILLISH 426
Cdd:COG4161 176 ITAQVVEIIRELSQ-TGITQVIVTH 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-425 |
3.83e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkYGGQltSGQVSLGGRSQ------- 73
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP-HGTY--EGEIIFEGEELqasnird 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 ------AMMFQEAG--EQFTMAtpreEIIFamenLGKSKTEFAdRLKLASEFAEIDSLLDQ---------KIVTMSGGEK 136
Cdd:PRK13549 79 teragiAIIHQELAlvKELSVL----ENIF----LGNEITPGG-IMDYDAMYLRAQKLLAQlkldinpatPVGNLGLGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 137 QRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDG--VYRfKGEQV-----D 209
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTicVIR-DGRHIgtrpaA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 210 LLTKDEQALLLATEPIGLHFPLPENEPAAFVM--KNF----AIKQGRPLLEQKELSIPKGKVTLITGPNGSGK----SSL 279
Cdd:PRK13549 229 GMTEDDIITMMVGRELTALYPREPHTIGEVILevRNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRtelvQCL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 280 FKAmtklldYQGSltWEGK---EVAKLKERTYFQHVAQ-------------------IFQN----ASDQFMAITVKEElA 333
Cdd:PRK13549 309 FGA------YPGR--WEGEifiDGKPVKIRNPQQAIAQgiamvpedrkrdgivpvmgVGKNitlaALDRFTGGSRIDD-A 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 334 LSQKHAspyftpevlDQALADLDL-ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD-------QKSIEQ 405
Cdd:PRK13549 380 AELKTI---------LESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakyeiYKLINQ 450
|
490 500
....*....|....*....|
gi 489717269 406 VVQllqkcqekSGQTILLIS 425
Cdd:PRK13549 451 LVQ--------QGVAIIVIS 462
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
249-426 |
4.50e-10 |
|
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: 59.81 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKLKERTYFQHVAQIFQnaSDQFMAIT 327
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVLQ--ENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQKHASPYFTPEVLDQALAD---LDLADHMDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQ 400
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAGAHdfiSELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180
....*....|....*....|....*..
gi 489717269 401 KSIEQVVQLLQK-CqekSGQTILLISH 426
Cdd:cd03252 172 ESEHAIMRNMHDiC---AGRTVIIIAH 195
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-188 |
4.52e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPKYGGQLTSGQVSLGGRSQAMMFQEAGeqftmatpREEIIFAME 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVDIKGSAALIAISSGLNGQLTG--------IENIELKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 99 NLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKE 178
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKE 191
|
170
....*....|
gi 489717269 179 QGKTIIITDH 188
Cdd:PRK13545 192 QGKTIFFISH 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
251-426 |
4.82e-10 |
|
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: 59.66 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKERTyfQHVAQIFQNASdQFMAITVK 329
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGGEDATDVPVQE--RNVGFVFQHYA-LFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELA--LSQKHASPYFTPEVLDQALADL----DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSI 403
Cdd:cd03296 93 DNVAfgLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180
....*....|....*....|...
gi 489717269 404 EQVVQLLQKCQEKSGQTILLISH 426
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTH 195
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-186 |
5.00e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 10 LTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ--LTSGQVSLGGRSQAMMFqeageqFTMA 87
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQiqIDGKTATRGDRSRFMAY------LGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 88 TPREEIIFAMENLG--------KSKTEFADRLKLASEFAEIDSLLDQkivtMSGGEKQRVALAVLVAMDVDLFLLDEPFA 159
Cdd:PRK13543 91 PGLKADLSTLENLHflcglhgrRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180
....*....|....*....|....*....
gi 489717269 160 SVDPAARRfLIGRL--AKLKEQGKTIIIT 186
Cdd:PRK13543 167 NLDLEGIT-LVNRMisAHLRGGGAALVTT 194
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-192 |
5.12e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLT-FSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkYGGQLTSGQVSLggRSQAMMF----- 77
Cdd:PRK11174 349 TIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIEL--RELDPESwrkhl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 78 ----QEAgeQFTMATPREEIIFAMENLGKSKTEFADRLKLASEFaeIDSL---LDQKI----VTMSGGEKQRVALAVLVA 146
Cdd:PRK11174 426 swvgQNP--QLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEF--LPLLpqgLDTPIgdqaAGLSVGQAQRLALARALL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489717269 147 MDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITdHLFDD 192
Cdd:PRK11174 502 QPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQLED 546
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
258-427 |
5.95e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.21 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKL--KERTyfqhVAQIFQNaSDQFMAITVKEELAL 334
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTpASGSLTLNGQDHTTTppSRRP----VSMLFQE-NNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 ----------SQKHAspyftpevLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIE 404
Cdd:PRK10771 95 glnpglklnaAQREK--------LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180
....*....|....*....|....
gi 489717269 405 QVVQLL-QKCQEKsGQTILLISHH 427
Cdd:PRK10771 167 EMLTLVsQVCQER-QLTLLMVSHS 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-185 |
8.44e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.75 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-PKYGGQLTSGQ----VSLGG--RSQ 73
Cdd:PRK13657 332 KGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQSGRILIDGTdirtVTRASlrRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQEAGeqftmatpreeiIFAM---ENL--GK---SKTEFADRLKL--ASEFAE-----IDSLLDQKIVTMSGGEKQR 138
Cdd:PRK13657 412 AVVFQDAG------------LFNRsieDNIrvGRpdaTDEEMRAAAERaqAHDFIErkpdgYDTVVGERGRQLSGGERQR 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 139 VALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIII 185
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII 526
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
244-426 |
9.13e-10 |
|
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: 58.50 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 244 FAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMT-KLLDYQGSLTW-------EGKEVAKLKERTYFQHVAQi 315
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWsnknesePSFEATRSRNRYSVAYAAQ- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 316 fqnaSDQFMAITVKEELALsqkhASPYFTPE---VLDQA--LADLDLADHMDQVV-----YSLSGGQKKKLEILLMLLSG 385
Cdd:cd03290 87 ----KPWLLNATVEENITF----GSPFNKQRykaVTDACslQPDIDLLPFGDQTEigergINLSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 386 QEVLLIDEPLSGLDQKSIEQVVQ--LLQKCQEKSgQTILLISH 426
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTH 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-197 |
9.45e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 9.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 7 IDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAglypkygGQL--TSGQVSLGGRSQAMMFqeagEQF 84
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQLqaDSGRIHCGTKLEVAYF----DQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 85 TMATPREEIIfaMENLGKSKTEFA----DR--LKLASEFaeidsLLDQK-----IVTMSGGEKQRVALAVLVAMDVDLFL 153
Cdd:PRK11147 391 RAELDPEKTV--MDNLAEGKQEVMvngrPRhvLGYLQDF-----LFHPKramtpVKALSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 154 LDEPFASVDpaarrflIGRLAKLKEqgktiiitdhLFDDYQGKV 197
Cdd:PRK11147 464 LDEPTNDLD-------VETLELLEE----------LLDSYQGTV 490
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
258-426 |
1.25e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTW-----EGKEVAKLKE---------RTYFQHVAQI------- 315
Cdd:PRK13651 28 VEINQGEFIAIIGQTGSGKTTFIEHLNALLlPDTGTIEWifkdeKNKKKTKEKEkvleklviqKTRFKKIKKIkeirrrv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 316 ---FQNASDQFMAITVKEELALSqkhASPYFTP--EVLDQA-----LADLDLaDHMDQVVYSLSGGQKKKLEILLMLLSG 385
Cdd:PRK13651 108 gvvFQFAEYQLFEQTIEKDIIFG---PVSMGVSkeEAKKRAakyieLVGLDE-SYLQRSPFELSGGQKRRVALAGILAME 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489717269 386 QEVLLIDEPLSGLDQKSIEQVVQLLQKCQeKSGQTILLISH 426
Cdd:PRK13651 184 PDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTH 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
258-426 |
1.43e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.33 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKG-KVTLItGPNGSGKSSLFKAMTKLLdY--QGSLTWEGKEVAKlKERTYFQHVAQIFQNASDQFMAITVKEELAL 334
Cdd:COG4586 43 FTIEPGeIVGFI-GPNGAGKSTTIKMLTGIL-VptSGEVRVLGYVPFK-RRKEFARRIGVVFGQRSQLWWDLPAIDSFRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 sqkHASPYFTPEV-----LDQaLAD-LDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQ 408
Cdd:COG4586 120 ---LKAIYRIPDAeykkrLDE-LVElLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIRE 195
|
170
....*....|....*...
gi 489717269 409 LLQKCQEKSGQTILLISH 426
Cdd:COG4586 196 FLKEYNRERGTTILLTSH 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
253-444 |
1.44e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMT-KLLDYQGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAITVKEE 331
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 332 LALSQKHASPYFTPEVLDQaLADL--DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQL 409
Cdd:PRK11614 101 LAMGGFFAERDQFQERIKW-VYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDT 179
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 410 LQKCQEKsGQTILLISHHfygistwCDYHLRLAGR 444
Cdd:PRK11614 180 IEQLREQ-GMTIFLVEQN-------ANQALKLADR 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
216-428 |
1.49e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 216 QALLLATEPIGLHFPLPENEPAAFVMKN--FA--IKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD--Y 289
Cdd:PLN03130 592 EELLLAEERVLLPNPPLEPGLPAISIKNgyFSwdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPprS 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 290 QGSLTWEGKeVAklkertYFQHVAQIFqNAsdqfmaiTVKEELALsqkhASPyFTPEVLDQAL------ADLDLADHMDQ 363
Cdd:PLN03130 672 DASVVIRGT-VA------YVPQVSWIF-NA-------TVRDNILF----GSP-FDPERYERAIdvtalqHDLDLLPGGDL 731
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489717269 364 VV-----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVvqlLQKC--QEKSGQTILLISH--HF 428
Cdd:PLN03130 732 TEigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV---FDKCikDELRGKTRVLVTNqlHF 802
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
230-448 |
1.69e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 230 PLPENEPAAFVMKNFAIKQGRP--LLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAklkert 307
Cdd:PTZ00243 651 PTSERSAKTPKMKTDDFFELEPkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIA------ 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 308 YFQHVAQIfqnasdqfMAITVKEELAlsqkhaspYFTPEvlDQA-LADL--------DLAD-------HMDQVVYSLSGG 371
Cdd:PTZ00243 725 YVPQQAWI--------MNATVRGNIL--------FFDEE--DAArLADAvrvsqleaDLAQlgggletEIGEKGVNLSGG 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 372 QKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLqKCQEKSGQTILLISHHFYgISTWCDYHLRLAGRELAF 448
Cdd:PTZ00243 787 QKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC-FLGALAGKTRVLATHQVH-VVPRADYVVALGDGRVEF 861
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
242-436 |
1.71e-09 |
|
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: 57.76 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 242 KNFAIKQGRPL-LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKertyFQHVAQI-FQN 318
Cdd:cd03266 9 KRFRDVKKTVQaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGFATVDGFDVVKEP----AEARRRLgFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 ASDQFMA-ITVKEELAlsqkhaspYF------TPEVLDQALADL----DLADHMDQVVYSLSGGQKKKLEILLMLLSGQE 387
Cdd:cd03266 85 DSTGLYDrLTARENLE--------YFaglyglKGDELTARLEELadrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489717269 388 VLLIDEPLSGLDQKSIEQVVQLLQKcQEKSGQTILLISHHFYGISTWCD 436
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCD 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-188 |
2.61e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.45 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSL-GGRS----QAM---M 76
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSlsqqKGLirqL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 FQEAG---EQFTMATPREeiifAMENL--------GKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLV 145
Cdd:PRK11264 84 RQHVGfvfQNFNLFPHRT----VLENIiegpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 146 AMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTH 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-188 |
2.64e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 6 TIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYpkYGGQLTSGQVSLGGRSQAMMFQEAG--EQ 83
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI--QGNNFTGTILANNRKPTKQILKRTGfvTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 84 ----FTMATPREEIIF-AMENLGKSKTEFADRLKLASEFAEI------DSLLDQK-IVTMSGGEKQRVALAVLVAMDVDL 151
Cdd:PLN03211 148 ddilYPHLTVRETLVFcSLLRLPKSLTKQEKILVAESVISELgltkceNTIIGNSfIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190
....*....|....*....|....*....|....*..
gi 489717269 152 FLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
253-426 |
3.24e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLfkaMTKL--LDYQGSLTWE--GKEVAKLK-------ERTYFQHVAQIFQNASD 321
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTL---MNILgcLDKPTSGTYRvaGQDVATLDadalaqlRREHFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 322 QFMA--ITVKEELALSQKHASPYFTPEVLDQaladLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:PRK10535 101 LTAAqnVEVPAVYAGLERKQRLLRAQELLQR----LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180
....*....|....*....|....*..
gi 489717269 400 QKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:PRK10535 177 SHSGEEVMAILHQLRDR-GHTVIIVTH 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-189 |
3.54e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYG---DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggQLTSGQVSLGGrsqAMMFQEAG 81
Cdd:PLN03232 615 ISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS----HAETSSVVIRG---SVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 82 EQFTMATPREEIIFAmenlgkSKTEfADRLKLASEFAEIDSLLD-----------QKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:PLN03232 688 SWIFNATVRENILFG------SDFE-SERYWRAIDVTALQHDLDllpgrdlteigERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQGKT-IIITDHL 189
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFDSCMKDELKGKTrVLVTNQL 800
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-188 |
3.55e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 56.88 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTL----------LKIMAGLYP---KYGGQLTSGQV-SLGGRSQAMMFQEageQFT 85
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAyarQFLGQMDKPDVdSIEGLSPAIAIDQ---KTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 86 MATPREEIifamenlgKSKTEFADRLKLAseFAEI------DSL---------LDQKIVTMSGGEKQRVALAVLVAMDVD 150
Cdd:cd03270 88 SRNPRSTV--------GTVTEIYDYLRLL--FARVgirerlGFLvdvglgyltLSRSAPTLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 151 --LFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03270 158 gvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-188 |
3.56e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSY----GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLypkygGQLTSGQVSLGGRSQAMM 76
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCL-----DKPTSGTYRVAGQDVATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 FQEAgeqftMATPREE---IIF----------AMENL-------GKSKTEfadRLKLASEFAE---IDSLLDQKIVTMSG 133
Cdd:PRK10535 76 DADA-----LAQLRREhfgFIFqryhllshltAAQNVevpavyaGLERKQ---RLLRAQELLQrlgLEDRVEYQPSQLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 134 GEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
241-447 |
3.99e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 241 MKNFAIKQGRPLLEQ------KELSIPKGKVTLITGPNGSGKSSLFKAMT-KLLDYQGSLTWEGKEVAKLKERTYFQHVA 313
Cdd:PRK10938 1 MSSLQISQGTFRLSDtktlqlPSLTLNAGDSWAFVGANGSGKSALARALAgELPLLSGERQSQFSHITRLSFEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 314 QIFQ-NASDQFMA------ITVKEELALSQKHaspyftPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQ 386
Cdd:PRK10938 81 DEWQrNNTDMLSPgeddtgRTTAEIIQDEVKD------PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 387 EVLLIDEPLSGLDQKSIEQVVQLLQKCQeKSGQTILLISHHFYGISTWCDYHLRLAGRELA 447
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
251-448 |
4.83e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSI----PKGKVTL---------------ITGPNGSGKSSLFKAMTKLL----DYQGSLTWEGKEVAKLKE-- 305
Cdd:PRK09473 11 ALLDVKDLRVtfstPDGDVTAvndlnfslragetlgIVGESGSGKSQTAFALMGLLaangRIGGSATFNGREILNLPEke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 306 --RTYFQHVAQIFQN----------ASDQFMaitvkEELALsQKHASpyfTPEVLDQALADLDLA------DHMDQVVYS 367
Cdd:PRK09473 91 lnKLRAEQISMIFQDpmtslnpymrVGEQLM-----EVLML-HKGMS---KAEAFEESVRMLDAVkmpearKRMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 368 LSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCDYHLRL-AGREL 446
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMyAGRTM 241
|
..
gi 489717269 447 AF 448
Cdd:PRK09473 242 EY 243
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
251-436 |
5.49e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.61 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSI----PKGKV--------TL-------ITGPNGSGKSSLFKAMTKLLDYQGSLT-----WEGKEVAKL--K 304
Cdd:COG4170 2 PLLDIRNLTIeidtPQGRVkavdrvslTLnegeirgLVGESGSGKSLIAKAICGITKDNWHVTadrfrWNGIDLLKLspR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 305 ERTYF--QHVAQIFQNAS----------DQFM----AITVK----EELALSQKHASpyftpevldQALADLDLADH---M 361
Cdd:COG4170 82 ERRKIigREIAMIFQEPSscldpsakigDQLIeaipSWTFKgkwwQRFKWRKKRAI---------ELLHRVGIKDHkdiM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 362 DQVVYSLSGGQKKKLEILlMLLSGQEVLLI-DEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCD 436
Cdd:COG4170 153 NSYPHELTEGECQKVMIA-MAIANQPRLLIaDEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWAD 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
262-426 |
6.07e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 262 KGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAKLKERTYFQH-----------------VAQIFQNASDQFM 324
Cdd:PRK13631 51 KNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELItnpyskkiknfkelrrrVSMVFQFPEYQLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 AITVKEEL-----ALSQ------KHASPYFTPEVLDQaladldlaDHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDE 393
Cdd:PRK13631 131 KDTIEKDImfgpvALGVkkseakKLAKFYLNKMGLDD--------SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 394 PLSGLDQKSIEQVVQLLqKCQEKSGQTILLISH 426
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLI-LDAKANNKTVFVITH 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
243-426 |
6.27e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 243 NFAIKQGRPLLEQK----------ELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE---RTY 308
Cdd:PRK15079 17 HFDIKDGKQWFWQPpktlkavdgvTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWLGKDLLGMKDdewRAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 309 FQHVAQIFQN--AS-DQFMAI--TVKEELALSQKHASpyfTPEVLDQALADLD----LADHMDQVVYSLSGGQKKKLEIL 379
Cdd:PRK15079 97 RSDIQMIFQDplASlNPRMTIgeIIAEPLRTYHPKLS---RQEVKDRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 380 LMLLSGQEVLLIDEPLSGLDQkSIE-QVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDV-SIQaQVVNLLQQLQREMGLSLIFIAH 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
258-426 |
6.79e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.40 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKERTyfQHVAQIFQNASdQFMAITVKEELALS- 335
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQtSGHIRFHGTDVSRLHARD--RKVGFVFQHYA-LFRHMTVFDNIAFGl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 336 ---QKHASPyfTPEVLDQALADL----DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQ 408
Cdd:PRK10851 100 tvlPRRERP--NAAAIKAKVTQLlemvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRR 177
|
170
....*....|....*...
gi 489717269 409 LLQKCQEKSGQTILLISH 426
Cdd:PRK10851 178 WLRQLHEELKFTSVFVTH 195
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-188 |
7.81e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.36 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLT-SGQVSLGGRSQAMMFQEAGeqftmatpREEIIFAME 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrNGEVSVIAISAGLSGQLTG--------IENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 99 NLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKE 178
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE 191
|
170
....*....|
gi 489717269 179 QGKTIIITDH 188
Cdd:PRK13546 192 QNKTIFFVSH 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-188 |
7.98e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAE--LTIDHLTFSYGDRE----VIRDLSLTL-PAGTFSLlIGPTGCGKSTLLKIMAGLypkygGQLTSGQVSLGGRSQ 73
Cdd:PRK10584 1 MPAEniVEVHHLKKSVGQGEhelsILTGVELVVkRGETIAL-IGESGSGKSTLLAILAGL-----DDGSSGEVSLVGQPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQEAGEQFT-----------MATPreeIIFAMENL-------GKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGE 135
Cdd:PRK10584 75 HQMDEEARAKLRakhvgfvfqsfMLIP---TLNALENVelpallrGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 136 KQRVALAVLVAMDVDLFLLDEPFASVDpaarRFLIGRLAKL-----KEQGKTIIITDH 188
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLD----RQTGDKIADLlfslnREHGTTLILVTH 205
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
259-426 |
9.69e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.67 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 259 SIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQG-----SLTWEGKEVAKLKERTYFQ----HVAQIFQNASDQF-----M 324
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaeKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPMTSLnpcytV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 AITVKEELALSQ---KHASPYFTPEVLDQaLADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:PRK11022 109 GFQIMEAIKVHQggnKKTRRQRAIDLLNQ-VGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT 187
|
170 180
....*....|....*....|....*
gi 489717269 402 SIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK11022 188 IQAQIIELLLELQQKENMALVLITH 212
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
13-189 |
1.10e-08 |
|
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: 55.35 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 13 SYGDREVIrDLSLTLPAGTFsLLIGPTGCGKSTLLKIMA-GLYpkyggqltsGQVSLGGRSQAM-MFQEAGEQFTmatpr 90
Cdd:cd03279 13 PFREEQVI-DFTGLDNNGLF-LICGPTGAGKSTILDAITyALY---------GKTPRYGRQENLrSVFAPGEDTA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 91 eEIIFAMENLGK----------SKTEFADRLKLASefAEIDSLLDQKIVTMSGGEKQRVALAVLVAMD----------VD 150
Cdd:cd03279 77 -EVSFTFQLGGKkyrversrglDYDQFTRIVLLPQ--GEFDRFLARPVSTLSGGETFLASLSLALALSevlqnrggarLE 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 489717269 151 LFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:cd03279 154 ALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHV 192
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
258-426 |
1.11e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.81 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLD------YQGSLTWEGKE-------VAKLkeRTYFQHVAQ--------IF 316
Cdd:COG1117 32 LDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgarVEGEILLDGEDiydpdvdVVEL--RRRVGMVFQkpnpfpksIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 317 QNasdqfMA-------ITVKEELAlsqkhaspyftpEVLDQAL--ADL--DLADHMDQVVYSLSGGQKKKL--------- 376
Cdd:COG1117 110 DN-----VAyglrlhgIKSKSELD------------EIVEESLrkAALwdEVKDRLKKSALGLSGGQQQRLciaralave 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489717269 377 -EILLMllsgqevlliDEPLSGLDQKSIEQVVQLLQkcQEKSGQTILLISH 426
Cdd:COG1117 173 pEVLLM----------DEPTSALDPISTAKIEELIL--ELKKDYTIVIVTH 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
248-447 |
1.14e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.38 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEV---AKLKeRTYFQHVAQiFQNASDQF 323
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVparARLA-RARIGVVPQ-FDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 maiTVKEELALSQKhaspYF------TPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSG 397
Cdd:PRK13536 130 ---TVRENLLVFGR----YFgmstreIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 398 LDQKS----IEQVVQLLQKcqeksGQTILLISHHFYGISTWCDyhlRL----AGRELA 447
Cdd:PRK13536 203 LDPHArhliWERLRSLLAR-----GKTILLTTHFMEEAERLCD---RLcvleAGRKIA 252
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-189 |
1.19e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSY---GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyggqLTSGQVSLGGR----SQ-AMM 76
Cdd:PLN03130 615 ISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP----RSDASVVIRGTvayvPQvSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 FQeageqftmATPREEIIFAmenlgkskTEF-ADRLKLASEFAEIDSLLD-----------QKIVTMSGGEKQRVALAVL 144
Cdd:PLN03130 691 FN--------ATVRDNILFG--------SPFdPERYERAIDVTALQHDLDllpggdlteigERGVNISGGQKQRVSMARA 754
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489717269 145 VAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKT-IIITDHL 189
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTrVLVTNQL 800
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-188 |
1.22e-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: 57.61 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 2 QAELTIDHLTFSY--GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqlTSGQVSLGGRS-QAMMFQ 78
Cdd:TIGR01271 1215 GGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS------TEGEIQIDGVSwNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 79 EAGEQFTMaTPREEIIFA---MENLGK----SKTEF---ADRLKLASEFAEIDSLLDQKIV----TMSGGEKQRVALAVL 144
Cdd:TIGR01271 1289 TWRKAFGV-IPQKVFIFSgtfRKNLDPyeqwSDEEIwkvAEEVGLKSVIEQFPDKLDFVLVdggyVLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 145 VAMDVDLFLLDEPFASVDPAARRfLIGRLAKLKEQGKTIIITDH 188
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQ-IIRKTLKQSFSNCTVILSEH 1410
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
251-399 |
1.55e-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: 57.26 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGkEVAKLKERTYFQHVaqifqnasdqfmaiTVK 329
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDkVEGHVHMKG-SVAYVPQQAWIQND--------------SLR 716
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 330 EELALSQKHASPYFTPEVLDQA-LADLDLADHMDQVV-----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD 399
Cdd:TIGR00957 717 ENILFGKALNEKYYQQVLEACAlLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
251-426 |
1.56e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.17 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGK---------------VTLITGPNGSGKSSLFKAMTKLLDYQ------GSLTWEGKEVAKLKERT-- 307
Cdd:PRK14239 4 PILQVSDLSVYYNKkkalnsvsldfypneITALIGPSGSGKSTLLRSINRMNDLNpevtitGSIVYNGHNIYSPRTDTvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 308 YFQHVAQIFQNASDQFMAI--TVKEELALSQKHASpyftpEVLDQAL------ADL--DLADHMDQVVYSLSGGQKKKLE 377
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyeNVVYGLRLKGIKDK-----QVLDEAVekslkgASIwdEVKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489717269 378 ILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsgQTILLISH 426
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTR 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-192 |
2.07e-08 |
|
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: 56.95 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 28 PAGTFSLLiGPTGCGKSTLLKIMAGlypkyGGQLTSGQVSLGGRSQAMMFQEAGE------QF----TMATPREEIIFAM 97
Cdd:TIGR01257 1964 PGECFGLL-GVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTNISDVHQnmgycpQFdaidDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 98 ENLGKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLK 177
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170
....*....|....*
gi 489717269 178 EQGKTIIITDHLFDD 192
Cdd:TIGR01257 2118 REGRAVVLTSHSMEE 2132
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
248-408 |
2.14e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 248 QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ---GSLTWEGKEVAKL--KERT------YFQHVAQIf 316
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKDLLELspEDRAgegifmAFQYPVEI- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 317 QNASDQFMaitvkeeLALSQKHASPYFTPEVLDQaladLDLADHMDQVVYSL---------------SGGQKKKLEILLM 381
Cdd:PRK09580 91 PGVSNQFF-------LQTALNAVRSYRGQEPLDR----FDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQM 159
|
170 180
....*....|....*....|....*..
gi 489717269 382 LLSGQEVLLIDEPLSGLDQKSIEQVVQ 408
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVAD 186
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
258-426 |
2.35e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLL-DYQGSLTWEGKEVAKLKERTYFQHVAQIFqnaSDQFMAitvkEELALSQ 336
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGKPVTAEQPEDYRKLFSAVF---TDFHLF----DQLLGPE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 337 KHASPyftPEVLDQALADLDLADHMDQV-----VYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD-QKSIEQVVQLL 410
Cdd:PRK10522 417 GKPAN---PALVEKWLERLKMAHKLELEdgrisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDpHFRREFYQVLL 493
|
170
....*....|....*.
gi 489717269 411 QKCQEKsGQTILLISH 426
Cdd:PRK10522 494 PLLQEM-GKTIFAISH 508
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-188 |
2.93e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlypKYGGQLTSGQVSLGGRSQA---------- 74
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG---REDYEVTGGTVEFKGKDLLelspedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 75 ---MMFQEAGE------QFTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEI-DSLLDQKI-VTMSGGEKQRVALAV 143
Cdd:PRK09580 79 gifMAFQYPVEipgvsnQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVnVGFSGGEKKRNDILQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-188 |
3.22e-08 |
|
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: 53.40 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 15 GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlyPKYGGqLTSGQVSLGGRSQAMMFQ-EAG--EQ----FTMA 87
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAG-VITGEILINGRPLDKNFQrSTGyvEQqdvhSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 88 TPREEIIFAMENLGksktefadrlklasefaeidslldqkivtMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARR 167
Cdd:cd03232 95 TVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180
....*....|....*....|.
gi 489717269 168 FLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIH 166
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-191 |
3.34e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.75 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTLLKimaglypkyggqltsgQVSLGgrsqammfqeageqFTMATPREeiifamen 99
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILD----------------AIGLA--------------LGGAQSAT-------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 100 lgKSKTEFADRLKLASEFAEIDSLLDQkivtMSGGEKQRVALAVLVA----MDVDLFLLDEPFASVDPAARRFLIGRLAK 175
Cdd:cd03227 53 --RRRSGVKAGCIVAAVSAELIFTRLQ----LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
170
....*....|....*.
gi 489717269 176 LKEQGKTIIITDHLFD 191
Cdd:cd03227 127 HLVKGAQVIVITHLPE 142
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-189 |
3.38e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 18 EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGG-------QLTSGQVSLggRSQA--MMFQEAGeqfTMAT 88
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGelliddhPLHFGDYSY--RSQRirMIFQDPS---TSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 89 PREEIIFAMENLGKSKTEFA--DRLKLASEFAEIDSLLDQKIV----TMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD 162
Cdd:PRK15112 102 PRQRISQILDFPLRLNTDLEpeQREKQIIETLRQVGLLPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180
....*....|....*....|....*....
gi 489717269 163 PAARRFLIGRLAKLKE-QGKTII-ITDHL 189
Cdd:PRK15112 182 MSMRSQLINLMLELQEkQGISYIyVTQHL 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-162 |
4.02e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.74 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAG-TFSLlIGPTGCGKSTLLKIMAGLYPKyggqlTSGQVSLGGR-----SQA----------MMFQ------- 78
Cdd:COG4608 36 GVSFDIRRGeTLGL-VGESGCGKSTLGRLLLRLEEP-----TSGEILFDGQditglSGRelrplrrrmqMVFQdpyasln 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 79 ----------EAGEQFTMATP---REEIIFAMENLGkSKTEFADRlkLASEFaeidslldqkivtmSGGEKQRVALAVLV 145
Cdd:COG4608 110 prmtvgdiiaEPLRIHGLASKaerRERVAELLELVG-LRPEHADR--YPHEF--------------SGGQRQRIGIARAL 172
|
170
....*....|....*..
gi 489717269 146 AMDVDLFLLDEPFASVD 162
Cdd:COG4608 173 ALNPKLIVCDEPVSALD 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-188 |
4.49e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 8 DHLTFSY-GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQ----------LTSGQVSLGGRSQAMM 76
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKiwfsghditrLKNREVPFLRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 FQEagEQFTM-ATPREEIIFAMENLGKSKTEFADRLKLASEFAeidSLLDQK---IVTMSGGEKQRVALAVLVAMDVDLF 152
Cdd:PRK10908 85 FQD--HHLLMdRTVYDNVAIPLIIAGASGDDIRRRVSAALDKV---GLLDKAknfPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 153 LLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
231-426 |
5.16e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 231 LPENEPAAFVMKNFAIKQGR---PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGS--------LTWEGKE 299
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmlLRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 300 VAKLKERTYFQ-------HVAQIFQNASDQFMAI-TVKEELALSQKHASPYFTPEVLDQALADLDLA------DHMDQVV 365
Cdd:PRK10261 87 VIELSEQSAAQmrhvrgaDMAMIFQEPMTSLNPVfTVGEQIAESIRLHQGASREEAMVEAKRMLDQVripeaqTILSRYP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 366 YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITH 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
249-426 |
5.23e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.84 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKLKerTYFQHVAQIFQNASdQFMAIT 327
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYA-LFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQKHaSPYFTPEVLDQALADLDLAdHMDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSI 403
Cdd:PRK11607 108 VEQNIAFGLKQ-DKLPKAEIASRVNEMLGLV-HMQEFAkrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180
....*....|....*....|....*..
gi 489717269 404 E----QVVQLLqkcqEKSGQTILLISH 426
Cdd:PRK11607 186 DrmqlEVVDIL----ERVGVTCVMVTH 208
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
13-190 |
5.38e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 53.09 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 13 SYGDREVIRdlsltLPAGTFsLLIGPTGCGKSTLLK-IMAGLY------PKYGGQL-----TSGQVSL-----GGRSQAM 75
Cdd:COG0419 12 SYRDTETID-----FDDGLN-LIVGPNGAGKSTILEaIRYALYgkarsrSKLRSDLinvgsEEASVELefehgGKRYRIE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 76 MFQEAGEQFTMATP--REEIIFAMENLGKSKtEFADRLK-----LASEFAEIDSLLDQK------------IVTMSGGEK 136
Cdd:COG0419 86 RRQGEFAEFLEAKPseRKEALKRLLGLEIYE-ELKERLKeleeaLESALEELAELQKLKqeilaqlsgldpIETLSGGER 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489717269 137 QRVALAVLVAMDVDlflldepFASVDPAARRFLIGRLAKLKeqgktiIITdHLF 190
Cdd:COG0419 165 LRLALADLLSLILD-------FGSLDEERLERLLDALEELA------IIT-HVI 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
258-442 |
5.89e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQgsltwEGKEVakLKERTYFQHVAQI------------FQNASdQFMA 325
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQ-----KGRIV--LNGRVLFDAEKGIclppekrrigyvFQDAR-LFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALSQKHASP-YFtpevlDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIE 404
Cdd:PRK11144 91 YKVRGNLRYGMAKSMVaQF-----DKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 489717269 405 QVVQLLQKCQEKSGQTILLISHHFYGIstwcdyhLRLA 442
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEI-------LRLA 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
250-426 |
6.47e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.72 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 250 RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLK---ERTYFQHVAQIFQNASDqfma 325
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVsEGDIRFHDIPLTKLQldsWRSRLAVVSQTPFLFSD---- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 iTVKEELALSQKHAspyfTPEVLDQA--LAD-----LDLADHMDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEP 394
Cdd:PRK10789 404 -TVANNIALGRPDA----TQQEIEHVarLASvhddiLRLPQGYDTEVgergVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 395 LSGLDQKSIEQVVQLLQkcQEKSGQTILLISH 426
Cdd:PRK10789 479 LSAVDGRTEHQILHNLR--QWGEGRTVIISAH 508
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
249-426 |
6.64e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKLKERT---YFQHVAQIFQNaSDQFM 324
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQD-HHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 325 AITVKEELA--LSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:PRK10908 93 DRTVYDNVAipLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180
....*....|....*....|....
gi 489717269 403 IEQVVQLLQKCQeKSGQTILLISH 426
Cdd:PRK10908 173 SEGILRLFEEFN-RVGVTVLMATH 195
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
237-426 |
6.98e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.22 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 237 AAFVMKNFaIKQ--GRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL--------------LDYQGSLTWEGKEV 300
Cdd:PRK11264 2 SAIEVKNL-VKKfhGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeqpeagtirvgditIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 301 AKLKertyfQHVAQIFQNAsDQFMAITVKE---ELALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLE 377
Cdd:PRK11264 81 RQLR-----QHVGFVFQNF-NLFPHRTVLEniiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 378 ILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLL-QKCQEKsgQTILLISH 426
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIrQLAQEK--RTMVIVTH 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
265-427 |
7.20e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.61 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 265 VTLITGPNGSGKSSLFKAM-----------TKLLDYQGSLTWEGKEVAKLKERtyfqhvaqiFQNASDQFMAITVKeela 333
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkyaltgelppnSKGGAHDPKLIREGEVRAQVKLA---------FENANGKKYTITRS---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 334 lsqkhaspyftPEVLDQAL----ADLD--LADHMDQvvysLSGGQKKKLEILL-----MLLSGQ-EVLLIDEPLSGLDQK 401
Cdd:cd03240 91 -----------LAILENVIfchqGESNwpLLDMRGR----CSGGEKVLASLIIrlalaETFGSNcGILALDEPTTNLDEE 155
|
170 180
....*....|....*....|....*..
gi 489717269 402 SIE-QVVQLLQKCQEKSGQTILLISHH 427
Cdd:cd03240 156 NIEeSLAEIIEERKSQKNFQLIVITHD 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
258-427 |
8.00e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.25 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLldYQ---GSLTWEGKEVAklkertyFQHVAQ--------IFQNASdQFMAI 326
Cdd:COG1129 25 LELRPGEVHALLGENGAGKSTLMKILSGV--YQpdsGEILLDGEPVR-------FRSPRDaqaagiaiIHQELN-LVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQKHASPYFtpevLD---------QALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSG 397
Cdd:COG1129 95 SVAENIFLGREPRRGGL----IDwramrrrarELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190
....*....|....*....|....*....|
gi 489717269 398 LDQKSIEQVVQLLQKCQEKsGQTILLISHH 427
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQ-GVAIIYISHR 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
251-426 |
8.72e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTK--LLDyQGSLTWEGK-EVAKLK-------ERTYFQHVAQIFQNAS 320
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevLLD-DGRIIYEQDlIVARLQqdpprnvEGTVYDFVAEGIEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 321 D---QFMAITVKEELALSQKHASPYFT-PEVLD------------QALADLDLadHMDQVVYSLSGGQKKKLEILLMLLS 384
Cdd:PRK11147 96 EylkRYHDISHLVETDPSEKNLNELAKlQEQLDhhnlwqlenrinEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 385 GQEVLLIDEPLSGLDQKSIEQVVQLLqkcqeKSGQ-TILLISH 426
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFL-----KTFQgSIIFISH 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-192 |
8.79e-08 |
|
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: 52.26 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 17 REVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGqlTSGQVSLGGrsqaMMFQEAGEQFtmatpREEIIFA 96
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS--VEGDIHYNG----IPYKEFAEKY-----PGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 97 MENLGKSKT-------EFADRLKlasefaeidslLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPA-ARRF 168
Cdd:cd03233 89 SEEDVHFPTltvretlDFALRCK-----------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSStALEI 157
|
170 180 190
....*....|....*....|....*....|..
gi 489717269 169 LIGRLAKLKEQGKTIIIT--------DHLFDD 192
Cdd:cd03233 158 LKCIRTMADVLKTTTFVSlyqasdeiYDLFDK 189
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-169 |
1.02e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPKYGGQLTSGQVSLGGRSQammfqeagEQ 83
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGIKLGYFAQ--------HQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 84 FTMATPREEIIFAMENLGKSKTEFADRLKLASEFAEIDSLLDQKiVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDP 163
Cdd:PRK10636 385 LEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEET-RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
....*.
gi 489717269 164 AARRFL 169
Cdd:PRK10636 464 DMRQAL 469
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
257-426 |
1.04e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.57 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 257 ELSIPKGK-VTLItGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAK--LKERTyfqhVAQIFQN-ASDQFMAITVKEE 331
Cdd:PRK11432 26 NLTIKQGTmVTLL-GPSGCGKTTVLRLVAGLEKpTEGQIFIDGEDVTHrsIQQRD----ICMVFQSyALFPHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 332 LALSQKHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD---QKSIEQVVQ 408
Cdd:PRK11432 101 YGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDanlRRSMREKIR 180
|
170
....*....|....*...
gi 489717269 409 LLQKcqeKSGQTILLISH 426
Cdd:PRK11432 181 ELQQ---QFNITSLYVTH 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
240-426 |
1.07e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.76 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFAikqGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKLKERTYFqhvaqIFQN 318
Cdd:PRK11247 18 VSKRYG---ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAPLAEAREDTRL-----MFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 ASdQFMAITVKEELALSQKHAspyFTPEVLdQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:PRK11247 90 AR-LLPWKKVIDNVGLGLKGQ---WRDAAL-QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180
....*....|....*....|....*...
gi 489717269 399 DQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-188 |
1.11e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 35 LIGPTGCGKSTLLKIMAG-LYPkyggqlTSGQVS------LGGRSQAmmfQEAGEQFTMAtprEEIIFAMENLGKSKTEf 107
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGdLEP------SAGNVSldpnerLGKLRQD---QFAFEEFTVL---DTVIMGHTELWEVKQE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 108 ADRL---------------KLASEFAEID---------SLL-------DQKIVTMSG---GEKQRVALAVLVAMDVDLFL 153
Cdd:PRK15064 99 RDRIyalpemseedgmkvaDLEVKFAEMDgytaearagELLlgvgipeEQHYGLMSEvapGWKLRVLLAQALFSNPDILL 178
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 154 LDEPFASVDPAARRFLIGrlaKLKEQGKTIIITDH 188
Cdd:PRK15064 179 LDEPTNNLDINTIRWLED---VLNERNSTMIIISH 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
252-426 |
1.19e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.66 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 252 LLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE----------------RTYFQHVAQ 314
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNGQTINLVRDkdgqlkvadknqlrllRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 315 IFQNASDQFMAITVKEE----LALSQKHASpyftpevlDQALADLDLA--DHMDQVVY--SLSGGQKKKLEILLMLLSGQ 386
Cdd:PRK10619 100 HFNLWSHMTVLENVMEApiqvLGLSKQEAR--------ERAVKYLAKVgiDERAQGKYpvHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 387 EVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTH 210
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
258-437 |
1.31e-07 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 52.62 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSL-----FKAMTKLLDYQGSLTWEGKEVAKLKE--------------------RTY---F 309
Cdd:cd03271 16 VDIPLGVLTCVTGVSGSGKSSLindtlYPALARRLHLKKEQPGNHDRIEGLEHidkvividqspigrtprsnpATYtgvF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 310 QHVAQIF------QNASDQFMAITVK-----EELALSQKHASPYFT--PEVLD--QALADLDLAD-HMDQVVYSLSGG-- 371
Cdd:cd03271 96 DEIRELFcevckgKRYNRETLEVRYKgksiaDVLDMTVEEALEFFEniPKIARklQTLCDVGLGYiKLGQPATTLSGGea 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 372 QKKKL-EILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISHHFYGISTwCDY 437
Cdd:cd03271 176 QRIKLaKELSKRSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDVIKC-ADW 240
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
244-426 |
1.34e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.95 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 244 FAIKQGRPLLEQKELSIP-KGKVTLItGPNGSGKSSLfkaMTKLLDY----QGSLTWEGKEVAKLKERTYFQHVAQIFQN 318
Cdd:PRK10790 348 FAYRDDNLVLQNINLSVPsRGFVALV-GHTGSGKSTL---ASLLMGYypltEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 A---SDQFMA-ITVKEELalsqkhaspyfTPEVLDQALADLDLAD---HMDQVVYS--------LSGGQKKKLEILLMLL 383
Cdd:PRK10790 424 PvvlADTFLAnVTLGRDI-----------SEEQVWQALETVQLAElarSLPDGLYTplgeqgnnLSVGQKQLLALARVLV 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 384 SGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSgqTILLISH 426
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAH 533
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
258-393 |
1.41e-07 |
|
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: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLldY---QGSLTWEGKEVAKLKERTYFQHVAQIFqnaSDQFMAitvkEELAL 334
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGL--YrpeSGEILLDGQPVTADNREAYRQLFSAVF---SDFHLF----DRLLG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489717269 335 SQKHASpyftPEVLDQALADLDLAD--HMDQVVYS---LSGGQKKKLEILLMLLSGQEVLLIDE 393
Cdd:COG4615 424 LDGEAD----PARARELLERLELDHkvSVEDGRFSttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
257-433 |
1.55e-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: 51.17 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 257 ELSIPKGKVTLITGPNGSGKSSLFKAMTKlldyqgsltwEGKEVAKLKERTYFQHVAQIFqnaSDQFMAITvkeELALSq 336
Cdd:cd03238 15 DVSIPLNVLVVVTGVSGSGKSTLVNEGLY----------ASGKARLISFLPKFSRNKLIF---IDQLQFLI---DVGLG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 337 khaspYFTpevLDQALAdldladhmdqvvySLSGGQKKKLEILLMLLSGQE--VLLIDEPLSGLDQKSIEQVVQLLQKCQ 414
Cdd:cd03238 78 -----YLT---LGQKLS-------------TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLI 136
|
170
....*....|....*....
gi 489717269 415 EKsGQTILLISHHFYGIST 433
Cdd:cd03238 137 DL-GNTVILIEHNLDVLSS 154
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
253-436 |
1.64e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKllDYQ---GSLTWEGKEVAklkertyfqhvaqiFQNASDQFMA---- 325
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG--NYQpdaGSILIDGQEMR--------------FASTTAALAAgvai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ----------ITVKEELALSQ---------KHASPYFTPEVLDQALADLDladhMDQVVYSLSGGQKKKLEILLMLLSGQ 386
Cdd:PRK11288 84 iyqelhlvpeMTVAENLYLGQlphkggivnRRLLNYEAREQLEHLGVDID----PDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 387 EVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISHHFYGISTWCD 436
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCD 208
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
238-426 |
1.68e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.82 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 238 AFVMKNFaikqgRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAklkeRTYFqhVAQIfq 317
Cdd:cd03227 1 KIVLGRF-----PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVK----AGCI--VAAV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 nasdqfmaitvkeelalsqkHASPYFTpevLDQaladldladhmdqvvysLSGGQKKKLEiLLMLLSGQEV-----LLID 392
Cdd:cd03227 68 --------------------SAELIFT---RLQ-----------------LSGGEKELSA-LALILALASLkprplYILD 106
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 393 EPLSGLDQKSIEQVVQLLQKcQEKSGQTILLISH 426
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILE-HLVKGAQVIVITH 139
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
243-423 |
1.71e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 243 NFAIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMT-KL---LDYQGSLTWEGKevaKLKERTYFQHVAQIFQN 318
Cdd:PLN03140 171 NLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAgKLdpsLKVSGEITYNGY---RLNEFVPRKTSAYISQN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 319 asDQFMAI-TVKE-------------------ELALSQKHASPYFTPEV-----------------LDQALADLDL---A 358
Cdd:PLN03140 248 --DVHVGVmTVKEtldfsarcqgvgtrydllsELARREKDAGIFPEAEVdlfmkatamegvkssliTDYTLKILGLdicK 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 359 DHM--DQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILL 423
Cdd:PLN03140 326 DTIvgDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM 392
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-188 |
1.82e-07 |
|
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: 52.16 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSY--GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqlTSGQVSLGGRS-QAMMFQEA 80
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN------TEGDIQIDGVSwNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 GEQFTMaTPREEIIFA---MENL---GKSKTE----FADRLKLASEFAEIDSLLDQKIV----TMSGGEKQRVALAVLVA 146
Cdd:cd03289 76 RKAFGV-IPQKVFIFSgtfRKNLdpyGKWSDEeiwkVAEEVGLKSVIEQFPGQLDFVLVdggcVLSHGHKQLMCLARSVL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 147 MDVDLFLLDEPFASVDPAARRfLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQ-VIRKTLKQAFADCTVILSEH 195
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
258-416 |
1.87e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.95 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLL--DyQGSLTWEGKEVAKLK--ER-----TYfqhVAQ---IFQNAS--DQF 323
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVkpD-SGRIFLDGEDITHLPmhKRarlgiGY---LPQeasIFRKLTveDNI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 324 MAITvkEELALSQKHASpyftpEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSI 403
Cdd:COG1137 100 LAVL--ELRKLSKKERE-----ERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAV 172
|
170
....*....|...
gi 489717269 404 EQVVQLLQKCQEK 416
Cdd:COG1137 173 ADIQKIIRHLKER 185
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
241-428 |
2.32e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 51.16 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 241 MKNFaikqgRPLLEQKELSIPKGkVTLITGPNGSGKSSLFKAMTKLL--------DYQGSLTWEGKEVA------KLKER 306
Cdd:COG0419 7 LENF-----RSYRDTETIDFDDG-LNLIVGPNGAGKSTILEAIRYALygkarsrsKLRSDLINVGSEEAsvelefEHGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 307 TY----FQHVAQIFQNASDQFMAITVKEELALS-----QKHASPYFtpEVLDQALADLDLADHMDQV----------VYS 367
Cdd:COG0419 81 RYrierRQGEFAEFLEAKPSERKEALKRLLGLEiyeelKERLKELE--EALESALEELAELQKLKQEilaqlsgldpIET 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 368 LSGGQKKKLEILLMLlsgqeVLLIDepLSGLDQKSIEQVVQLLQKcqeksgqtILLISHHF 428
Cdd:COG0419 159 LSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEE--------LAIITHVI 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
4-188 |
2.42e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSY--GDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY------------PKYGGQLTSGQVSLG 69
Cdd:PRK10789 313 ELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFdvsegdirfhdiPLTKLQLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 70 GRSQA-MMFQEageqfTMATpreEIIFAMENLGKSKTEFADRLklASEFAEI-------DSLLDQKIVTMSGGEKQRVAL 141
Cdd:PRK10789 393 VVSQTpFLFSD-----TVAN---NIALGRPDATQQEIEHVARL--ASVHDDIlrlpqgyDTEVGERGVMLSGGQKQRISI 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 142 AVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKeQGKTIIITDH 188
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAH 508
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-157 |
2.48e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPKYGGQLTSGQVSLGgrsqaMMFQEAGEQ 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGeLEPDSGTVKWSENANIG-----YYAQDHAYD 394
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 84 FtmatprEEIIFAMENLGKSKTEFADRLKLASE-----FAEIDslLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEP 157
Cdd:PRK15064 395 F------ENDLTLFDWMSQWRQEGDDEQAVRGTlgrllFSQDD--IKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-188 |
2.55e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDRE---VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY-----------PKYGGQLTSGQV 66
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkNEHTNDMTNEQD 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 67 SLGGRSQAM---------------------MFQEAGE------------------QFTMATpREEIIFAM---ENL--GK 102
Cdd:PTZ00265 1242 YQGDEEQNVgmknvnefsltkeggsgedstVFKNSGKilldgvdicdynlkdlrnLFSIVS-QEPMLFNMsiyENIkfGK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 103 SKTEFADrLKLASEFAEIDSLL-------DQKI----VTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIG 171
Cdd:PTZ00265 1321 EDATRED-VKRACKFAAIDEFIeslpnkyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250
....*....|....*...
gi 489717269 172 RLAKLKEQG-KTIIITDH 188
Cdd:PTZ00265 1400 TIVDIKDKAdKTIITIAH 1417
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
253-426 |
2.85e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.34 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE----RTYFQHVAQIFQNASdQFMAIT 327
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDaelrEVRRKKIAMVFQSFA-LMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 VKEELALSQKHA---SPYFTPEVLDqALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIE 404
Cdd:PRK10070 123 VLDNTAFGMELAginAEERREKALD-ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180
....*....|....*....|..
gi 489717269 405 QVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISH 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
242-426 |
3.73e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 51.69 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 242 KNFAikqGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVA---KLKERtyfqHVAQIFQ 317
Cdd:COG1118 10 KRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpDSGRIVLNGRDLFtnlPPRER----RVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 NAsDQF--MaiTVKEELA--LSQKHASPyftPEVLDQALADLDL--ADHM-----DQvvysLSGGQKKKLEILLMLLSGQ 386
Cdd:COG1118 83 HY-ALFphM--TVAENIAfgLRVRPPSK---AEIRARVEELLELvqLEGLadrypSQ----LSGGQRQRVALARALAVEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 387 EVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTH 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
239-429 |
4.27e-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: 52.24 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 239 FVMKNF--AIKQGRPLLEQKELS-IPKGKVTLItGPNGSGKSSLFKAMTKL-LDYQG-SLTWEGKEVAKLK-------ER 306
Cdd:TIGR03719 5 YTMNRVskVVPPKKEILKDISLSfFPGAKIGVL-GLNGAGKSTLLRIMAGVdKDFNGeARPQPGIKVGYLPqepqldpTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 307 TYFQHV---AQIFQNASDQFMAITVK------EELALSQKHASpyfTPEVLDQALA-DLDL-----ADHM-----DQVVY 366
Cdd:TIGR03719 84 TVRENVeegVAEIKDALDRFNEISAKyaepdaDFDKLAAEQAE---LQEIIDAADAwDLDSqleiaMDALrcppwDADVT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489717269 367 SLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLqkcQEKSGqTILLISHHFY 429
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL---QEYPG-TVVAVTHDRY 219
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-202 |
4.44e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.30 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 34 LLIGPTGCGKSTLLKIMaglypKYGgqlTSGQVSLGGRSQAMMfqeageqftmatprEEIIFAMENLGKSKTEFADR--- 110
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL-----KYA---LTGELPPNSKGGAHD--------------PKLIREGEVRAQVKLAFENAngk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 111 -LKLASEFA-----------EIDSLLDQKIVTMSGGEKQ------RVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGR 172
Cdd:cd03240 84 kYTITRSLAilenvifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAE 163
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 173 LAKLKEQGKT---IIITDHlfDDYQGKVDGVYR 202
Cdd:cd03240 164 IIEERKSQKNfqlIVITHD--EELVDAADHIYR 194
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
356-436 |
4.85e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 356 DLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWC 435
Cdd:PRK15093 147 DHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWA 226
|
.
gi 489717269 436 D 436
Cdd:PRK15093 227 D 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
250-446 |
5.65e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 250 RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAM-TKLLDYQGSLTWEGKEVAKLKERTYFQ---HVAQIFQNASdQFMA 325
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIgGQIAPDHGEILFDGENIPAMSRSRLYTvrkRMSMLFQSGA-LFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALS-QKHASpyfTPEVLDQALADLDL--------ADHMDQvvySLSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:PRK11831 99 MNVFDNVAYPlREHTQ---LPAPLLHSTVMMKLeavglrgaAKLMPS---ELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489717269 397 GLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGISTWCDYHLRLAGREL 446
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
233-426 |
5.91e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 233 ENEPAAFVMKNFAIKQG-----RPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDyQGSLTWEGKEVAKLKERT 307
Cdd:TIGR00956 754 ESGEDIFHWRNLTYEVKikkekRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT-TGVITGGDRLVNGRPLDS 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 308 YFQHVAQIFQNASDQFMAITVKEELALSQ-----KHASPYFTPEVLDQALADLDLADHMDQVV----YSLSGGQKKKLEI 378
Cdd:TIGR00956 833 SFQRSIGYVQQQDLHLPTSTVRESLRFSAylrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTI 912
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489717269 379 LLMLLSGQEVLL-IDEPLSGLDQKSIEQVVQLLQKCQeKSGQTILLISH 426
Cdd:TIGR00956 913 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-197 |
5.93e-07 |
|
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: 48.91 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 34 LLIGPTGCGKSTLLKIMAGLYPKYGGQLtsgqvslggrsqammfqeageqftmatpreeIIFAMENLGKSKTEFADRLKL 113
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGV-------------------------------IYIDGEDILEEVLDQLLLIIV 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 114 ASEFAEIdslldqkivtmSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARR------FLIGRLAKLKEQGKTIIITD 187
Cdd:smart00382 55 GGKKASG-----------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEAllllleELRLLLLLKSEKNLTVILTT 123
|
170
....*....|
gi 489717269 188 HLFDDYQGKV 197
Cdd:smart00382 124 NDEKDLGPAL 133
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
263-427 |
6.73e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.80 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFKAMTKLLdyQGS------LTWEGKEVAKLKERTYFqhVAQifqnasDQFM--AITVKEELAL 334
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRI--QGNnftgtiLANNRKPTKQILKRTGF--VTQ------DDILypHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 SQ-----KHASPYFTPEVLDQALADLDLADHMDQVV-----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIE 404
Cdd:PLN03211 164 CSllrlpKSLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180
....*....|....*....|...
gi 489717269 405 QVVQLLQKCQEKsGQTILLISHH 427
Cdd:PLN03211 244 RLVLTLGSLAQK-GKTIVTSMHQ 265
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-188 |
6.89e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFsYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKyGGQLTSGQV----------SLGG 70
Cdd:PRK10418 1 MPQQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA-GVRQTAGRVlldgkpvapcALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 71 RSQAMMFQEAGEQF----TMATPREEIIFAmenLGKSKTEfaDRLKLASE---FAEIDSLLDQKIVTMSGGEKQRVALAV 143
Cdd:PRK10418 79 RKIATIMQNPRSAFnplhTMHTHARETCLA---LGKPADD--ATLTAALEavgLENAARVLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489717269 144 LVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL-KEQGKTIIITDH 188
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTH 199
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-162 |
8.25e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.81 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 18 EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGL-YPKYGGQLTSGQV--SLGGRSQAMMF-QEAG--EQFTMATPRe 91
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPmsKLSSAAKAELRnQKLGfiYQFHHLLPD- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 92 eiIFAMENL-------GKSKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVD 162
Cdd:PRK11629 102 --FTALENVamplligKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
258-426 |
8.41e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKL--KERTyfqhVAQIFQNASdQFMAITVKEELAL 334
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDItSGDLFIGEKRMNDVppAERG----VGMVFQSYA-LYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 SQKHASPYfTPEV---LDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLD-----QKSIEqv 406
Cdd:PRK11000 99 GLKLAGAK-KEEInqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvQMRIE-- 175
|
170 180
....*....|....*....|
gi 489717269 407 vqlLQKCQEKSGQTILLISH 426
Cdd:PRK11000 176 ---ISRLHKRLGRTMIYVTH 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
258-426 |
1.05e-06 |
|
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: 50.94 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPK-GKVTLITGPNGSGKSSLFKAMTKLL-----DYQGSLTWE-------GKEVaklkeRTYFQHVA----------Q 314
Cdd:COG1245 93 LPVPKkGKVTGILGPNGIGKSTALKILSGELkpnlgDYDEEPSWDevlkrfrGTEL-----QDYFKKLAngeikvahkpQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 315 IFQNASDQFMAiTVKEELALSQKHAspyftpeVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEP 394
Cdd:COG1245 168 YVDLIPKVFKG-TVRELLEKVDERG-------KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*
gi 489717269 395 LSGLDqksIEQ---VVQLLQKCQEKsGQTILLISH 426
Cdd:COG1245 240 SSYLD---IYQrlnVARLIRELAEE-GKYVLVVEH 270
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
252-441 |
1.35e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.39 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 252 LLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKE----RTYFQHVAQIFQNasdqFMAI 326
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQMDEearaKLRAKHVGFVFQS----FMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 TVKEELALSQ-----KHASPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:PRK10584 101 PTLNALENVElpallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 402 SIEQVVQLLQKCQEKSGQTILLISHHFYgISTWCDYHLRL 441
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHDLQ-LAARCDRRLRL 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-188 |
1.52e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 16 DR-EVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGlyPKYGGQLtSGQVSLGG--RSQAMMFQEAG--EQFTMATP- 89
Cdd:PLN03140 891 DRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI-EGDIRISGfpKKQETFARISGycEQNDIHSPq 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 90 ---REEIIF-AMENLGK--SKTE---FADRLklaSEFAEIDSLLDQ-----KIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:PLN03140 968 vtvRESLIYsAFLRLPKevSKEEkmmFVDEV---MELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
247-399 |
1.60e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL---------DYQGSLTWEGKEVAKLKERTYFQHVAQIFQ 317
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 NASDQFmAITVKEELALSQ-KHA-----SPYFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLML--------- 382
Cdd:PRK13547 91 AAQPAF-AFSAREIVLLGRyPHArragaLTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170
....*....|....*..
gi 489717269 383 LSGQEVLLIDEPLSGLD 399
Cdd:PRK13547 170 AQPPRYLLLDEPTAALD 186
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
239-427 |
1.65e-06 |
|
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: 48.97 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 239 FVMKNFAIKQgRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAM---------TKLLDYQGSLTwegkEVAKLKERTyf 309
Cdd:COG4778 14 FTLHLQGGKR-LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdsgSILVRHDGGWV----DLAQASPRE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 310 qhVAQIFQNA----SdQFM-------AITVKEELALSQKHAspyfTPEVLDQA---LADLDLADHMdqvvYSL-----SG 370
Cdd:COG4778 87 --ILALRRRTigyvS-QFLrviprvsALDVVAEPLLERGVD----REEARARArelLARLNLPERL----WDLppatfSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 371 GQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQeKSGQTILLISHH 427
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHD 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-198 |
1.75e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 35 LIGPTGCGKSTLLKIMAG-LYPKYGGQLTSGQVSLGGRSQAMMfqeAGEQFTmATPreeiIFAMENLGKSKTEFADRLKL 113
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGeLQPSSGTVFRSAKVRMAVFSQHHV---DGLDLS-SNP----LLYMMRCFPGVPEQKLRAHL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 114 ASeFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLkeQGKTIIIT--DHLFd 191
Cdd:PLN03073 612 GS-FGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF--QGGVLMVShdEHLI- 687
|
....*..
gi 489717269 192 dyQGKVD 198
Cdd:PLN03073 688 --SGSVD 692
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
236-426 |
1.90e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.42 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 236 PAAFVMKNFAIKQGRPLLEQKELSipKGKVTLITGPNGSGKSSLFKAMTKLLdyQGSLTWEGKEVAklkERTYFQHVAQI 315
Cdd:cd03279 3 PLKLELKNFGPFREEQVIDFTGLD--NNGLFLICGPTGAGKSTILDAITYAL--YGKTPRYGRQEN---LRSVFAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 316 ------FQNASDQFMAItvkEELALSQKHaspyFTPEVLdqaLADLDLADHMDQVVYSLSGGQKKKLEILLML-LSGQ-- 386
Cdd:cd03279 76 aevsftFQLGGKKYRVE---RSRGLDYDQ----FTRIVL---LPQGEFDRFLARPVSTLSGGETFLASLSLALaLSEVlq 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 387 -------EVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:cd03279 146 nrggarlEALFIDEGFGTLDPEALEAVATALELIRTE-NRMVGVISH 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
247-422 |
2.25e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.01 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 247 KQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD---YQGSLTWEGKEVAKLKERT--YFQHVAQIFQNAsd 321
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagvITGEILINGRPLDKNFQRStgYVEQQDVHSPNL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 322 qfmaiTVKEELALSqkhaspyftpevldqalADLDladhmdqvvySLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQK 401
Cdd:cd03232 95 -----TVREALRFS-----------------ALLR----------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|.
gi 489717269 402 SIEQVVQLLQKCQEkSGQTIL 422
Cdd:cd03232 143 AAYNIVRFLKKLAD-SGQAIL 162
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
265-426 |
2.67e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 265 VTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKER--TYFQHVAQIFqnasdqfMAITVKEELALSQKHasp 341
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQpSSGNIYYKNCNINNIAKPycTYIGHNLGLK-------LEMTVFENLKFWSEI--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 342 YFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLqKCQEKSGQTI 421
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMKANSGGIV 176
|
....*
gi 489717269 422 LLISH 426
Cdd:PRK13541 177 LLSSH 181
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
263-413 |
3.02e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFKAMTK-----LLDYQGSLTWEGKEVAKLKERtYFQHVAQIFQNaSDQFMAITVKEELALSQK 337
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASntdgfHIGVEGVITYDGITPEEIKKH-YRGDVVYNAET-DVHFPHLTVGETLDFAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 338 HASPYFTPEVLDQ-----ALADLDLA----DHM------DQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:TIGR00956 165 CKTPQNRPDGVSReeyakHIADVYMAtyglSHTrntkvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
170
....*....|.
gi 489717269 403 IEQVVQLLQKC 413
Cdd:TIGR00956 245 ALEFIRALKTS 255
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
258-447 |
3.02e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.65 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKlKERTYFQHVAQI--FQNASDQFmaiTVKEELAL 334
Cdd:PRK13537 28 FHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAGSISLCGEPVPS-RARHARQRVGVVpqFDNLDPDF---TVRENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 SQK------HASPYFTPEVLDQAladlDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS----IE 404
Cdd:PRK13537 104 FGRyfglsaAAARALVPPLLEFA----KLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhlmWE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 405 QVVQLLqkcqeKSGQTILLISHHFYGISTWCDYHLRL-AGRELA 447
Cdd:PRK13537 180 RLRSLL-----ARGKTILLTTHFMEEAERLCDRLCVIeEGRKIA 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
240-426 |
3.18e-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: 48.70 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFAIK---QGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEG---KEVAKLKERTYFQHVA 313
Cdd:cd03289 4 TVKDLTAKyteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGvswNSVPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 314 Q---IFQNA-----------SDQFMaITVKEELALSQkhaspyftpeVLDQALADLDLAdhMDQVVYSLSGGQKKKLEIL 379
Cdd:cd03289 84 QkvfIFSGTfrknldpygkwSDEEI-WKVAEEVGLKS----------VIEQFPGQLDFV--LVDGGCVLSHGHKQLMCLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489717269 380 LMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQkcQEKSGQTILLISH 426
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
251-426 |
3.50e-06 |
|
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: 49.63 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMT-KLLDYQGSLTWEGKEVaklkertyFQHVAQIFQNAS--DQFMAIt 327
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTgDTTVTSGDATVAGKSI--------LTNISDVHQNMGycPQFDAI- 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 328 vkEELALSQKHASPYF---------TPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:TIGR01257 2024 --DDLLTGREHLYLYArlrgvpaeeIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180
....*....|....*....|....*...
gi 489717269 399 DQKSIEQVVQLLQKCQeKSGQTILLISH 426
Cdd:TIGR01257 2102 DPQARRMLWNTIVSII-REGRAVVLTSH 2128
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-191 |
3.86e-06 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 20 IRDLSLTLPAGTFSLLIGPTGCGKSTLlkIMAGLYP-----KYGGQLTSGQV-----------------SLGGRSQ---- 73
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSL--INDTLYPalarrLHLKKEQPGNHdrieglehidkvividqSPIGRTPrsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 ---AMMFQE---------AGEQFTmatpRE--EIIFamenLGKSkteFADRLKL----ASEFAE--------IDSLLD-- 125
Cdd:cd03271 89 atyTGVFDEirelfcevcKGKRYN----REtlEVRY----KGKS---IADVLDMtveeALEFFEnipkiarkLQTLCDvg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 126 -------QKIVTMSGGEKQRVALAVLVAMDVD---LFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFD 191
Cdd:cd03271 158 lgyiklgQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD 233
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
260-435 |
4.56e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 260 IPKGKVTLITGPNGSGKSSLfkamTKLLdyqGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAITVKEELALSQKHA 339
Cdd:PRK13545 47 VPEGEIVGIIGLNGSGKSTL----SNLI---AGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 340 SPYFTPEVLDQAladlDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQ 419
Cdd:PRK13545 120 IKEIIPEIIEFA----DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GK 194
|
170
....*....|....*.
gi 489717269 420 TILLISHHFYGISTWC 435
Cdd:PRK13545 195 TIFFISHSLSQVKSFC 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
259-426 |
5.25e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 259 SIPKGKVTLITGPNGSGKSSLFKAMTkLLD--YQGSLTWEGKEVA---KLKERTYFQHVAQIFQN--AS---DQFMAITV 328
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLT-MIEtpTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNpyGSlnpRKKVGQIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 KEELALSQKHASPYFTPEVLdQALADLDL-ADHMDQVVYSLSGGQKKKLEIL--LMLlsGQEVLLIDEPLSGLDQkSIE- 404
Cdd:PRK11308 116 EEPLLINTSLSAAERREKAL-AMMAKVGLrPEHYDRYPHMFSGGQRQRIAIAraLML--DPDVVVADEPVSALDV-SVQa 191
|
170 180
....*....|....*....|..
gi 489717269 405 QVVQLLQKCQEKSGQTILLISH 426
Cdd:PRK11308 192 QVLNLMMDLQQELGLSYVFISH 213
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
74-279 |
5.31e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 AMMFQEAgEQFTMATPR-EEIIFAMENLGksktefadrlklasefaeIDSL-LDQKIVTMSGGEKQRVALAVLVAMDVD- 150
Cdd:PRK00635 770 EMTAYEA-EKFFLDEPSiHEKIHALCSLG------------------LDYLpLGRPLSSLSGGEIQRLKLAYELLAPSKk 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 151 --LFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHlfDDYQGKV-DGVYRFKGEQVDLltkdeQALLLAT----E 223
Cdd:PRK00635 831 ptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH--NMHVVKVaDYVLELGPEGGNL-----GGYLLAScspeE 903
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489717269 224 PIGLHFP-----------------LPENEPAAFVMKNFAIKQG-RPLLEQKELSIPKGKVTLITGPNGSGKSSL 279
Cdd:PRK00635 904 LIHLHTPtakalrpylsspqelpyLPDPSPKPPVPADITIKNAyQHNLKHIDLSLPRNALTAVTGPSASGKHSL 977
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
251-431 |
5.61e-06 |
|
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: 47.10 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 251 PLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNAsdQFMAITVK 329
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVElSSGSILIDGVDISKIGLHDLRSRISIIPQDP--VLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 330 EELALSQKHaspyfTPEVLDQALADLDLADHMDQVVYSL-----------SGGQKKKLEILLMLLSGQEVLLIDEPLSGL 398
Cdd:cd03244 96 SNLDPFGEY-----SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 399 DQKSIEQVVQLLQkcQEKSGQTILLISHHFYGI 431
Cdd:cd03244 171 DPETDALIQKTIR--EAFKDCTVLTIAHRLDTI 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
367-431 |
5.98e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 5.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489717269 367 SLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGI 431
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
129-206 |
7.40e-06 |
|
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: 46.41 E-value: 7.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 129 VTMSGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQG-KTIIITDHLFDDYQGKVDGVYRFKGE 206
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
255-287 |
9.62e-06 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.97 E-value: 9.62e-06
10 20 30
....*....|....*....|....*....|...
gi 489717269 255 QKELSIPKGKVTLITGPNGSGKSSLFKAMTKLL 287
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
240-426 |
9.70e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFAikqGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQH----VAQ 314
Cdd:PRK15439 17 ISKQYS---GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCARLTPAKAHQLgiylVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 315 ---IFQNasdqfmaITVKEELALS-QKHASPYftpEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLL 390
Cdd:PRK15439 94 eplLFPN-------LSVKENILFGlPKRQASM---QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 391 IDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISH 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
258-436 |
1.09e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTKLldYQ---GSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAITVKEELAL 334
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGI--YTrdaGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 335 SQKHASPYFT---PEVLDQA---LADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQ 408
Cdd:PRK10762 103 GREFVNRFGRidwKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFR 182
|
170 180
....*....|....*....|....*...
gi 489717269 409 LLQKCQEKsGQTILLISHHFYGISTWCD 436
Cdd:PRK10762 183 VIRELKSQ-GRGIVYISHRLKEIFEICD 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
268-427 |
1.27e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.71 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 268 ITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQHVAQIFQNASD-----QFMAITVKEELALSQKhASP 341
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTslnprQRISQILDFPLRLNTD-LEP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 342 YFTPEVLDQALADLDL-ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQT 420
Cdd:PRK15112 123 EQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIS 202
|
....*..
gi 489717269 421 ILLISHH 427
Cdd:PRK15112 203 YIYVTQH 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
268-437 |
1.68e-05 |
|
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: 45.48 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 268 ITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKERTYFQHVAQIFQNASdQFMAiTVKEELalsqkhaSPY--FT 344
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAeEGKIEIDGIDISTIPLEDLRSSLTIIPQDPT-LFSG-TIRSNL-------DPFdeYS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 345 PEVLDQALADLDLADhmdqvvySLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS---IEQVVQllqkcQEKSGQTI 421
Cdd:cd03369 110 DEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdalIQKTIR-----EEFTNSTI 177
|
170
....*....|....*.
gi 489717269 422 LLISHHfygISTWCDY 437
Cdd:cd03369 178 LTIAHR---LRTIIDY 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-162 |
2.76e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.69 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 1 MQAELTIDHLTFSYGDREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAG-LYPkyggqlTSGQVSLGGRSQAMM--- 76
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAP------DAGEVHYRMRDGQLRdly 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 77 -FQEAGEQFTMAT--------PRE-------------EIIFA--MENLGKSKTEFADRLklasEFAEID-SLLDQKIVTM 131
Cdd:PRK11701 77 aLSEAERRRLLRTewgfvhqhPRDglrmqvsaggnigERLMAvgARHYGDIRATAGDWL----ERVEIDaARIDDLPTTF 152
|
170 180 190
....*....|....*....|....*....|.
gi 489717269 132 SGGEKQRVALAVLVAMDVDLFLLDEPFASVD 162
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
252-444 |
3.03e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.19 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 252 LLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKL-LDYQGSLTWEGKEVAKLKERT-------------YFQHVAQIFQ 317
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAkaelrnqklgfiyQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 318 NASDQFMAITV-KEELALSQKHASpyftpevldQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLS 396
Cdd:PRK11629 104 ALENVAMPLLIgKKKPAEINSRAL---------EMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489717269 397 GLDQKSIEQVVQLLQKCQEKSGQTILLISHhfygistwcdyHLRLAGR 444
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTH-----------DLQLAKR 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
239-429 |
3.12e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 239 FVMKNF--AIKQGRPLLEQKELS-IPKGKVTLItGPNGSGKSSLFKAMTKL-LDYQGSLTW------------------- 295
Cdd:PRK11819 7 YTMNRVskVVPPKKQILKDISLSfFPGAKIGVL-GLNGAGKSTLLRIMAGVdKEFEGEARPapgikvgylpqepqldpek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 296 -------EG-KEVAKLKERtyFQHVAQIFQNASDQFMAiTVKEELALSQK--HASPYFTPEVLDQALADLDLADhMDQVV 365
Cdd:PRK11819 86 tvrenveEGvAEVKAALDR--FNEIYAAYAEPDADFDA-LAAEQGELQEIidAADAWDLDSQLEIAMDALRCPP-WDAKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489717269 366 YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLqkcQEKSGqTILLISHHFY 429
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL---HDYPG-TVVAVTHDRY 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-188 |
3.97e-05 |
|
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: 44.79 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 4 ELTIDHLTFSYGDRE--VIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkyggqLTSGQVSLGGRS-QAMMFQEA 80
Cdd:cd03244 2 DIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE-----LSSGSILIDGVDiSKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 81 GEQFTMaTPREEIIFA---MENLG----KSKTEFADRLKLASEFAEIDSLLDQ--KIVTMSG-----GEKQRVALAVLVA 146
Cdd:cd03244 77 RSRISI-IPQDPVLFSgtiRSNLDpfgeYSDEELWQALERVGLKEFVESLPGGldTVVEEGGenlsvGQRQLLCLARALL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489717269 147 MDVDLFLLDEPFASVDPAARRfLIGRLAKLKEQGKTIIITDH 188
Cdd:cd03244 156 RKSKILVLDEATASVDPETDA-LIQKTIREAFKDCTVLTIAH 196
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
249-425 |
4.45e-05 |
|
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: 43.96 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 249 GRPLLEQKELSIP-----------KGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGKEVAKLKERTYFQH-VAQI 315
Cdd:cd03215 1 GEPVLEVRGLSVKgavrdvsfevrAGEIVGIAGLVGNGQTELAEALFGLRPpASGEITLDGKPVTRRSPRDAIRAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 316 FQNASDQ--FMAITVKEELALSQkhaspyftpevldqaladldladhmdqvvySLSGG--QKkkleILL--MLLSGQEVL 389
Cdd:cd03215 81 PEDRKREglVLDLSVAENIALSS------------------------------LLSGGnqQK----VVLarWLARDPRVL 126
|
170 180 190
....*....|....*....|....*....|....*.
gi 489717269 390 LIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLIS 425
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLIS 161
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-188 |
5.84e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 30 GTFSLLIGPTGCGKSTLLKIMAGlyPKYGGQLTSGQVSLGGRSQAMMFQEAG---EQ----FTMATPREEIIFAM----- 97
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSFQRSIgyvQQqdlhLPTSTVRESLRFSAylrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 98 -ENLGKSKTEFADRLklaSEFAEIDSLLDqKIVTMSGG-----EKQRVALAV-LVAMDVDLFLLDEPFASVDPAARRFLI 170
Cdd:TIGR00956 867 kSVSKSEKMEYVEEV---IKLLEMESYAD-AVVGVPGEglnveQRKRLTIGVeLVAKPKLLLFLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*...
gi 489717269 171 GRLAKLKEQGKTIIITDH 188
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIH 960
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
253-436 |
9.50e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 253 LEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLDY-QGSLTWEGKEVAKLKERTYFQHVAQIFQNASDQFMAITVKEE 331
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKdSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 332 LALSQKHASPYF---------TPEVLDQALADLDLADHmdqvVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS 402
Cdd:PRK10982 94 MWLGRYPTKGMFvdqdkmyrdTKAIFDELDIDIDPRAK----VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 403 IEQVVQLLQKCQEKsGQTILLISHHFYGISTWCD 436
Cdd:PRK10982 170 VNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCD 202
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
366-426 |
1.10e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.92 E-value: 1.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489717269 366 YSLSGGQKKKLEILLMLLS---GQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQtILLISH 426
Cdd:pfam13304 235 FELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQ-LILTTH 297
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-185 |
1.13e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.94 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 9 HLTFSYGDREV--IRDLSLTLPAGTFSLLIGPTGCGKS-TLLKIMaGLYPKYGgqLTSGQVSLGGRS------------- 72
Cdd:PRK09473 19 RVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANG--RIGGSATFNGREilnlpekelnklr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 ---QAMMFQE----------AGEQFTmatpreEIIFAMENLGKSKTefadrlklaseFAEIDSLLD-------QKIVTM- 131
Cdd:PRK09473 96 aeqISMIFQDpmtslnpymrVGEQLM------EVLMLHKGMSKAEA-----------FEESVRMLDavkmpeaRKRMKMy 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489717269 132 ----SGGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIII 185
Cdd:PRK09473 159 phefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAII 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
263-426 |
1.14e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.57 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFKAMTKLLDYQ-GSLTWEGKEVAKLKERTYFQHVAQIFQNASdqFMAITVKEELALSQKHASP 341
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQsGRILIDGTDIRTVTRASLRRNIAVVFQDAG--LFNRSIEDNIRVGRPDATD 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 342 YFTPEVLDQALAdLDL----ADHMDQVV----YSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKC 413
Cdd:PRK13657 439 EEMRAAAERAQA-HDFierkPDGYDTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
170
....*....|...
gi 489717269 414 QEksGQTILLISH 426
Cdd:PRK13657 518 MK--GRTTFIIAH 528
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-54 |
1.43e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 1.43e-04
10 20 30
....*....|....*....|....*....|....*....
gi 489717269 16 DREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLY 54
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
131-188 |
1.45e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.53 E-value: 1.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489717269 131 MSGGEKQRVALAVLVAMDVD---LFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:pfam13304 237 LSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-287 |
1.53e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.53e-04
10 20
....*....|....*....|....*..
gi 489717269 261 PKGKVTLITGPNGSGKSSLFKAMTKLL 287
Cdd:COG4913 22 FDGRGTLLTGDNGSGKSTLLDAIQTLL 48
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
262-428 |
1.67e-04 |
|
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: 41.98 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 262 KGKVTLITGPNGSGKSSLFKAMTKLLDYQGsltwegkevaklkertyfqhvAQIFqnasdqfmaitvkeelalsqkhasp 341
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG---------------------GGVI------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 342 YFTPEVLDQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKS-----IEQVVQLLQKCQEK 416
Cdd:smart00382 35 YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQealllLLEELRLLLLLKSE 114
|
170
....*....|..
gi 489717269 417 SGQTILLISHHF 428
Cdd:smart00382 115 KNLTVILTTNDE 126
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
258-426 |
2.21e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLfkAMtklldyqGSLTWEGkevaklkERTYFQHVAqifqNASDQFMAITVKEE------ 331
Cdd:cd03270 16 VDIPRNKLVVITGVSGSGKSSL--AF-------DTIYAEG-------QRRYVESLS----AYARQFLGQMDKPDvdsieg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 332 ----LALSQKHAS--PYFT----PEVLD---------------QALADLDLaDH--MDQVVYSLSGGQKKKLEILLMLLS 384
Cdd:cd03270 76 lspaIAIDQKTTSrnPRSTvgtvTEIYDylrllfarvgirerlGFLVDVGL-GYltLSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489717269 385 G-QEVLLI-DEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:cd03270 155 GlTGVLYVlDEPSIGLHPRDNDRLIETLKRLRDL-GNTVLVVEH 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-201 |
2.41e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 5 LTIDHLTfsygdREVIRDLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPKYGGQLTSGQVSLGGRS------------ 72
Cdd:PRK15439 269 LTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlarglvyl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 73 -----QAMMFQEA-----------GEQ-FTMATPREEIIFAMEnlgksktefadRLKLASEFAEIDslldQKIVTMSGGE 135
Cdd:PRK15439 344 pedrqSSGLYLDAplawnvcalthNRRgFWIKPARENAVLERY-----------RRALNIKFNHAE----QAARTLSGGN 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 136 KQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDHLFDDYQGKVDGVY 201
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVL 474
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
258-279 |
2.53e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 2.53e-04
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-191 |
3.18e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 3.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 124 LDQKIVTMSGGEKQRVALAV-LVAMDV--DLFLLDEP-----FASVdpaarRFLIGRLAKLKEQGKTIIITDHLFD 191
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKeLSKRSTgrTLYILDEPttglhFDDI-----KKLLEVLQRLVDKGNTVVVIEHNLD 893
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-188 |
3.96e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 22 DLSLTLPAGTFSLLIGPTGCGKSTLLKIMAGLYPkYGGQltSGQVSLGGR---------SQAM----MFQEAG--EQFTM 86
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGSY--EGEILFDGEvcrfkdirdSEALgiviIHQELAliPYLSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 87 AtpreEIIFamenLG--KSKTEFADRLKLASEFAEidsLLDQ---------KIVTMSGGEKQRVALAVLVAMDVDLFLLD 155
Cdd:NF040905 96 A----ENIF----LGneRAKRGVIDWNETNRRARE---LLAKvgldespdtLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190
....*....|....*....|....*....|...
gi 489717269 156 EPFASVDPAARRFLIGRLAKLKEQGKTIIITDH 188
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
242-426 |
4.20e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.34 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 242 KNFAIKQGRPLLEQKELSIPK-----GKVTLITGPNGSGKSSLFKAMTKLLD---------------------------- 288
Cdd:COG1106 3 ISFSIENFRSFKDELTLSMVAsglrlLRVNLIYGANASGKSNLLEALYFLRNlvlnssqpgdklvepflldsesknepse 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 289 -----------YQGSLTWEGKEVakLKERTYF-----QHVAQIFQNASDQF---MAITVKEELALSQKHASPYFTPEVLD 349
Cdd:COG1106 83 feilflldgvrYEYGFELDKERI--ISEWLYFlstaaQLNVPLLSPLYDWFdnnISLDTSSDGLTLLLKEDESLKEELLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 350 -QALADLDLAD-------------------HMDQVVY----SLSGGQKKKLEILLML---LSGQEVLLIDEPLSGLDQKS 402
Cdd:COG1106 161 lLKIADPGIEDieveeeeiedlverklifkHKGGNVPlplsEESDGTKRLLALAGALldaLAKGGVLLIDEIEASLHPSL 240
|
250 260
....*....|....*....|....
gi 489717269 403 IEQVVQLLQKCQEKSGQTILLISH 426
Cdd:COG1106 241 LRKLLKLFLDLANKNNAQLIFTTH 264
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
284-426 |
5.05e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 284 TKLLDYQGSLTWEGKEVAKLKE---RTYFQHVAQIFQNA-SDQFMAITVKEELALSQKHASPYFTPEvldQALAdldlad 359
Cdd:PRK00635 405 TGLGDYANAATWHGKTFAEFQQmslQELFIFLSQLPSKSlSIEEVLQGLKSRLSILIDLGLPYLTPE---RALA------ 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 360 hmdqvvySLSGGQKKKLEILLML---LSGQEVLLiDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:PRK00635 476 -------TLSGGEQERTALAKHLgaeLIGITYIL-DEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEH 536
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
130-188 |
5.26e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 5.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489717269 130 TMSGGEKQRVALA-VLVAMDVD--LFLLDEP-----FASVdpaarRFLIGRLAKLKEQGKTIIITDH 188
Cdd:COG0178 826 TLSGGEAQRVKLAsELSKRSTGktLYILDEPttglhFHDI-----RKLLEVLHRLVDKGNTVVVIEH 887
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-218 |
6.20e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 124 LDQKIVTMSGGEKQRVALA---VLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKLKEQGKTIIITDH-----LFDDY-- 193
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAkflYLPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHdpallKQADYli 1772
|
90 100 110
....*....|....*....|....*....|
gi 489717269 194 -----QGKVDGVYRFKGEQVDLLTKDEQAL 218
Cdd:PRK00635 1773 emgpgSGKTGGKILFSGPPKDISASKDSLL 1802
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
263-399 |
6.40e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.45 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFKAM-TKLLDYQGSLTWEGK-----EVAKLKE-------RTY--FQHvaqifQNASDQF-MAI 326
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYRMRdgqlrDLYALSEaerrrllRTEwgFVH-----QHPRDGLrMQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 327 T----VKEEL-ALSQKHASpyftpEVLDQA---LADLDL-ADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSG 397
Cdd:PRK11701 107 SaggnIGERLmAVGARHYG-----DIRATAgdwLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGG 181
|
..
gi 489717269 398 LD 399
Cdd:PRK11701 182 LD 183
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-189 |
8.10e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 3 AELTIDHLTFSYGD-----REVIRdLSLTLPAGTFSLLIGPTGCGKS-TLLKIMaGLYpKYGGQLTSGQVSLGGRSQ--- 73
Cdd:PRK11022 2 ALLNVDKLSVHFGDesapfRAVDR-ISYSVKQGEVVGIVGESGSGKSvSSLAIM-GLI-DYPGRVMAEKLEFNGQDLqri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 74 -------------AMMFQEAgeqFTMATPREEIIFA-MENL-----GKSKTEFADRLKLASEFAEID--SLLDQKIVTMS 132
Cdd:PRK11022 79 sekerrnlvgaevAMIFQDP---MTSLNPCYTVGFQiMEAIkvhqgGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 133 GGEKQRVALAVLVAMDVDLFLLDEPFASVDPAARRFLIGRLAKL--KEQGKTIIITDHL 189
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDL 214
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
241-284 |
8.52e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.17 E-value: 8.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489717269 241 MKNFAIkqgrplLEQKELSIPKGkVTLITGPNGSGKSSLFKAMT 284
Cdd:pfam13476 3 IENFRS------FRDQTIDFSKG-LTLITGPNGSGKTTILDAIK 39
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
245-426 |
9.02e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 41.66 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 245 AIKQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFKAMTKLLD-YQGSLTWEGK-EVAKLKERTYF------QHVaqIF 316
Cdd:TIGR00954 460 VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPvYGGRLTKPAKgKLFYVPQRPYMtlgtlrDQI--IY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 317 QNASDQFmaitvkEELALSQKhaspyftpeVLDQALADLDL-------------ADHMDQvvysLSGGQKKKLEILLMLL 383
Cdd:TIGR00954 538 PDSSEDM------KRRGLSDK---------DLEQILDNVQLthilereggwsavQDWMDV----LSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 384 SGQEVLLIDEPLSGLdqkSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:TIGR00954 599 HKPQFAILDECTSAV---SVDVEGYMYRLCREF-GITLFSVSH 637
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
258-426 |
9.20e-04 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 40.94 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 258 LSIPKGKVTLITGPNGSGKSSLFKAMTkLLDY--QGSLTWEGKEVAKLKERTYFQHVA---QI----------FQNasdq 322
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCIN-LLETpdSGEIRVGGEEIRLKPDRDGELVPAdrrQLqrirtrlgmvFQS---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 323 F-----MaiTVKEE--------LALSQKhaspyftpEVLDQALADLD---LADHMDQVVYSLSGGQKKKLEILLMLLSGQ 386
Cdd:COG4598 104 FnlwshM--TVLENvieapvhvLGRPKA--------EAIERAEALLAkvgLADKRDAYPAHLSGGQQQRAAIARALAMEP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489717269 387 EVLLIDEPLSGLDQKSIEQVVQLLQKCQEKsGQTILLISH 426
Cdd:COG4598 174 EVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTH 212
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
130-287 |
9.64e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 130 TMSGGEKQRVALAV-----LVAMdvdLFLLDEPfaSV-----DpaARRfLIGRLAKLKEQGKTIIITDHLFD-----DYQ 194
Cdd:PRK00349 489 TLSGGEAQRIRLATqigsgLTGV---LYVLDEP--SIglhqrD--NDR-LIETLKHLRDLGNTLIVVEHDEDtiraaDYI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 195 gkVD-----GVYrfkGEQV-------DLLtKDEQAL----LLATEPIglhfPLPENEPaafvmknfaIKQGRPL------ 252
Cdd:PRK00349 561 --VDigpgaGVH---GGEVvasgtpeEIM-KNPNSLtgqyLSGKKKI----EVPKERR---------KGNGKFLklkgar 621
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489717269 253 ---LEQKELSIPKGKVTLITGPNGSGKSS-----LFKAMTKLL 287
Cdd:PRK00349 622 ennLKNVDVEIPLGKFTCVTGVSGSGKSTlinetLYKALARKL 664
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
256-282 |
1.13e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 1.13e-03
10 20
....*....|....*....|....*..
gi 489717269 256 KELSIPKGKVTLITGPNGSGKSSLFKA 282
Cdd:COG4637 14 RDLELPLGPLTVLIGANGSGKSNLLDA 40
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
126-186 |
1.53e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.76 E-value: 1.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 126 QKIVTMSGGEKQRVALAVLVAM----DVDLFLLDEPFASVDPA-ARRFlIGRLAKLKEQGKTIIIT 186
Cdd:cd03278 109 QRLSLLSGGEKALTALALLFAIfrvrPSPFCVLDEVDAALDDAnVERF-ARLLKEFSKETQFIVIT 173
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
96-189 |
1.66e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 96 AMENLGKSKTEFADRLKLASEFAEIDSLLD-------QKIVTMSGGEKQRVALAVLVAM----------DVDLFLLDEPF 158
Cdd:TIGR00618 909 ANQSEGRFHGRYADSHVNARKYQGLALLVAdaytgsvRPSATLSGGETFLASLSLALALadllstsggtVLDSLFIDEGF 988
|
90 100 110
....*....|....*....|....*....|.
gi 489717269 159 ASVDPAARRFLIGRLAKLKEQGKTIIITDHL 189
Cdd:TIGR00618 989 GSLDEDSLDRAIGILDAIREGSKMIGIISHV 1019
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
27-186 |
1.71e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 39.90 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 27 LPAGTFSLLIGPTGCGKSTLlkimaglypkyGGQLTSGQVSLGGRSqamMFqeageqFTMATPREEIIFAMENLGKSKTE 106
Cdd:COG0467 17 LPRGSSTLLSGPPGTGKTTL-----------ALQFLAEGLRRGEKG---LY------VSFEESPEQLLRRAESLGLDLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 107 FADRLKL-------ASEFAEIDSLLDQKIVTMSGGEKQRVALavlvamD-VDLFLLdepfASVDPA-ARRFLIGRLAKLK 177
Cdd:COG0467 77 YIESGLLriidlspEELGLDLEELLARLREAVEEFGAKRVVI------DsLSGLLL----ALPDPErLREFLHRLLRYLK 146
|
....*....
gi 489717269 178 EQGKTIIIT 186
Cdd:COG0467 147 KRGVTTLLT 155
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
27-189 |
1.78e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 39.29 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 27 LPAGTFSLLIGPTGCGKSTL-----LKIMAGLyPKYGGQLTSGQVSlggrsqAMMFQeaGEQftmatPREEIIFAMENLG 101
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLaldlaAAVATGK-PWLGGPRVPEQGK------VLYVS--AEG-----PADELRRRLRAAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 102 KsKTEFADRLKLASEFAEIDSLLDQKIVTMSGGEKQRVALAVLVAMDVDLFLLDePFASV-------DPAARRFlIGRLA 174
Cdd:pfam13481 96 A-DLDLPARLLFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVEDPDLVVID-PLARAlggdensNSDVGRL-VKALD 172
|
170
....*....|....*.
gi 489717269 175 KLKEQ-GKTIIITDHL 189
Cdd:pfam13481 173 RLARRtGATVLLVHHV 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
357-431 |
1.83e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 1.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 357 LADHMDQVVYS----LSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHFYGI 431
Cdd:PTZ00265 565 LPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
34-148 |
1.85e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 38.34 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 34 LLIGPTGCGKSTLLKIMAG-LYPKY----GGQLTSGQVSLGGRSQAMMFQEAgeqFTMATPreeIIFamenlgksktefa 108
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKeLGAPFieisGSELVSKYVGESEKRLRELFEAA---KKLAPC---VIF------------- 62
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489717269 109 drlklaseFAEIDSLLdQKIVTMSGGEKQRVALAVLVAMD 148
Cdd:pfam00004 63 --------IDEIDALA-GSRGSGGDSESRRVVNQLLTELD 93
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
130-175 |
1.98e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.21 E-value: 1.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 130 TMSGGEKQRVA----LAVLVAM---------DVDLFLLDEPFASVDPAARRFLIGRLAK 175
Cdd:pfam13558 32 GLSGGEKQLLAylplAAALAAQygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
240-357 |
2.10e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 240 VMKNFAIKQGRPLLEqkelsiPKGKVTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKEVAKLK------------ERT 307
Cdd:cd03239 5 TLKNFKSYRDETVVG------GSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGggvkaginsasvEIT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489717269 308 YFQHVAQIFQNASDQFMA------ITVKEELALSQKHASPYFtpeVLDQALADLDL 357
Cdd:cd03239 79 FDKSYFLVLQGKVEQILSggekslSALALIFALQEIKPSPFY---VLDEIDAALDP 131
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
265-299 |
2.19e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 2.19e-03
10 20 30
....*....|....*....|....*....|....*
gi 489717269 265 VTLITGPNGSGKSSLFKAMTKLLDYQGSLTWEGKE 299
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDE 35
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
234-399 |
2.91e-03 |
|
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: 40.28 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 234 NEPAAFVMKNFAIkQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFkaMTKLLDYQGSltwEGKevaklkertyFQHVA 313
Cdd:TIGR01271 424 NGDDGLFFSNFSL-YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLL--MMIMGELEPS---EGK----------IKHSG 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 314 QI-FQNASDQFMAITVKEELALSQKHASPYFTPEVLD-QALADLDLADHMDQVVY-----SLSGGQKKKLEILLMLLSGQ 386
Cdd:TIGR01271 488 RIsFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKAcQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDA 567
|
170
....*....|...
gi 489717269 387 EVLLIDEPLSGLD 399
Cdd:TIGR01271 568 DLYLLDSPFTHLD 580
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
256-288 |
3.34e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 3.34e-03
10 20 30
....*....|....*....|....*....|....
gi 489717269 256 KELSIP-KGKVTLITGPNGSGKSSLFKAMTKLLD 288
Cdd:COG3593 15 KDLSIElSDDLTVLVGENNSGKSSILEALRLLLG 48
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
263-432 |
3.41e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.17 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 263 GKVTLITGPNGSGKSSLFKAMTKLL--DYQGSLtwEGKEVAKLKERTYFQ----HVAQIFQNASDQFMA----ITV---- 328
Cdd:cd03272 23 PKHNVVVGRNGSGKSNFFAAIRFVLsdEYTHLR--EEQRQALLHEGSGPSvmsaYVEIIFDNSDNRFPIdkeeVRLrrti 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 329 ---KEELALSQKHAS-----------------PYFtpeVLDQ------ALADLDLADHMDQvvysLSGGQkKKLEILLML 382
Cdd:cd03272 101 glkKDEYFLDKKNVTkndvmnllesagfsrsnPYY---IVPQgkinslTNMKQDEQQEMQQ----LSGGQ-KSLVALALI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489717269 383 LSGQEV-----LLIDEPLSGLDQKSIEQVVQLLQKcQEKSGQTI--------LLISHHFYGIS 432
Cdd:cd03272 173 FAIQKCdpapfYLFDEIDAALDAQYRTAVANMIKE-LSDGAQFItttfrpelLEVADKFYGVK 234
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
258-279 |
3.66e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 3.66e-03
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
232-406 |
3.92e-03 |
|
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: 39.07 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 232 PENEPAAFvMKNFAIkQGRPLLEQKELSIPKGKVTLITGPNGSGKSSLFkaMTKLLDYQGSltwEGKevaklkertyFQH 311
Cdd:cd03291 34 SSDDNNLF-FSNLCL-VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL--MLILGELEPS---EGK----------IKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 312 VAQI-FQNASDQFMAITVKEELALSQKHASPYFTPEV----LDQALADLDLADH--MDQVVYSLSGGQKKKLEILLMLLS 384
Cdd:cd03291 97 SGRIsFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVkacqLEEDITKFPEKDNtvLGEGGITLSGGQRARISLARAVYK 176
|
170 180
....*....|....*....|..
gi 489717269 385 GQEVLLIDEPLSGLDQKSIEQV 406
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEI 198
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
256-426 |
3.93e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.18 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 256 KELSIPKGKVTLITGPNGSGKSSLFKAMtkLLDYQGSLTWEGKEVAKLKeRTYFQHVAQIFQNASD-----QFMAITVKE 330
Cdd:COG4938 13 KEAELELKPLTLLIGPNGSGKSTLIQAL--LLLLQSNFIYLPAERSGPA-RLYPSLVRELSDLGSRgeytaDFLAELENL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 331 ELALSQKHASPYFTPEVLDQAL-ADLDLADHMDQV--VYSLSG------------GQKKKLEILLMLLSG---QEVLLID 392
Cdd:COG4938 90 EILDDKSKELLEQVEEWLEKIFpGKVEVDASSDLVrlVFRPSGngkriplsnvgsGVSELLPILLALLSAakpGSLLIIE 169
|
170 180 190
....*....|....*....|....*....|....
gi 489717269 393 EPLSGLDQKSIEQVVQLLQKCQeKSGQTILLISH 426
Cdd:COG4938 170 EPEAHLHPKAQSALAELLAELA-NSGVQVIIETH 202
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
326-426 |
5.59e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 326 ITVKEELALSQ-----KHASPYFTPEVLDQALADLDLADHMDQVV-----YSLSGGQKKKLEILLMLLSGQEVLLIDEPL 395
Cdd:PLN03140 968 VTVRESLIYSAflrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
90 100 110
....*....|....*....|....*....|.
gi 489717269 396 SGLDQKSIEQVVQLLQKCQEkSGQTILLISH 426
Cdd:PLN03140 1048 SGLDARAAAIVMRTVRNTVD-TGRTVVCTIH 1077
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
367-428 |
6.09e-03 |
|
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: 37.55 E-value: 6.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489717269 367 SLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLQKCQEKSGQTILLISHHF 428
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
349-427 |
6.90e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 38.56 E-value: 6.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489717269 349 DQALADLDLADHMDQVVYSLSGGQKKKLEILLMLLSGQEVLLIDEPLSGLDQKSIEQVVQLLqKCQEKSGQTILLISHH 427
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQY 203
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
27-186 |
8.90e-03 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 37.63 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 27 LPAGTFSLLIGPTGCGKSTLlkimaglypkyGGQLTSGQVSLGgrsqammfqEAGEQFTMATPREEIIFAMENLGKSKTE 106
Cdd:cd01124 16 IPKGSVTLLTGGPGTGKTLF-----------GLQFLYAGAKNG---------EPGLFFTFEESPERLLRNAKSFGWDFDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489717269 107 FADRLKLAsefaeidsLLDQKIVTMSGGEKQRVALAVL----------VAMD-VDLFLLdepFASVDPAARRFLIGRLAK 175
Cdd:cd01124 76 MEDEGKLI--------IVDAPPTEAGRFSLDELLSRILsiiksfkakrVVIDsLSGLRR---AKEDQMRARRIVIALLNE 144
|
170
....*....|.
gi 489717269 176 LKEQGKTIIIT 186
Cdd:cd01124 145 LRAAGVTTIFT 155
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
14-58 |
9.61e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.74 E-value: 9.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489717269 14 YGDREVIRDLSLTLPAGTFS--LLIGPTGCGKSTLLKIMAGLYPKYG 58
Cdd:cd00009 1 VGQEEAIEALREALELPPPKnlLLYGPPGTGKTTLARAIANELFRPG 47
|
|
| |
