|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-325 |
0e+00 |
|
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: 540.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVkEGEILFQNENVLSKSEKE 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT-SGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHELSGGMKQRV 164
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIF 244
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 245 QSPNHPYTKGLLNSLPKIsNGVKERLAPIQGVTPNLLHPPKGCPFAERCPHKMDICEKERPPYFEIGNGRRSMCWLNDRA 324
Cdd:COG0444 240 ENPRHPYTRALLSSIPRL-DPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEEE 318
|
.
gi 1078707892 325 V 325
Cdd:COG0444 319 A 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-261 |
3.30e-145 |
|
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: 419.86 E-value: 3.30e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVKEGEILFQNENVLSK 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHELSGGM 160
Cdd:COG4172 82 SERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHV 240
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
250 260
....*....|....*....|.
gi 1078707892 241 LDIFQSPNHPYTKGLLNSLPK 261
Cdd:COG4172 242 AELFAAPQHPYTRKLLAAEPR 262
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-319 |
7.60e-140 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 399.10 E-value: 7.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVkEGEILFQNENVLSK 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI-GGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHELSGGM 160
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHV 240
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 241 LDIFQSPNHPYTKGLLNSLPKIsNGVKERLAPIQGVTPNLLHPPKGCPFAERCPHKMDICEKErPPYFEIGNGRRSMCW 319
Cdd:PRK09473 247 RDVFYQPSHPYSIGLLNAVPRL-DAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSA-PPLEEFGPGRLRACF 323
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-318 |
8.11e-118 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 342.88 E-value: 8.11e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHELSGGMKQRV 164
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIF 244
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 245 QSPNHPYTKGLLNSLPKISNGvKERLAPIQGVTPNLLHPPKGCPFAERCPHKMDICEKERPPYFEIGnGRRSMC 318
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFAQD-KARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLA-GRQSKC 314
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-238 |
5.38e-116 |
|
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: 334.47 E-value: 5.38e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtspGKVKEGEILFQNENVLSKSEKe 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL----LKPTSGSIIFDGKDLLKLSRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVnLLKQVGLSSPEERVRQYPHELSGGMKQRV 164
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-327 |
1.62e-112 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 329.39 E-value: 1.62e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFFI-------EDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALV--TSpgkvkeGEIL 71
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEepTS------GEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 72 FQNENVLSKSEKELRSIRgNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLssPEERVRQ 151
Cdd:COG4608 77 FDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGL--RPEHADR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 152 YPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYG 231
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 232 GLIMEEGHVLDIFQSPNHPYTKGLLNSLPKISNGVKERLAPIQGVTPNLLHPPKGCPFAERCPHKMDICEKERPPYFEIG 311
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVG 313
|
330
....*....|....*.
gi 1078707892 312 NGRRSMCWLNDRAVGD 327
Cdd:COG4608 314 PGHQVACHLAEEGSGV 329
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-262 |
2.73e-103 |
|
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: 312.22 E-value: 2.73e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFFI-EDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLS 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL----RPTSGSILFDGKDLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 80 KSEKELRSIRGnQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLssPEERVRQYPHELSGG 159
Cdd:COG1123 332 LSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGL--PPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250 260
....*....|....*....|...
gi 1078707892 240 VLDIFQSPNHPYTKGLLNSLPKI 262
Cdd:COG1123 489 TEEVFANPQHPYTRALLAAVPSL 511
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-247 |
3.76e-100 |
|
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: 304.13 E-value: 3.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFfiEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVkEGEILFQNENVLSKSE 82
Cdd:COG1123 2 TPLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KelrsIRGNQISLISQDPMSALNPVvKIGKQMTEVIiRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGMKQ 162
Cdd:COG1123 79 A----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEAL-ENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLD 242
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
....*
gi 1078707892 243 IFQSP 247
Cdd:COG1123 230 ILAAP 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-260 |
6.91e-92 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 283.52 E-value: 6.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKV-KEGEILFQNENVLS 79
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 80 KSEKELRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHELSGG 159
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260
....*....|....*....|.
gi 1078707892 240 VLDIFQSPNHPYTKGLLNSLP 260
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEP 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-262 |
9.73e-88 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 275.58 E-value: 9.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 2 SEKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALV-TSPGKVKEGEILFQ--NENVL 78
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLeQAGGLVQCDKMLLRrrSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 79 S---KSEKELRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHE 155
Cdd:PRK10261 89 ElseQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIM 235
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260
....*....|....*....|....*..
gi 1078707892 236 EEGHVLDIFQSPNHPYTKGLLNSLPKI 262
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQL 275
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-300 |
8.72e-87 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 264.07 E-value: 8.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQISLISQDPMSALNPVVKIGKQMTEVII----------RHQKVKKReaqniAVNLLKQVGLSSPEERVRQYPH 154
Cdd:COG4170 83 RRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPswtfkgkwwqRFKWRKKR-----AIELLHRVGIKDHKDIMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 235 MEEGHVLDIFQSPNHPYTKGLLNSLPKISNGV--KERLAPIQGVTPNLLHPPKGCPFAERCPHKMDIC 300
Cdd:COG4170 238 VESGPTEQILKSPHHPYTKALLRSMPDFRQPLphKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKC 305
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-318 |
9.66e-86 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 261.05 E-value: 9.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNL------KTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVmALVTSPgkvKEGEILFQN 74
Cdd:PRK11308 1 SQQPLLQAIDLkkhypvKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLL-TMIETP---TGGELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 75 ENVLSKSEKELRSIRgNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSsPEERVRqYPH 154
Cdd:PRK11308 77 QDLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLR-PEHYDR-YPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 235 MEEGHVLDIFQSPNHPYTKGLLNSLPKISNGVKERLAPIQGVTPNLLHPPKGCPFAERCPHKMDICEKERPPYFEIGnGR 314
Cdd:PRK11308 234 VEKGTKEQIFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYD-GR 312
|
....
gi 1078707892 315 RSMC 318
Cdd:PRK11308 313 LVAC 316
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-262 |
3.73e-85 |
|
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: 266.17 E-value: 3.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDG-------EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvkEGEILFQNENV 77
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-----EGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 LSKSEKELRSIRgNQISLISQDPMSALNPVVKIGKQMTEVIIRHQ-KVKKREAQNIAVNLLKQVGLSsPEERVRqYPHEL 156
Cdd:COG4172 350 DGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLD-PAARHR-YPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 SGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIME 236
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....*.
gi 1078707892 237 EGHVLDIFQSPNHPYTKGLLNSLPKI 262
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAPLL 532
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-305 |
3.62e-83 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 254.63 E-value: 3.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEK---LLEVKNLKTSFFIEDGE---------VEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEG 68
Cdd:PRK15079 1 VTEGkkvLLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV----KATDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 69 EILFQNENVLSKSEKELRSIRgNQISLISQDPMSALNPVVKIGKQMTE-VIIRHQKVKKREAQNIAVNLLKQVGLSspEE 147
Cdd:PRK15079 77 EVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEpLRTYHPKLSRQEVKDRVKAMMLKVGLL--PN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 148 RVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVI 227
Cdd:PRK15079 154 LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 228 VMYGGLIMEEGHVLDIFQSPNHPYTKGLLNSLPkISNGVKERLAPIQ---GVTPNLLHPPKGCPFAERCPHKMDICEKER 304
Cdd:PRK15079 234 VMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP-IPDPDLERNKTIQlleGELPSPINPPSGCVFRTRCPIAGPECAKTR 312
|
.
gi 1078707892 305 P 305
Cdd:PRK15079 313 P 313
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-260 |
2.32e-81 |
|
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: 247.02 E-value: 2.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKE 84
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLE----RPWSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSirgnQISLISQDPMSALNPVVKIGKQMTEVIiRHQKVKKREAQniAVNLLKQVGLssPEERVRQYPHELSGGMKQRV 164
Cdd:COG1124 77 FRR----RVQMVFQDPYASLHPRHTVDRILAEPL-RIHGLPDREER--IAELLEQVGL--PPSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIF 244
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 1078707892 245 QSPNHPYTKGLLNSLP 260
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-256 |
7.99e-79 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 239.96 E-value: 7.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVKEGEILFQNENVLSKSekelrsIRGNQISLISQDPMSA 103
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 104 LNPVVKIGKQMTEVIIRHQKVKKrEAQNIAVNLLKQVGLSSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPT 183
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707892 184 TALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPYTKGLL 256
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLL 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-300 |
6.37e-74 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 231.23 E-value: 6.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIR-------HQKVKKREAQniAVNLLKQVGLSSPEERVRQYPHELS 157
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGwtykgrwWQRFGWRKRR--AIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 238 GHVLDIFQSPNHPYTKGLLNSLPKISNGV--KERLAPIQGVTPNLLHPPKGCPFAERCPHKMDIC 300
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDFGSAMphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQREC 305
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-259 |
1.09e-63 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 202.35 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSvMALVTSPGkvkEGEILFQN-----E 75
Cdd:COG4107 4 EEQPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKC-LYFDLAPT---SGSVYYRDrdggpR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 76 NVLSKSEKELRSIRGNQISLISQDPMSALNPVV----KIGKQMTEVIIRH-QKVKKReaqniAVNLLKQVGLssPEERVR 150
Cdd:COG4107 80 DLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVsaggNIAERLMAAGERHyGDIRAR-----ALEWLERVEI--PLERID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 151 QYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMY 230
Cdd:COG4107 153 DLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMK 232
|
250 260
....*....|....*....|....*....
gi 1078707892 231 GGLIMEEGHVLDIFQSPNHPYTKGLLNSL 259
Cdd:COG4107 233 NGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-234 |
6.66e-59 |
|
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: 188.85 E-value: 6.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMaksvMALVTSPGKVKEGEILFQNENVLSKSEKEL 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGGLDRPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGNQISLISQDP-----MSALNPVvkigkqmtEVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGM 160
Cdd:cd03255 77 AAFRRRHIGFVFQSFnllpdLTALENV--------ELPLLLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIvAQNCTRVIVMYGGLI 234
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-256 |
9.59e-59 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 197.24 E-value: 9.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 2 SEKLLEVKNLKTSFFIEDG-------EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvkEGEILFQN 74
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-----QGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 75 ENVLSKSEKELRSIRgNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKV---KKREAQNIAVnlLKQVGLSsPEERVRq 151
Cdd:PRK15134 347 QPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlsaAQREQQVIAV--MEEVGLD-PETRHR- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 152 YPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYG 231
Cdd:PRK15134 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
250 260
....*....|....*....|....*
gi 1078707892 232 GLIMEEGHVLDIFQSPNHPYTKGLL 256
Cdd:PRK15134 502 GEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-239 |
1.85e-58 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 187.94 E-value: 1.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTSPgkvKEGEILFQNENVLSKSE 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRP---TSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSIRGNQISLISQDP-----MSALNPVvkigkqmtEVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELS 157
Cdd:COG1136 78 RELARLRRRHIGFVFQFFnllpeLTALENV--------ALPLLLAGVSRKERRERARELLERVGL---GDRLDHRPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIvAQNCTRVIVMYGGLIMEE 237
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDGRIVSD 225
|
..
gi 1078707892 238 GH 239
Cdd:COG1136 226 ER 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-258 |
4.09e-58 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 188.12 E-value: 4.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFFIEDG-----EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEILFqNENV 77
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAK-MLAGIIEP---TSGEILI-NGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 LSKSEKELRSirgNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSspEERVRQYPHELS 157
Cdd:COG4167 77 LEYGDYKYRC---KHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLL--PEHANFYPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEY 231
|
250 260
....*....|....*....|.
gi 1078707892 238 GHVLDIFQSPNHPYTKGLLNS 258
Cdd:COG4167 232 GKTAEVFANPQHEVTKRLIES 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-275 |
1.61e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 189.13 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAL--VTSpgkvkeGEILFQNENVLSKSEK 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLerPTS------GSVLVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 84 ELRSIRGnQISLISQD---------------PMsalnpvvkigkqmteviiRHQKVKKREAQNIAVNLLKQVGLSspeER 148
Cdd:COG1135 76 ELRAARR-KIGMIFQHfnllssrtvaenvalPL------------------EIAGVPKAEIRKRVAELLELVGLS---DK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 149 VRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIV 228
Cdd:COG1135 134 ADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAV 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1078707892 229 MYGGLIMEEGHVLDIFQSPNHPYTKGLLNSL--PKISNGVKERLAPIQG 275
Cdd:COG1135 214 LENGRIVEQGPVLDVFANPQSELTRRFLPTVlnDELPEELLARLREAAG 262
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-260 |
4.29e-57 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 194.69 E-value: 4.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 2 SEKLLEVKNLKTSFFIEDG-------EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQN 74
Cdd:PRK10261 310 GEPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVES----QGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 75 ENVLSKSEKELRSIRGNqISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSsPEERVRqYPH 154
Cdd:PRK10261 386 QRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLL-PEHAWR-YPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
250 260
....*....|....*....|....*.
gi 1078707892 235 MEEGHVLDIFQSPNHPYTKGLLNSLP 260
Cdd:PRK10261 543 VEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-256 |
8.79e-57 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 184.52 E-value: 8.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAlVTSPG-KVKEGEILFQNENVlsksekELRSIRGNQISLISQDPMSA 103
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALG-ILPAGvRQTAGRVLLDGKPV------APCALRGRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 104 LNPVVKIGKQMTEVIirhQKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPT 183
Cdd:PRK10418 92 FNPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707892 184 TALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPYTKGLL 256
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-259 |
4.24e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 177.11 E-value: 4.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVlSKSEKE 84
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGTITVDGEDL-TDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGnQISLISQD----P-MSALNPVvkigkqmTEVIIRHQKVKKREAQNIAVNLLKQVGLSspeERVRQYPHELSGG 159
Cdd:COG1126 72 INKLRR-KVGMVFQQfnlfPhLTVLENV-------TLAPIKVKKMSKAEAEERAMELLERVGLA---DKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250 260
....*....|....*....|
gi 1078707892 240 VLDIFQSPNHPYTKGLLNSL 259
Cdd:COG1126 220 PEEFFENPQHERTRAFLSKV 239
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-247 |
1.42e-52 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 172.77 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTsPgkvKEGEILFQNENVLSKSEKE 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER-P---TSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRgNQISLISQ--DPMSAlnpvvkigKQMTEVI---IRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGG 159
Cdd:cd03258 77 LRKAR-RRIGMIFQhfNLLSS--------RTVFENValpLEIAGVPKAEIEERVLELLELVGL---EDKADAYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
....*...
gi 1078707892 240 VLDIFQSP 247
Cdd:cd03258 225 VEEVFANP 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-253 |
2.94e-52 |
|
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: 172.47 E-value: 2.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSK 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL----RPDSGEILVDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSIRgNQISLISQDpmSAL--------N---PvvkigkqmtevIIRHQKVKKREAQNIAVNLLKQVGLSSPEERv 149
Cdd:COG1127 73 SEKELYELR-RRIGMLFQG--GALfdsltvfeNvafP-----------LREHTDLSEAEIRELVLEKLELVGLPGAADK- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 150 rqYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVM 229
Cdd:COG1127 138 --MPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVL 215
|
250 260
....*....|....*....|....
gi 1078707892 230 YGGLIMEEGHVLDIFQSpNHPYTK 253
Cdd:COG1127 216 ADGKIIAEGTPEELLAS-DDPWVR 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-244 |
2.29e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 169.82 E-value: 2.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKtsfFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKEL 85
Cdd:COG1122 1 IELENLS---FSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL----KPTSGEVLVDGKDITKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSirgnQISLISQDPMSAL-NPVVKigkqmTEVI--IRHQKVKKREAQNIAVNLLKQVGLSSPEERVrqyPHELSGGMKQ 162
Cdd:COG1122 74 RR----KVGLVFQNPDDQLfAPTVE-----EDVAfgPENLGLPREEIRERVEEALELVGLEHLADRP---PHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLD 242
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
..
gi 1078707892 243 IF 244
Cdd:COG1122 221 VF 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-232 |
8.90e-50 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 164.95 E-value: 8.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 7 EVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtspGKVKEGEILFQNENVLSKSEKELR 86
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL----LGPTSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 sirgNQISLISQDPMSAL-NPVVKigkqmTEVII--RHQKVKKREAQNIAVNLLKQVGLSSPEERVrqyPHELSGGMKQR 163
Cdd:cd03225 75 ----RKVGLVFQNPDDQFfGPTVE-----EEVAFglENLGLPEEEIEERVEEALELVGLEGLRDRS---PFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 164 VMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-238 |
1.02e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.61 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKEL 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL----RPTSGEVRVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RsirgnQISLISQDPmsALNPVVKiGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGMKQRVM 165
Cdd:COG1131 73 R-----RIGYVPQEP--ALYPDLT-VRENLRFFARLYGLPRKEARERIDELLELFGL---TDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-253 |
1.16e-47 |
|
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: 160.36 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTsPGKvkeGEILFQNENVLSKSEKEL 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-PDS---GEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQDpmSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGMKQRVM 165
Cdd:cd03261 73 YRLR-RRMGMLFQS--GALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL---RGAEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQ 245
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*...
gi 1078707892 246 SPnHPYTK 253
Cdd:cd03261 227 SD-DPLVR 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-239 |
4.89e-47 |
|
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: 158.75 E-value: 4.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAkSVMA---LVTSpGKVK-EGEILFQnen 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLL-GLLAgldRPTS-GTVRlAGQDLFA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 77 vLSksEKELRSIRGNQISLISQD----P-MSALNPVvkigkqMTEVIIRHQkvkkREAQNIAVNLLKQVGLSspeERVRQ 151
Cdd:COG4181 79 -LD--EDARARLRARHVGFVFQSfqllPtLTALENV------MLPLELAGR----RDARARARALLERVGLG---HRLDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 152 YPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIvAQNCTRVIVMYG 231
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL-AARCDRVLRLRA 221
|
....*...
gi 1078707892 232 GLIMEEGH 239
Cdd:COG4181 222 GRLVEDTA 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-258 |
1.33e-46 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 158.17 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTSPGkvkEGEILFQNE----- 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLL-NALSARLAPD---AGEVHYRMRdgqlr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 76 NVLSKSEKELRSIRGNQISLISQDPMSALNPVVKIGKQMTEviiRHQKVKKREAQNI---AVNLLKQVGLssPEERVRQY 152
Cdd:PRK11701 74 DLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGE---RLMAVGARHYGDIratAGDWLERVEI--DAARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 153 PHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250 260
....*....|....*....|....*....
gi 1078707892 233 LIMEEG---HVLDifqSPNHPYTKGLLNS 258
Cdd:PRK11701 229 RVVESGltdQVLD---DPQHPYTQLLVSS 254
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-234 |
3.85e-46 |
|
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: 155.77 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVlSKSEKEL 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGTIIIDGLKL-TDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQD----P-MSALNPVvkigkqmTEVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGM 160
Cdd:cd03262 72 NELR-QKVGMVFQQfnlfPhLTVLENI-------TLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-272 |
7.05e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 158.81 E-value: 7.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 7 EVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvTSPgkvKEGEILFQNENVLSKSEKELR 86
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-ERP---TSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 SIRgNQISLISQD---------------PMSALNpvvkigkqmteviIRHQKVKKReaqniaVN-LLKQVGLSspeERVR 150
Cdd:PRK11153 79 KAR-RQIGMIFQHfnllssrtvfdnvalPLELAG-------------TPKAEIKAR------VTeLLELVGLS---DKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 151 QYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMY 230
Cdd:PRK11153 136 RYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVID 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1078707892 231 GGLIMEEGHVLDIFQSPNHPYTKGLLNSL--PKISNGVKERLAP 272
Cdd:PRK11153 216 AGRLVEQGTVSEVFSHPKHPLTREFIQSTlhLDLPEDYLARLQA 259
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-260 |
1.13e-45 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 156.39 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvTSPGKvkeGEILFQNENVLSKSEKELRSIRGNqISLISQDPMSAL 104
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQ---GNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 105 NPVVKIGKQMTEVIiRH-QKVKKREAQNIAVNLLKQVGLssPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPT 183
Cdd:PRK10419 103 NPRKTVREIIREPL-RHlLSLDKAERLARASEMLRAVDL--DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 184 TALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIfQSPNHPYTKGLLNS-LP 260
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK-LTFSSPAGRVLQNAvLP 256
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-258 |
1.78e-45 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 155.72 E-value: 1.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFFIEDG-----EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGkvkeGEILFqNENV 77
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS----GELLI-DDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 LSKSEKELRSIRgnqISLISQDPMSALNPVVKIGkQMTEVIIRHQKVKKREAQNIAVNL-LKQVGLSSpeERVRQYPHEL 156
Cdd:PRK15112 77 LHFGDYSYRSQR---IRMIFQDPSTSLNPRQRIS-QILDFPLRLNTDLEPEQREKQIIEtLRQVGLLP--DHASYYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 SGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIME 236
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 1078707892 237 EGHVLDIFQSPNHPYTKGLLNS 258
Cdd:PRK15112 231 RGSTADVLASPLHELTKRLIAG 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-248 |
9.22e-45 |
|
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: 153.28 E-value: 9.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKE 84
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLL----KPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSirgnQISLISQDPMSALNpvvkigkqMT--EVIIR----HQKVKKREAQN---IAVNLLKQVGLSSPEERvrqYPHE 155
Cdd:COG1120 73 LAR----RIAYVPQEPPAPFG--------LTvrELVALgrypHLGLFGRPSAEdreAVEEALERTGLEHLADR---PVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIM 235
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
250
....*....|...
gi 1078707892 236 EEGHVLDIFQSPN 248
Cdd:COG1120 218 AQGPPEEVLTPEL 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-236 |
2.84e-44 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 150.96 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKE 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNP----TSGEVLFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQISLISQ-----DPMSALNPVvkigkqMTEVIIRHQKVKkrEAQNIAVNLLKQVGLsspEERVRQYPHELSGG 159
Cdd:TIGR02211 77 RAKLRNKKLGFIYQfhhllPDFTALENV------AMPLLIGKKSVK--EAKERAYEMLEKVGL---EHRINHRPSELSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIvAQNCTRVIVMYGGLIME 236
Cdd:TIGR02211 146 ERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLEL-AKKLDRVLEMKDGQLFN 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-229 |
3.06e-43 |
|
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: 148.39 E-value: 3.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGkvkEGEILFQNENVlsksekel 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLR-IIAGLERPT---SGEVLVDGEPV-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rSIRGNQISLISQDP-----MSAL-NpvVKIGkqmteviIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGG 159
Cdd:cd03293 69 -TGPGPDRGYVFQQDallpwLTVLdN--VALG-------LELQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVM 229
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
4.32e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.70 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVlsk 80
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLL----PPTSGTVRLFGKPP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 sekelrSIRGNQISLISQD-------PMSALNpVVKIGkqmtevIIRHQKVKKR---EAQNIAVNLLKQVGLSSPEERvr 150
Cdd:COG1121 71 ------RRARRRIGYVPQRaevdwdfPITVRD-VVLMG------RYGRRGLFRRpsrADREAVDEALERVGLEDLADR-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 151 QYpHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMY 230
Cdd:COG1121 136 PI-GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLN 213
|
250
....*....|....*...
gi 1078707892 231 GGLImEEGHVLDIFQSPN 248
Cdd:COG1121 214 RGLV-AHGPPEEVLTPEN 230
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-259 |
5.58e-43 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 148.83 E-value: 5.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNEN-----V 77
Cdd:TIGR02323 1 KPLLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLA----PDHGTATYIMRSgaeleL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 LSKSEKELRSIRGNQISLISQDPMSALNPVVKIGKQMTEviiRHQKVKKREAQNI---AVNLLKQVGLssPEERVRQYPH 154
Cdd:TIGR02323 73 YQLSEAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGE---RLMAIGARHYGNIratAQDWLEEVEI--DPTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....*
gi 1078707892 235 MEEGHVLDIFQSPNHPYTKGLLNSL 259
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-229 |
1.41e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.93 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSK 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLE----KPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 sekelrsirGNQISLISQDP-----MSAL-NpvVKIGkqmteviIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPH 154
Cdd:COG1116 79 ---------GPDRGVVFQEPallpwLTVLdN--VALG-------LELRGVPKAERRERARELLELVGLAGFEDA---YPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDV----TIQAQILDLMKnlknETNMSLLLITHD------LGivaqncT 224
Cdd:COG1116 138 QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLWQ----ETGKTVLFVTHDvdeavfLA------D 207
|
....*
gi 1078707892 225 RVIVM 229
Cdd:COG1116 208 RVVVL 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-238 |
1.05e-41 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 145.02 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKEL 85
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP----TSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGnQISLISQDP-----MSALNPVvkigkqMTEVIIRHQKVK------KREAQNIAVNLLKQVGLSspeERVRQYPH 154
Cdd:cd03256 74 RQLRR-QIGMIFQQFnlierLSVLENV------LSGRLGRRSTWRslfglfPKEEKQRALAALERVGLL---DKAYQRAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
....
gi 1078707892 235 MEEG 238
Cdd:cd03256 224 VFDG 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-235 |
1.71e-41 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 143.44 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 7 EVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEIlfqneNVLSKSEKELR 86
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL----KPTSGSI-----RVFGKPLEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 SIRG--NQISLISQD-PMSALNpVVKIGKQMTEVIIRHQKVKKREAqniAVNLLKQVGLSspEERVRQYpHELSGGMKQR 163
Cdd:cd03235 68 KRIGyvPQRRSIDRDfPISVRD-VVLMGLYGHKGLFRRLSKADKAK---VDEALERVGLS--ELADRQI-GELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 164 VMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIM 235
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-238 |
2.16e-41 |
|
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: 142.19 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 7 EVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKELR 86
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL----KPSSGEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 sirgNQISLISQdpmsalnpvvkigkqmteviirhqkvkkreaqniavnLLKQVGLSSPEERvrqYPHELSGGMKQRVMI 166
Cdd:cd03214 73 ----RKIAYVPQ-------------------------------------ALELLGLAHLADR---PFNELSGGERQRVLL 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 167 AMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-256 |
6.40e-41 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 142.92 E-value: 6.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSKSEKE 84
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE----ITSGDLIVDGLKVNDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 lRSIRG------NQISLISQdpMSALNPVVkIGKqmteviIRHQKVKKREAQNIAVNLLKQVGLSspeERVRQYPHELSG 158
Cdd:PRK09493 73 -RLIRQeagmvfQQFYLFPH--LTALENVM-FGP------LRVRGASKEEAEKQARELLAKVGLA---ERAHHYPSELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
250
....*....|....*...
gi 1078707892 239 HVLDIFQSPNHPYTKGLL 256
Cdd:PRK09493 219 DPQVLIKNPPSQRLQEFL 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-235 |
5.83e-40 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 140.58 E-value: 5.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 4 KLLEVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSKSEK 83
Cdd:COG3638 1 PMLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE----PTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 84 ELRSIRGnQISLISQDP-----MSALNPVVkIGK--QMTevIIRH--QKVKKREaQNIAVNLLKQVGLSspeERVRQYPH 154
Cdd:COG3638 74 ALRRLRR-RIGMIFQQFnlvprLSVLTNVL-AGRlgRTS--TWRSllGLFPPED-RERALEALERVGLA---DKAYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
.
gi 1078707892 235 M 235
Cdd:COG3638 226 V 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-251 |
7.28e-39 |
|
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: 138.55 E-value: 7.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 4 KLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEK 83
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI----EPTSGKVLIDGQDIAAMSRK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 84 ELRSIRGNQISLISQDpmSALNPvvkigkQMT---------EViirhQKVKKREAQNIAVNLLKQVGLsspEERVRQYPH 154
Cdd:cd03294 95 ELRELRRKKISMVFQS--FALLP------HRTvlenvafglEV----QGVPRAEREERAAEALELVGL---EGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
250
....*....|....*..
gi 1078707892 235 MEEGHVLDIFQSPNHPY 251
Cdd:cd03294 240 VQVGTPEEILTNPANDY 256
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-238 |
1.77e-38 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 136.66 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKE 84
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP----SSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRgNQISLISQD-----PMSALNPVV--KIGKQMTEVIIRHQKvkKREAQNIAVNLLKQVGLSspeERVRQYPHELS 157
Cdd:TIGR02315 74 LRKLR-RRIGMIFQHynlieRLTVLENVLhgRLGYKPTWRSLLGRF--SEEDKERALSALERVGLA---DKAYQRADQLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
.
gi 1078707892 238 G 238
Cdd:TIGR02315 228 G 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-245 |
2.92e-38 |
|
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: 136.79 E-value: 2.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSksEKEL 85
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLP----TSGKVTVDGLDTLD--EENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQDPMSALnpvvkIGKQMTEVI--------IRHQKVKKR--EAqniavnlLKQVGLsspEERVRQYPHE 155
Cdd:TIGR04520 73 WEIR-KKVGMVFQNPDNQF-----VGATVEDDVafglenlgVPREEMRKRvdEA-------LKLVGM---EDFRDREPHL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIA--MAMscNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQnCTRVIVMYGGL 233
Cdd:TIGR04520 137 LSGGQKQRVAIAgvLAM--RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGK 213
|
250
....*....|..
gi 1078707892 234 IMEEGHVLDIFQ 245
Cdd:TIGR04520 214 IVAEGTPREIFS 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-238 |
6.51e-38 |
|
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: 134.18 E-value: 6.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVlSKSEKEL 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER----PDSGEILIDGRDV-TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIrgnqiSLISQDPmsALNPvvkigkQMT--EVI---IRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGGM 160
Cdd:cd03259 72 RNI-----GMVFQDY--ALFP------HLTvaENIafgLKLRGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03259 136 QQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-251 |
2.44e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.38 E-value: 2.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSK 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET----PDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 S-EKelrsiRGnqISLISQDPmsALNPvvkigkQMT--EVI---IRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPH 154
Cdd:COG3842 73 PpEK-----RN--VGMVFQDY--ALFP------HLTvaENVafgLRMRGVPKAEIRARVAELLELVGLEGLADR---YPH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDlgivaQN-----CTRVIVM 229
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD-----QEealalADRIAVM 209
|
250 260
....*....|....*....|..
gi 1078707892 230 YGGLIMEEGHVLDIFQSPNHPY 251
Cdd:COG3842 210 NDGRIEQVGTPEEIYERPATRF 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-246 |
1.33e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.83 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKEGEILFQNENVLS 79
Cdd:PRK13635 1 MKEEIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGMVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 80 ksekelrsIRgNQISLISQDPMsalNPVV-------------KIGKQMTEVIIRHQkvkkrEAqniavnlLKQVGLsspE 146
Cdd:PRK13635 79 --------VR-RQVGMVFQNPD---NQFVgatvqddvafgleNIGVPREEMVERVD-----QA-------LRQVGM---E 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 147 ERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQnCTRV 226
Cdd:PRK13635 132 DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRV 210
|
250 260
....*....|....*....|
gi 1078707892 227 IVMYGGLIMEEGHVLDIFQS 246
Cdd:PRK13635 211 IVMNKGEILEEGTPEEIFKS 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-239 |
2.13e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.56 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 19 DGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKELRSIRgNQISLISQ 98
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE----RPTSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 99 D---------------PMsalnpvvkigkqmtEVIirhqKVKKREAQNIAVNLLKQVGLSspeERVRQYPHELSGGMKQR 163
Cdd:COG2884 87 DfrllpdrtvyenvalPL--------------RVT----GKSRKEIRRRVREVLDLVGLS---DKAKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 164 VMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-234 |
2.53e-36 |
|
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: 128.67 E-value: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKel 85
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL----KPDSGEIKVLGKDIKKEPEE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsIRGNqISLISQDPMSalnpvvkigkqmteviirhqkvkkreaqniavnllkqvglsSPEERVRQYpHELSGGMKQRVM 165
Cdd:cd03230 71 --VKRR-IGYLPEEPSL-----------------------------------------YENLTVREN-LKLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-184 |
3.33e-36 |
|
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: 127.76 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPgkvkEGEILFQNENVLSKSEKELRSirgnQISLISQDPmsAL 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT----EGTILLDGQDLTDDERKSLRK----EIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 105 NPVVKIGKQMTEVIiRHQKVKKREAQNIAVNLLKQVGLSS-PEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPT 183
Cdd:pfam00005 71 FPRLTVRENLRLGL-LLKGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1078707892 184 T 184
Cdd:pfam00005 150 A 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-232 |
4.75e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 127.75 E-value: 4.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 7 EVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPgkvkEGEILFQNENVLSKSEKELR 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT----SGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 sirgNQISLISQdpmsalnpvvkigkqmteviirhqkvkkreaqniavnllkqvglsspeervrqypheLSGGMKQRVMI 166
Cdd:cd00267 73 ----RRIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 167 AMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-243 |
8.48e-36 |
|
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: 129.59 E-value: 8.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGKvkeGEILFQNENVlSKSEKE 84
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLR-MLAGLLKPDS---GSILIDGEDV-RKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSirgnQISLISQDPMSalnPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSspEERVRQYpHELSGGMKQRV 164
Cdd:COG4555 72 ARR----QIGVLPDERGL---YDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLE--EFLDRRV-GELSTGMKKKV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDI 243
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-262 |
2.64e-35 |
|
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: 128.19 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKELRSIRGNQISLIsqdpmsA 103
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP----TSGEIFIDGEDIREQDPVELRRKIGYVIQQI------G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 104 LNPVVKIgKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSsPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPT 183
Cdd:cd03295 86 LFPHMTV-EENIALVPKLLKWPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 184 TALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPYTKGLLNSLPKI 262
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADRLL 242
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-229 |
2.88e-35 |
|
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: 126.15 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPgkvkEGEILFQNENVlSKSEKEL 85
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD----SGSILIDGEDL-TDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQDPmsALNPvvkigkqmteviirHQKVKkreaQNIAvnllkqvglsspeervrqYPheLSGGMKQRVM 165
Cdd:cd03229 72 PPLR-RRIGMVFQDF--ALFP--------------HLTVL----ENIA------------------LG--LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVM 229
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-232 |
3.53e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 3.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVeaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtSPGkvkEGEILFQNENVLSKSEKEL 85
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLD-PPT---SGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSirgnQISLISQDPMSALNPVvkiGKQMTEVIIRHQKVKKREAqniAVNLLKQVGLssPEERVRQYPHELSGGMKQRVM 165
Cdd:COG4619 73 RR----QVAYVPQEPALWGGTV---RDNLPFPFQLRERKFDRER---ALELLERLGL--PPDILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-257 |
1.27e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.79 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfieDGEVeAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK11264 4 IEVKNLVKKF---HGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpEAGTIRVGDITIDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRgNQISLISQD----P-MSALNPVVKigkqmTEVIIRhqKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGG 159
Cdd:PRK11264 80 IRQLR-QHVGFVFQNfnlfPhRTVLENIIE-----GPVIVK--GEPKEEATARARELLAKVGLAGKETS---YPRRLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
250
....*....|....*...
gi 1078707892 240 VLDIFQSPNHPYTKGLLN 257
Cdd:PRK11264 228 AKALFADPQQPRTRQFLE 245
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-227 |
1.57e-34 |
|
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: 125.04 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 8 VKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTSPGKvkeGEILFQNENVLSKSEKELRS 87
Cdd:TIGR03608 1 LKNISKKF----GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLL-NIIGLLEKFDS---GQVYLNGQETPPLNSKKASK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 88 IRGNQISLISQDpmSAL--NPVVKigkQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSpeeRVRQYPHELSGGMKQRVM 165
Cdd:TIGR03608 73 FRREKLGYLFQN--FALieNETVE---ENLDLGLKYKKLSKKEKREKKKEALEKVGLNL---KLKQKIYELSGGEQQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLgIVAQNCTRVI 227
Cdd:TIGR03608 145 LARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-247 |
1.63e-34 |
|
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: 126.01 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTspGKVK--EGEILFQNENVLSKSEK 83
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT----TLFNLIS--GFLRptSGSVLFDGEDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 84 ElRSIRG----NQISLISQDpMSAL-NPVVKIGKQMTEVIIRHQKVKK-REAQNIAVNLLKQVGLSspeERVRQYPHELS 157
Cdd:cd03219 71 E-IARLGigrtFQIPRLFPE-LTVLeNVMVAAQARTGSGLLLARARREeREARERAEELLERVGLA---DLADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
250
....*....|
gi 1078707892 238 GHVLDIFQSP 247
Cdd:cd03219 225 GTPDEVRNNP 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-238 |
1.64e-34 |
|
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: 125.56 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFQNENVLskseKEL 85
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIK----MLTTLLKPTSGRATVAGHDVV----REP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGNqISLISQDPmsALNPVVKiGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEER-VRQYphelSGGMKQRV 164
Cdd:cd03265 69 REVRRR-IGIVFQDL--SVDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRlVKTY----SGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-232 |
3.73e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 122.88 E-value: 3.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKEL 85
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY----DPTSGEILIDGVDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSirgnQISLISQDPmsalnpvvkigkqmtevIIRHQKVkkREaqNIavnllkqvglsspeervrqypheLSGGMKQRVM 165
Cdd:cd03228 75 RK----NIAYVPQDP-----------------FLFSGTI--RE--NI-----------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNetNMSLLLITHDLGIVaQNCTRVIVMYGG 232
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
1.90e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.33 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 2 SEKLLEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKS 81
Cdd:PRK13632 4 KSVMIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL----KPQSGEIKIDGITISKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 EKELRsirgNQISLISQDPMSALnpvvkIGKQMTEVI---IRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSG 158
Cdd:PRK13632 78 LKEIR----KKIGIIFQNPDNQF-----IGATVEDDIafgLENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGiVAQNCTRVIVMYGGLIMEEG 238
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQG 224
|
....*...
gi 1078707892 239 HVLDIFQS 246
Cdd:PRK13632 225 KPKEILNN 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-246 |
2.44e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.09 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSK 80
Cdd:PRK13648 3 DKNSIIVFKNV--SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE----KVKSGEIFYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSirgnQISLISQDPMSALnpVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSspeERVRQYPHELSGGM 160
Cdd:PRK13648 77 NFEKLRK----HIGIVFQNPDNQF--VGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDML---ERADYEPNALSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLgIVAQNCTRVIVMYGGLIMEEGHV 240
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNKGTVYKEGTP 226
|
....*.
gi 1078707892 241 LDIFQS 246
Cdd:PRK13648 227 TEIFDH 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-257 |
2.45e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.54 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtspGKVKEGEILFQNENV--- 77
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL----EKPSEGSIVVNGQTInlv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 ------LSKSEK-ELRSIRgNQISLISQ-----DPMSALNPVVkigkqmtEVIIRHQKVKKREAQNIAVNLLKQVGLssp 145
Cdd:PRK10619 73 rdkdgqLKVADKnQLRLLR-TRLTMVFQhfnlwSHMTVLENVM-------EAPIQVLGLSKQEARERAVKYLAKVGI--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 146 EERVRQ-YPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNmSLLLITHDLGIVAQNCT 224
Cdd:PRK10619 142 DERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSS 220
|
250 260 270
....*....|....*....|....*....|...
gi 1078707892 225 RVIVMYGGLIMEEGHVLDIFQSPNHPYTKGLLN 257
Cdd:PRK10619 221 HVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-234 |
2.98e-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: 121.98 E-value: 2.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 16 FIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtspGKVKEGEILFQNENVlskSEKELRSirgnQISL 95
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL----IKESSGSILLNGKPI---KAKERRK----SIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 96 ISQDPmsalnpvvkiGKQMT------EVIIRHQKVKKREAQniAVNLLKQVGLSSPEERvrqYPHELSGGMKQRVMIAMA 169
Cdd:cd03226 76 VMQDV----------DYQLFtdsvreELLLGLKELDAGNEQ--AETVLKDLDLYALKER---HPLSLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 170 MSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNmSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-238 |
4.03e-33 |
|
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: 129.18 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVlskSEKEL 85
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE----PTSGRILIDGIDL---RQIDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQDPM----SalnpvvkigkqmteviIRhqkvkkreaQNIA-----------VNLLKQVGLsspEERVR 150
Cdd:COG2274 545 ASLR-RQIGVVLQDVFlfsgT----------------IR---------ENITlgdpdatdeeiIEAARLAGL---HDFIE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 151 QYPH-----------ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNetNMSLLLITHDLGIV 219
Cdd:COG2274 596 ALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI 673
|
250
....*....|....*....
gi 1078707892 220 aQNCTRVIVMYGGLIMEEG 238
Cdd:COG2274 674 -RLADRIIVLDKGRIVEDG 691
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-238 |
7.96e-33 |
|
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: 121.52 E-value: 7.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVK-EGEILFQNENVLSKSEK- 83
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPdEGEVLLDGKDIYDLDVDv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 84 -ELRSirgnQISLISQDP----MSALNPVVkIGKQMteviirHQKVKKREAQNIAVNLLKQVGLSsPEERVRQYPHELSG 158
Cdd:cd03260 77 lELRR----RVGMVFQKPnpfpGSIYDNVA-YGLRL------HGIKLKEELDERVEEALRKAALW-DEVKDRLHALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtnMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
6-234 |
1.28e-32 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 120.51 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKEL 85
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT----TLLTLIGGLRSVQEGSLKVLGQELHGASKKQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQ-----DPMSALNPVvkigkQMTevIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGM 160
Cdd:TIGR02982 78 VQLR-RRIGYIFQahnllGFLTARQNV-----QMA--LELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGI--VAqncTRVIVMYGGLI 234
Cdd:TIGR02982 147 KQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRIldVA---DRILQMEDGKL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-256 |
2.98e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.95 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSeklLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTsPGkvkEGEILFQNENVLSK 80
Cdd:COG1118 1 MS---IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLET-PD---SGRIVLNGRDLFTN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 sekelRSIRGNQISLISQDPmsALNPvvkigkQMT--EVI---IRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHE 155
Cdd:COG1118 70 -----LPPRERRVGFVFQHY--ALFP------HMTvaENIafgLRVRPPSKAEIRARVEELLELVQLEGLADR---YPSQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIM 235
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
250 260
....*....|....*....|.
gi 1078707892 236 EEGHVLDIFQSPNHPYTKGLL 256
Cdd:COG1118 214 QVGTPDEVYDRPATPFVARFL 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-229 |
6.40e-32 |
|
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: 119.08 E-value: 6.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFI--EDG-EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMA--LVTSpgkvkeGEILFQNE---- 75
Cdd:COG4778 4 LLEVENLSKTFTLhlQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPDS------GSILVRHDggwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 76 NVLSKSEKELRSIRGNQISLISQ----DP-MSALnpvvkigkqmtEVII---RHQKVKKREAQNIAVNLLKQVGLssPEE 147
Cdd:COG4778 78 DLAQASPREILALRRRTIGYVSQflrvIPrVSAL-----------DVVAeplLERGVDREEARARARELLARLNL--PER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 148 RVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVI 227
Cdd:COG4778 145 LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVV 223
|
..
gi 1078707892 228 VM 229
Cdd:COG4778 224 DV 225
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-247 |
1.96e-31 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 121.36 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 18 EDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKELRSIRGNQISLIS 97
Cdd:COG4175 36 KTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLI----EPTAGEVLIDGEDITKLSKKELRELRRKKMSMVF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 98 QdpmS-ALNPvvkigkQMT---------EViirhQKVKKREAQNIAVNLLKQVGLSSPEErvrQYPHELSGGMKQRVMIA 167
Cdd:COG4175 112 Q---HfALLP------HRTvlenvafglEI----QGVPKAERRERAREALELVGLAGWED---SYPDELSGGMQQRVGLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 168 MAMSCNPDLLIADEPTTALDVTI----QAQILDLMKNLKNetnmSLLLITHDL------GivaqncTRVIVMYGGLIMEE 237
Cdd:COG4175 176 RALATDPDILLMDEAFSALDPLIrremQDELLELQAKLKK----TIVFITHDLdealrlG------DRIAIMKDGRIVQI 245
|
250
....*....|
gi 1078707892 238 GHVLDIFQSP 247
Cdd:COG4175 246 GTPEEILTNP 255
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-238 |
7.50e-31 |
|
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: 118.26 E-value: 7.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEILFQNENVLSKSEKELRSIrgnqiSLISQD 99
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIR-MLTTLLRP---TSGTARVAGYDVVREPRKVRRSI-----GIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 PmsalNPVVKI-GKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLS-SPEERVRQYphelSGGMKQRVMIAMAMSCNPDLL 177
Cdd:TIGR01188 75 A----SVDEDLtGRENLEMMGRLYGLPKDEAEERAEELLELFELGeAADRPVGTY----SGGMRRRLDIAASLIHQPDVL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 178 IADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:TIGR01188 147 FLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-247 |
8.88e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 116.27 E-value: 8.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEILFQNENV-LSK--SE 82
Cdd:COG4161 3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETP---DSGQLNIAGHQFdFSQkpSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSIRGNqISLISQDpmSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGGMKQ 162
Cdd:COG4161 75 KAIRLLRQK-VGMVFQQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHvLD 242
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-AS 226
|
....*
gi 1078707892 243 IFQSP 247
Cdd:COG4161 227 HFTQP 231
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
234-320 |
1.46e-30 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 110.91 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 234 IMEEGHVLDIFQSPNHPYTKGLLNSLPKIsNGVKERLAPIQGVTPNLLHPPKGCPFAERCPHKMDICEKERPPYFEIGNG 313
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPTI-KKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*..
gi 1078707892 314 RRSMCWL 320
Cdd:TIGR01727 81 HRVACHL 87
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-232 |
5.54e-30 |
|
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: 113.50 E-value: 5.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSV-MALVTSpgkvkEGEILFQNENVLSKSEKELRSIRgNQISLISQ 98
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLyGALTPS-----RGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 99 DpmsalnpvVKIGKQMT-----EVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGMKQRVMIAMAMSCN 173
Cdd:TIGR02673 87 D--------FRLLPDRTvyenvALPLEVRGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 174 PDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-256 |
6.18e-30 |
|
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: 113.97 E-value: 6.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGKvkeGEILFQNENVLSKSekel 85
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLR-LIAGLERPDS---GTILFGGEDATDVP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsIRGNQISLISQDpmSALNpvvkigKQMT---------EVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHEL 156
Cdd:cd03296 71 --VQERNVGFVFQH--YALF------RHMTvfdnvafglRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 SGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIME 236
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
250 260
....*....|....*....|
gi 1078707892 237 EGHVLDIFQSPNHPYTKGLL 256
Cdd:cd03296 218 VGTPDEVYDHPASPFVYSFL 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-239 |
7.99e-30 |
|
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: 119.09 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEvEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKEL 85
Cdd:COG4988 337 IELEDV--SFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL----PPYSGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RsirgNQISLISQDPmsalnpvvkigkqmteVIIrhqkvkkreAQNIAVNL---------------LKQVGLsspEERVR 150
Cdd:COG4988 410 R----RQIAWVPQNP----------------YLF---------AGTIRENLrlgrpdasdeeleaaLEAAGL---DEFVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 151 QYPH-------E----LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNL-KNETnmsLLLITHDLGI 218
Cdd:COG4988 458 ALPDgldtplgEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGRT---VILITHRLAL 534
|
250 260
....*....|....*....|.
gi 1078707892 219 VAQnCTRVIVMYGGLIMEEGH 239
Cdd:COG4988 535 LAQ-ADRILVLDDGRIVEQGT 554
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-253 |
9.96e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.85 E-value: 9.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVK-EGEILFQNENVLSKSEKE 84
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRsirgNQISLISQDPmsalNPV--------VKIGKQMTEVIirhqKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHEL 156
Cdd:PRK14247 80 LR----RRVQMVFQIP----NPIpnlsifenVALGLKLNRLV----KSKKELQERVRWALEKAQLWDEVKDRLDAPAGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 SGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtnMSLLLITHDLGIVAQNCTRVIVMYGGLIME 236
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
250
....*....|....*..
gi 1078707892 237 EGHVLDIFQSPNHPYTK 253
Cdd:PRK14247 226 WGPTREVFTNPRHELTE 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-229 |
1.43e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.81 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 2 SEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGkvkEGEILFQNENVlsks 81
Cdd:COG1129 1 AEPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMK-ILSGVYQPD---SGEILLDGEPV---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 ekELRSIRGNQ---ISLISQDpmsaLNPV--------VKIGKQMTeviiRHQKVKKREAQNIAVNLLKQVGLS-SPEERV 149
Cdd:COG1129 69 --RFRSPRDAQaagIAIIHQE----LNLVpnlsvaenIFLGREPR----RGGLIDWRAMRRRARELLARLGLDiDPDTPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 150 RqyphELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVM 229
Cdd:COG1129 139 G----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
1.91e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.63 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiEDGeVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENvLSKSEKE 84
Cdd:PRK13639 1 ILETRDLKYSY--PDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL----KPTSGEVLIKGEP-IKYDKKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRgNQISLISQDPMSAL-NPVVKigkQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVrqyPHELSGGMKQR 163
Cdd:PRK13639 73 LLEVR-KTVGIVFQNPDDQLfAPTVE---EDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 164 VMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDI 243
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
....*
gi 1078707892 244 FQSPN 248
Cdd:PRK13639 225 FSDIE 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-248 |
2.23e-29 |
|
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: 112.43 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLS-KSEKE 84
Cdd:cd03299 1 LKVENLSKDW----KEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI----KPDSGKILLNGKDITNlPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 lrsirgnQISLISQDpmSALNPVVKIGKQMtEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGGMKQRV 164
Cdd:cd03299 72 -------DISYVPQN--YALFPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNR---KPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIF 244
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
....
gi 1078707892 245 QSPN 248
Cdd:cd03299 219 KKPK 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-238 |
2.36e-29 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 111.54 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFqnenvLSKSEKEL 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI----KPDSGEITF-----DGKSYQKN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGNQISLISQ----DPMSALNPVVKIGKQMtevIIRHQKVKKreaqniavnLLKQVGLS-SPEERVRQYphelSGGM 160
Cdd:cd03268 68 IEALRRIGALIEApgfyPNLTARENLRLLARLL---GIRKKRIDE---------VLDVVGLKdSAKKKVKGF----SLGM 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03268 132 KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-253 |
3.20e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.44 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSV--M-ALVtsPG-KVkEGEILFQNENVLSKS 81
Cdd:COG1117 12 IEVRNL--NVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMnDLI--PGaRV-EGEILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 EK--ELRSirgnQISLISQDP----MS-----ALNPvvKIgkqmteviirHQKVKKREAQNIAVNLLKQVGLssPEE--- 147
Cdd:COG1117 85 VDvvELRR----RVGMVFQKPnpfpKSiydnvAYGL--RL----------HGIKSKSELDEIVEESLRKAAL--WDEvkd 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 148 RVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtnMSLLLITHDLgivaQNCTRV- 226
Cdd:COG1117 147 RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNM----QQAARVs 220
|
250 260 270
....*....|....*....|....*....|
gi 1078707892 227 ---IVMYGGLIMEEGHVLDIFQSPNHPYTK 253
Cdd:COG1117 221 dytAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-261 |
3.24e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFfiedgEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALV--TSpGKVKEGEILFQNEnvlsK 80
Cdd:PRK13634 6 QKVEHRYQYKTPF-----ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqpTS-GTVTIGERVITAG----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSIRgNQISLISQDPMSAL--NPVVK---IGKQmteviirHQKVKKREAQNIAVNLLKQVGLssPEERVRQYPHE 155
Cdd:PRK13634 76 KNKKLKPLR-KKVGIVFQFPEHQLfeETVEKdicFGPM-------NFGVSEEDAKQKAREMIELVGL--PEELLARSPFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIM 235
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
250 260
....*....|....*....|....*.
gi 1078707892 236 EEGHVLDIFQSPNHPYTKGLlnSLPK 261
Cdd:PRK13634 226 LQGTPREIFADPDELEAIGL--DLPE 249
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-229 |
3.44e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.83 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGkvkEGEILFQNENVLSKSEKEL 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMK-ILSGLYKPD---SGEILVDGKEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSiRGnqISLISQdpmsalnpvvkigkqmteviirhqkvkkreaqniavnllkqvglsspeervrqypheLSGGMKQRVM 165
Cdd:cd03216 73 RR-AG--IAMVYQ---------------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVM 229
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVL 155
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-237 |
4.76e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 111.45 E-value: 4.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiEDGEV--EAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGkvkeGEILFQNENVL 78
Cdd:PRK11629 1 MNKILLQCDNLCKRY--QEGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS----GDVIFNGQPMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 79 SKSEKELRSIRGNQISLISQ-----DPMSALNPVVkigkqMTEVIirhQKVKKREAQNIAVNLLKQVGLsspEERVRQYP 153
Cdd:PRK11629 75 KLSSAAKAELRNQKLGFIYQfhhllPDFTALENVA-----MPLLI---GKKKPAEINSRALEMLAAVGL---EHRANHRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 154 HELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIvAQNCTRVIVMYGGL 233
Cdd:PRK11629 144 SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL-AKRMSRQLEMRDGR 222
|
....
gi 1078707892 234 IMEE 237
Cdd:PRK11629 223 LTAE 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-232 |
1.39e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.11 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEklLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTSPgkvKEGEILFQNENVLSK 80
Cdd:COG4525 1 MSM--LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLL-NLIAGFLAP---SSGEITLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKelrsiRGnqisLISQDpmSALNP---V---VKIGKQMteviirhQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPH 154
Cdd:COG4525 75 GAD-----RG----VVFQK--DALLPwlnVldnVAFGLRL-------RGVPKAERRARAEELLALVGLADFARR---RIW 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHD------LGivaqncTRVIV 228
Cdd:COG4525 134 QLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSveealfLA------TRLVV 207
|
....
gi 1078707892 229 MYGG 232
Cdd:COG4525 208 MSPG 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-243 |
4.95e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 110.56 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFFIEDG-EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVkegEILFQNENVLSKS-- 81
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLpDTGTI---EWIFKDEKNKKKTke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 -EKELRSIrgnqisLISQDPMSALNPVVKIGKQMTEV----------------II---RHQKVKKREAQNIAVNLLKQVG 141
Cdd:PRK13651 80 kEKVLEKL------VIQKTRFKKIKKIKEIRRRVGVVfqfaeyqlfeqtiekdIIfgpVSMGVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 142 LssPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQ 221
Cdd:PRK13651 154 L--DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLE 230
|
250 260
....*....|....*....|..
gi 1078707892 222 NCTRVIVMYGGLIMEEGHVLDI 243
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDI 252
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-238 |
5.01e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.95 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSeklLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEILFQNENV-LS 79
Cdd:PRK11124 1 MS---IQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMP---RSGTLNIAGNHFdFS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 80 K--SEKELRSIRGNqISLISQDpmSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELS 157
Cdd:PRK11124 70 KtpSDKAIRELRRN-VGMVFQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
.
gi 1078707892 238 G 238
Cdd:PRK11124 223 G 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-244 |
5.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 5.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 2 SEKLLEVKNLKTSFFIEDGEVE--AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKEgeilfqnENVL 78
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIpSEGKVYV-------DGLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 79 SKSEKELRSIRgNQISLISQDPMSALnpVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSspeERVRQYPHELSG 158
Cdd:PRK13633 74 TSDEENLWDIR-NKAGMVFQNPDNQI--VATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMY---EYRRHAPHLLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQnCTRVIVMYGGLIMEEG 238
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
....*.
gi 1078707892 239 HVLDIF 244
Cdd:PRK13633 227 TPKEIF 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-237 |
6.20e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.19 E-value: 6.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSffiedgevEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSE 82
Cdd:COG1129 254 EVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD----PADSGEIRLDGKPVRIRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KElrSIRgNQISLISQD--------PMSalnpvvkIGKQMT----EVIIRHQKVKKREAQNIAVNLLKQVGL--SSPEER 148
Cdd:COG1129 322 RD--AIR-AGIAYVPEDrkgeglvlDLS-------IRENITlaslDRLSRGGLLDRRRERALAEEYIKRLRIktPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 149 VRQypheLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIV 228
Cdd:COG1129 392 VGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILV 466
|
....*....
gi 1078707892 229 MYGGLIMEE 237
Cdd:COG1129 467 MREGRIVGE 475
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-245 |
6.52e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFfiedgEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSE 82
Cdd:PRK13637 6 ENLTHIYMEGTPF-----EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL----KPTSGKIIIDGVDITDKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KeLRSIRgNQISLISQDPMSAL--NPVVK-IGKQMTEVIIRHQKVKKR--EAQNIavnllkqVGLSSpEERVRQYPHELS 157
Cdd:PRK13637 77 K-LSDIR-KKVGLVFQYPEYQLfeETIEKdIAFGPINLGLSEEEIENRvkRAMNI-------VGLDY-EDYKDKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
....*...
gi 1078707892 238 GHVLDIFQ 245
Cdd:PRK13637 227 GTPREVFK 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-238 |
1.04e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.34 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 19 DGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSKSEKELRSirgnQISLISQ 98
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD----PTSGRILIDGVDIRDLTLESLRR----QIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 99 DP----MSAL-NpvVKIGKQ---MTEVIirhqkvkkrEAqniavnlLKQVGLsspEERVRQYPH-----------ELSGG 159
Cdd:COG1132 422 DTflfsGTIReN--IRYGRPdatDEEVE---------EA-------AKAAQA---HEFIEALPDgydtvvgergvNLSGG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDV----TIQAQILDLMKnlknetNMSLLLITHDLGIVaQNCTRVIVMYGGLIM 235
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTeteaLIQEALERLMK------GRTTIVIAHRLSTI-RNADRILVLDDGRIV 553
|
...
gi 1078707892 236 EEG 238
Cdd:COG1132 554 EQG 556
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-269 |
1.35e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.73 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTsPGKVKEGEILFQNENVLSK 80
Cdd:PRK13640 1 MKDNIVEFKHV--SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLL-PDDNPNSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRsirgNQISLISQDPMSALnpvvkIGKQMTEVI---IRHQKVKKREAQNIAVNLLKQVGLSspeERVRQYPHELS 157
Cdd:PRK13640 78 TVWDIR----EKVGIVFQNPDNQF-----VGATVGDDVafgLENRAVPRPEMIKIVRDVLADVGML---DYIDSEPANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGiVAQNCTRVIVMYGGLIMEE 237
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQ 224
|
250 260 270
....*....|....*....|....*....|....*
gi 1078707892 238 GHVLDIFQSPNHPYTKGLlnSLP---KISNGVKER 269
Cdd:PRK13640 225 GSPVEIFSKVEMLKEIGL--DIPfvyKLKNKLKEK 257
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-237 |
1.37e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 107.56 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 2 SEKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKS 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS----TLLAILAGLDDGSSGEVSLVGQPLHQMD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 EKELRSIRGNQISLISQDPM--SALNPVVKIgkQMTeVIIRHQKvkKREAQNIAVNLLKQVGLsspEERVRQYPHELSGG 159
Cdd:PRK10584 79 EEARAKLRAKHVGFVFQSFMliPTLNALENV--ELP-ALLRGES--SRQSRNGAKALLEQLGL---GKRLDHLPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQnCTRVIVMYGGLIMEE 237
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-232 |
2.35e-27 |
|
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: 105.59 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSffiedgevEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSE 82
Cdd:cd03215 2 EPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR----PPASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSiRGnqISLISQDPMSalnpvvkigkqmtEVIIRHQKVkkreAQNIAVNLLkqvglsspeervrqypheLSGGMKQ 162
Cdd:cd03215 70 RDAIR-AG--IAYVPEDRKR-------------EGLVLDLSV----AENIALSSL------------------LSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-247 |
2.93e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 108.64 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 19 DGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALV--TSpgkvkeGEILFQNENVLSKSEKELRsiRG-----N 91
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIepTS------GRILIDGEDIRDLDPVELR--RRigyviQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 92 QISLIsqdpmsalnPvvkigkQMT-----EVIIRHQKVKKREAQNIAVNLLKQVGLSsPEERVRQYPHELSGGMKQRVMI 166
Cdd:COG1125 84 QIGLF---------P------HMTvaeniATVPRLLGWDKERIRARVDELLELVGLD-PEEYRDRYPHELSGGQQQRVGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 167 AMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHD------LGivaqncTRVIVMYGGLIMEEGHV 240
Cdd:COG1125 148 ARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDidealkLG------DRIAVMREGRIVQYDTP 221
|
....*..
gi 1078707892 241 LDIFQSP 247
Cdd:COG1125 222 EEILANP 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-253 |
3.20e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.12 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSF---------FIEDGEVE-----------AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKV 65
Cdd:PRK10070 5 LEIKNLYKIFgehpqrafkYIEQGLSKeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI----EP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 66 KEGEILFQNENVLSKSEKELRSIRGNQISLISQDpmSALNPVVKIGKQmTEVIIRHQKVKKREAQNIAVNLLKQVGLssp 145
Cdd:PRK10070 81 TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FALMPHMTVLDN-TAFGMELAGINAEERREKALDALRQVGL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 146 EERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTR 225
Cdd:PRK10070 155 ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDR 234
|
250 260
....*....|....*....|....*...
gi 1078707892 226 VIVMYGGLIMEEGHVLDIFQSPNHPYTK 253
Cdd:PRK10070 235 IAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-238 |
4.71e-27 |
|
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: 106.47 E-value: 4.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 21 EVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKELRSirgnQISLISQDP 100
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRS----QIGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 101 MSALNPV---VKIGK---QMTEVIirhQKVKKREAQNIAVNLLKQVglsspEERVRQYPHELSGGMKQRVMIAMAMSCNP 174
Cdd:cd03249 87 VLFDGTIaenIRYGKpdaTDEEVE---EAAKKANIHDFIMSLPDGY-----DTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 175 DLLIADEPTTALDV----TIQAQILDLMKnlknetNMSLLLITHDLGIVaQNCTRVIVMYGGLIMEEG 238
Cdd:cd03249 159 KILLLDEATSALDAesekLVQEALDRAMK------GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-262 |
6.27e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 108.62 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEklLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSK 80
Cdd:COG3839 1 MAS--LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLED----PTSGEILIGGRDVTDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKElrsiRGnqISLISQDPmsALNPvvkigkqmteviirHQKVkkreAQNIAVNLlKQVGLSSPE--ERVRQ------- 151
Cdd:COG3839 71 PPKD----RN--IAMVFQSY--ALYP--------------HMTV----YENIAFPL-KLRKVPKAEidRRVREaaellgl 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 152 ------YPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHD------LGiv 219
Cdd:COG3839 124 edlldrKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA-- 201
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1078707892 220 aqncTRVIVMYGGLIMEEGHVLDIFQSPNHPYTKGLLNSlPKI 262
Cdd:COG3839 202 ----DRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGS-PPM 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-238 |
6.53e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 110.63 E-value: 6.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKEL 85
Cdd:COG4987 334 LELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL----DPQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSirgnQISLISQDP----MSAL-NpvVKIGK------QMTEViirhqkvkkreaqniavnlLKQVGLsspEERVRQYPH 154
Cdd:COG4987 408 RR----RIAVVPQRPhlfdTTLReN--LRLARpdatdeELWAA-------------------LERVGL---GDWLAALPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 -------E----LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQIL-DLMKNLKNETnmsLLLITHDLGIVAQn 222
Cdd:COG4987 460 gldtwlgEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALAGRT---VLLITHRLAGLER- 535
|
250
....*....|....*.
gi 1078707892 223 CTRVIVMYGGLIMEEG 238
Cdd:COG4987 536 MDRILVLEDGRIVEQG 551
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-234 |
1.93e-26 |
|
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: 104.03 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKELRSIRgNQISLISQD 99
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP----TSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 P--MSALNPVVKIGKQMTEVIIRHQKVKKREAQniavnLLKQVGLSSpeeRVRQYPHELSGGMKQRVMIAMAMSCNPDLL 177
Cdd:cd03292 87 FrlLPDRNVYENVAFALEVTGVPPREIRKRVPA-----ALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 178 IADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-262 |
2.11e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.63 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 21 EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKEGEILFQNENvlskSEKELRSIRgNQISLISQD 99
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITITHKT----KDKYIRPVR-KRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 PMSAL--NPVVKigkqmtEVII--RHQKVKKREAQNIAVNLLKQVGLssPEERVRQYPHELSGGMKQRVMIAMAMSCNPD 175
Cdd:PRK13646 94 PESQLfeDTVER------EIIFgpKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 176 LLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNhpYTKGL 255
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK--KLADW 243
|
....*..
gi 1078707892 256 LNSLPKI 262
Cdd:PRK13646 244 HIGLPEI 250
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-256 |
2.52e-26 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 104.50 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtspGKVKEGEILFQNENVLSKSekel 85
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGL----EQPDSGRIRLNGQDATRVH---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsIRGNQISLISQDpmSALNPVVKIGKQMT--EVIIRHQKVKKREAQNiavNLLKQVGLSSPEERvrqYPHELSGGMKQR 163
Cdd:TIGR00968 69 --ARDRKIGFVFQH--YALFKHLTVRDNIAfgLEIRKHPKAKIKARVE---ELLELVQLEGLGDR---YPNQLSGGQRQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 164 VMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDI 243
Cdd:TIGR00968 139 VALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
250
....*....|...
gi 1078707892 244 FQSPNHPYTKGLL 256
Cdd:TIGR00968 219 YDHPANPFVMSFL 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-268 |
3.55e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.17 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 4 KLLEVKNLKTSFFiEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEK 83
Cdd:PRK13642 3 KILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE----FEGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 84 ELRsirgNQISLISQDP-----MSALNPVVKIGKQmTEVIIRHQKVKKREAQNIAVNLLkqvglsspEERVRQyPHELSG 158
Cdd:PRK13642 78 NLR----RKIGMVFQNPdnqfvGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNML--------DFKTRE-PARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNcTRVIVMYGGLIMEEG 238
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASS-DRILVMKAGEIIKEA 222
|
250 260 270
....*....|....*....|....*....|
gi 1078707892 239 HVLDIFQSPNHPYTKGLlnSLPKISNGVKE 268
Cdd:PRK13642 223 APSELFATSEDMVEIGL--DVPFSSNLMKD 250
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-232 |
4.18e-26 |
|
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: 103.13 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNenvlskseKEL 85
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII----LPDSGEVLFDG--------KPL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGNQISLISQDpmSALNPVVKIGKQMTeVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQyphELSGGMKQRVM 165
Cdd:cd03269 65 DIAARNRIGYLPEE--RGLYPKMKVIDQLV-YLAQLKGLKKEEARRRIDEWLERLELSEYANKRVE---ELSKGNQQKVQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELA-RAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-232 |
4.18e-26 |
|
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: 103.14 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 29 SFSLK-----KGEVVGIVGESGSGKSVMAKSVMALVTSPGkvkeGEILFqNENVLSKSEKELR-SIRGNQISLISQDpmS 102
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDG----GTIVL-NGTVLFDSRKKINlPPQQRKIGLVFQQ--Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 103 ALNPVVKIGKQMTEVIIRHQKVKKReaqnIAVNllKQVGLSSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEP 182
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNREDR----ISVD--ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1078707892 183 TTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-238 |
5.57e-26 |
|
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: 102.90 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEkEL 85
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL----PPRSGSIRFDGRDITGLPP-HE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGnqISLISQD-----PMSalnpvVKIGKQMTEVIIRHQKVKKREAQniAVNL---LKqvglsspeERVRQYPHELS 157
Cdd:cd03224 72 RARAG--IGYVPEGrrifpELT-----VEENLLLGAYARRRAKRKARLER--VYELfprLK--------ERRKQLAGTLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:cd03224 135 GGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
.
gi 1078707892 238 G 238
Cdd:cd03224 214 G 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-256 |
1.60e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.14 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 29 SFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKElrsiRGnqISLISQD----P-MS- 102
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS----TLLNLIAGFLPPDSGRILWNGQDLTALPPAE----RP--VSMLFQEnnlfPhLTv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 103 ------ALNPVVKIGKQmteviirhQKVKKREAqniavnlLKQVGLSSPEERvrqYPHELSGGMKQRVMIAMAMSCNPDL 176
Cdd:COG3840 89 aqniglGLRPGLKLTAE--------QRAQVEQA-------LERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 177 LIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPYTKGLL 256
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
1.78e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiEDGeVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVlSK 80
Cdd:PRK13636 1 MEDYILKVEELNYNY--SDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL----KPSSGRILFDGKPI-DY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSIRGNqISLISQDPMSALNPVVKIgkQMTEVIIRHQKVKKREAQNIAVNLLKQVGLsspeERVRQYP-HELSGG 159
Cdd:PRK13636 73 SRKGLMKLRES-VGMVFQDPDNQLFSASVY--QDVSFGAVNLKLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....*
gi 1078707892 240 VLDIF 244
Cdd:PRK13636 226 PKEVF 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-237 |
1.97e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTsffIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSE 82
Cdd:COG3845 255 EVVLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLR----PPASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSiRGnqISLISQDP--------MSALNPVVkIGKQMTEVIIRHQKVKKREAQNIAVNLLKQ--VGLSSPEERVRQy 152
Cdd:COG3845 328 RERRR-LG--VAYIPEDRlgrglvpdMSVAENLI-LGRYRRPPFSRGGFLDRKAIRAFAEELIEEfdVRTPGPDTPARS- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 153 pheLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:COG3845 403 ---LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEG 478
|
....*
gi 1078707892 233 LIMEE 237
Cdd:COG3845 479 RIVGE 483
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-238 |
3.23e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFF-IEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVkegEILFQNENV-LS 79
Cdd:TIGR03269 277 EPIIKVRNVSKRYIsVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEV---NVRVGDEWVdMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 80 KSEKELRSIRGNQISLISQDpmSALNPVVKIGKQMTEVIirHQKVKKREAQNIAVNLLKQVGLSS--PEERVRQYPHELS 157
Cdd:TIGR03269 354 KPGPDGRGRAKRYIGILHQE--YDLYPHRTVLDNLTEAI--GLELPDELARMKAVITLKMVGFDEekAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
.
gi 1078707892 238 G 238
Cdd:TIGR03269 510 G 510
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-248 |
4.77e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 101.35 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLktSFFIedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTspGKVK--EGEILFQNENVLSKSE 82
Cdd:COG4559 1 MLEAENL--SVRL--GGRTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLT--GELTpsSGEVRLNGRPLAAWSP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSIRGnqisLISQDpmSALN-P-----VVKIGKqmteviIRHQKVKKREAQnIAVNLLKQVGLSSPEERvrQYPhEL 156
Cdd:COG4559 71 WELARRRA----VLPQH--SSLAfPftveeVVALGR------APHGSSAAQDRQ-IVREALALVGLAHLAGR--SYQ-TL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 SGGMKQRVMIAMAM-----SCNPD--LLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVM 229
Cdd:COG4559 135 SGGEQQRVQLARVLaqlwePVDGGprWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLL 213
|
250
....*....|....*....
gi 1078707892 230 YGGLIMEEGHVLDIFQSPN 248
Cdd:COG4559 214 HQGRLVAQGTPEEVLTDEL 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-238 |
7.12e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.53 E-value: 7.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSffIEDGEVeaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAlvtSPG-KVKEGEILFQNENVLSKSEKE 84
Cdd:COG0396 1 LEIKNLHVS--VEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG---HPKyEVTSGSILLDGEDILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 lRSIRGnqISLISQDPM------------SALNpvvkigkqmtevIIRHQKVKKREAQNIAVNLLKQVGLssPEERVRQY 152
Cdd:COG0396 74 -RARAG--IFLAFQYPVeipgvsvsnflrTALN------------ARRGEELSAREFLKLLKEKMKELGL--DEDFLDRY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 153 PHE-LSGGMKQRVMIA-MAMsCNPDLLIADEPTTALDV-TIQAqILDLMKNLKNEtNMSLLLITH-----DLgIVAqncT 224
Cdd:COG0396 137 VNEgFSGGEKKRNEILqMLL-LEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDY-IKP---D 209
|
250
....*....|....
gi 1078707892 225 RVIVMYGGLIMEEG 238
Cdd:COG0396 210 FVHVLVDGRIVKSG 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-248 |
8.43e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSK-SEKELRSIRgNQISLISQDPMSAL-- 104
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALL----KPSSGTITIAGYHITPEtGNKNLKKLR-KKVSLVFQFPEAQLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 105 NPVVKigkqMTEVIIRHQKVKKREAQNIAVNLLKQVGLSspEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTT 184
Cdd:PRK13641 101 NTVLK----DVEFGPKNFGFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 185 ALDVTIQAQILDLMKNLKNETNmSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPN 248
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-248 |
1.02e-24 |
|
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: 100.00 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSKSEKEl 85
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET----PTSGEILLDGKDITNLPPHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsirgNQISLISQDpmSALNPVVKIgkqmTEVI---IRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGGMKQ 162
Cdd:cd03300 72 -----RPVNTVFQN--YALFPHLTV----FENIafgLRLKKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLD 242
Cdd:cd03300 138 RVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
....*.
gi 1078707892 243 IFQSPN 248
Cdd:cd03300 218 IYEEPA 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-215 |
1.26e-24 |
|
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: 99.09 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKS----VMAKSVMALvtspgkvkEGEILFQNENvLSK 80
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTtllrILAGLLPPS--------AGEVLWNGEP-IRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSirgnQISLISQDPmsALNPvvkigkQMT--EVIIRHQKVKKREAQNIAVN-LLKQVGLsspEERVRQYPHELS 157
Cdd:COG4133 69 AREDYRR----RLAYLGHAD--GLKP------ELTvrENLRFWAALYGLRADREAIDeALEAVGL---AGLADLPVRQLS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMsLLLITHD 215
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-251 |
1.53e-24 |
|
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: 102.11 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPgkvkEGEILFQNENVLSKSEKELRSIRGNQISLISQDpmSALNPv 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD----EGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 108 vkigkqmteviirHQKVKKreaqniavNLLKQVGLSSPEER----------------VRQYPHELSGGMKQRVMIAMAMS 171
Cdd:TIGR02142 89 -------------HLSVRG--------NLRYGMKRARPSERrisferviellgighlLGRLPGRLSGGEKQRVAIGRALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 172 CNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPY 251
Cdd:TIGR02142 148 SSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-232 |
1.98e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.47 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtsPGKVKEGEILFQNEnvlsk 80
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY--PHGTYEGEIIFEGE----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 sEKELRSIRGNQ---ISLISQDPMsalnpVVkigKQMT--EVI-----IRHQKVKKREAQNI-AVNLLKQVGLS-SPEER 148
Cdd:PRK13549 70 -ELQASNIRDTEragIAIIHQELA-----LV---KELSvlENIflgneITPGGIMDYDAMYLrAQKLLAQLKLDiNPATP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 149 VRQYphelSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIV 228
Cdd:PRK13549 141 VGNL----GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICV 215
|
....
gi 1078707892 229 MYGG 232
Cdd:PRK13549 216 IRDG 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-238 |
3.15e-24 |
|
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: 98.84 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFQNENVLSKSEKEL 85
Cdd:cd03253 1 IEFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR----LLFRFYDVSSGSILIDGQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSirgnQISLISQDpMSALNPVVKIGkqmteviIRHQKVKKREAQNIAVNLLKQVglsspEERVRQYPH----------- 154
Cdd:cd03253 74 RR----AIGVVPQD-TVLFNDTIGYN-------IRYGRPDATDEEVIEAAKAAQI-----HDKIMRFPDgydtivgergl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILD-LMKNLKNETnmsLLLITHDLGIVAqNCTRVIVMYGGL 233
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAaLRDVSKGRT---TIVIAHRLSTIV-NADKIIVLKDGR 212
|
....*
gi 1078707892 234 IMEEG 238
Cdd:cd03253 213 IVERG 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-238 |
4.35e-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: 97.96 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKEL 85
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKT----TTLKMLTGELRPTSGTAYINGYSIRTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIrgnqiSLISQDPM--SALNPvvkigKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGGMKQR 163
Cdd:cd03263 75 QSL-----GYCPQFDAlfDELTV-----REHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANK---RARTLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 164 VMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKneTNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-235 |
5.85e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.49 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGCLDKPTSGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQISLISQ--DPMSALNpvvkiGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGMKQ 162
Cdd:PRK10535 80 LAQLRREHFGFIFQryHLLSHLT-----AAQNVEVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQnCTRVIVMYGGLIM 235
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-238 |
6.89e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLktSFFIedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK13548 2 MLEARNL--SVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALSGELSPDSGEVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRG--NQISLISQdPMSALNpVVKIGkqmtevIIRHQKVKKrEAQNIAVNLLKQVGLSSPEERvrQYPhELSGGMKQ 162
Cdd:PRK13548 74 LARRRAvlPQHSSLSF-PFTVEE-VVAMG------RAPHGLSRA-EDDALVAAALAQVDLAHLAGR--DYP-QLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 163 RVMIAMAM----SCNPD--LLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIME 236
Cdd:PRK13548 142 RVQLARVLaqlwEPDGPprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
..
gi 1078707892 237 EG 238
Cdd:PRK13548 222 DG 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-232 |
8.14e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.65 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFFiEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVlskSE 82
Cdd:PRK13650 2 SNIIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL----EAESGQIIIDGDLL---TE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSIRgNQISLISQDPMSALnpvvkIGKQMTEVI--------IRHQKVKKREAQniAVNLlkqVGLSSPEERvrqYPH 154
Cdd:PRK13650 74 ENVWDIR-HKIGMVFQNPDNQF-----VGATVEDDVafglenkgIPHEEMKERVNE--ALEL---VGMQDFKER---EPA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNcTRVIVMYGG 232
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALS-DRVLVMKNG 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-245 |
1.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.28 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 21 EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAL-VTSPGKVKEGEILFQNENVlsksEKELRSIRgNQISLISQD 99
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPTQGSVRVDDTLITSTSK----NKDIKQIR-KKVGLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 PMSAL--NPVVKigkqmtEVIIRHQK--VKKREAQNIAVNLLKQVGLSspEERVRQYPHELSGGMKQRVMIAMAMSCNPD 175
Cdd:PRK13649 94 PESQLfeETVLK------DVAFGPQNfgVSQEEAEALAREKLALVGIS--ESLFEKNPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 176 LLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQ 245
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
28-268 |
1.15e-23 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 99.68 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVkeGEILFQNENVLSKSEKElrsiRGnqISLISQDpmSALNPV 107
Cdd:TIGR03258 24 LSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLT--GRIAIADRDLTHAPPHK----RG--LALLFQN--YALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 108 VKIGKQMTeVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALD 187
Cdd:TIGR03258 94 LKVEDNVA-FGLRAQKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 188 VTIQAQILDLMKNLKNE-TNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPYTK---GLLNSLPKIS 263
Cdd:TIGR03258 170 ANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAeflGAANILPAIA 249
|
....*
gi 1078707892 264 NGVKE 268
Cdd:TIGR03258 250 LGITE 254
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-261 |
1.25e-23 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 99.34 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGkvkeGEIlFQNENVLSKSEKEL 85
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTA----GTI-YQGGRDITRLPPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIrgnqiSLISQDpmSALNPVVKIGKQMtEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEervRQYPHELSGGMKQRVM 165
Cdd:TIGR03265 76 RDY-----GIVFQS--YALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGGQQQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQ 245
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYR 224
|
250
....*....|....*....
gi 1078707892 246 SPNHPYTK---GLLNSLPK 261
Cdd:TIGR03265 225 HPATPFVAdfvGEVNWLPG 243
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
235-300 |
1.44e-23 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 91.69 E-value: 1.44e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 235 MEEGHVLDIFQSPNHPYTKGLLNSLPKISNGvKERLAPIQGVTPNLLHPPKGCPFAERCPHKMDIC 300
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPP-KRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
1.98e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK13652 3 LIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL----KPTSGSVLIRGEPITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGnqisLISQDPMSAL-NPVVK--IGKQMTEVIIRHQKVKKREAQniavnLLKQVGLSSPEERVrqyPHELSGGMK 161
Cdd:PRK13652 76 VRKFVG----LVFQNPDDQIfSPTVEqdIAFGPINLGLDEETVAHRVSS-----ALHMLGLEELRDRV---PHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 162 QRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVL 241
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
....*..
gi 1078707892 242 DIFQSPN 248
Cdd:PRK13652 224 EIFLQPD 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-238 |
1.99e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 96.14 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 7 EVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKELR 86
Cdd:cd03254 4 EFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKT----TLINLLMRFYDPQKGQILIDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 sirgNQISLISQDP------------MSALNPvvkigkQMTEVIIRHQKVKkreAQNIAVNLLKqvGLsspEERVRQYPH 154
Cdd:cd03254 77 ----SMIGVVLQDTflfsgtimenirLGRPNA------TDEEVIEAAKEAG---AHDFIMKLPN--GY---DTVLGENGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDV----TIQAQILDLMKNlknetnMSLLLITHDLGIVaQNCTRVIVMY 230
Cdd:cd03254 139 NLSQGERQLLAIARAMLRDPKILILDEATSNIDTetekLIQEALEKLMKG------RTSIIIAHRLSTI-KNADKILVLD 211
|
....*...
gi 1078707892 231 GGLIMEEG 238
Cdd:cd03254 212 DGKIIEEG 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-238 |
2.00e-23 |
|
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: 95.72 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGeVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEILFQNENVLsKSEKEL 85
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMR-ILATLTPP---SSGTIRIDGQDVL-KQPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIrgnqISLISQDPMsalnpvvkIGKQMT-----EVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGGM 160
Cdd:cd03264 71 RRR----IGYLPQEFG--------VYPNFTvreflDYIAWLKGIPSKEVKARVDEVLELVNL---GDRAKKKIGSLSGGM 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKneTNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-245 |
2.83e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.30 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEIlfqnenvlsksekelrSIRGNQISLIsqD 99
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLK-LIAGILEP---TSGRV----------------EVNGRVSALL--E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 PMSALNPvvkigkQMTeviirhqkvkKREaqNIAVN--LLkqvGLSSPEER-------------------VRQYphelSG 158
Cdd:COG1134 95 LGAGFHP------ELT----------GRE--NIYLNgrLL---GLSRKEIDekfdeivefaelgdfidqpVKTY----SS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228
|
....*..
gi 1078707892 239 HVLDIFQ 245
Cdd:COG1134 229 DPEEVIA 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-238 |
2.89e-23 |
|
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: 95.29 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKtsffIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtsPG-KVKEGEILFQNENVLSKSEKE 84
Cdd:cd03217 1 LEIKDLH----VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH---PKyEVTEGEILFKGEDITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 lRSIRGnqISLISQDPMSAlnPVVKIGkqmteviirhqkvkkreaqniavNLLKQVGLSspeervrqypheLSGGMKQRV 164
Cdd:cd03217 74 -RARLG--IFLAFQYPPEI--PGVKNA-----------------------DFLRYVNEG------------FSGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQ-NCTRVIVMYGGLIMEEG 238
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYiKPDRVHVLYDGRIVKSG 187
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-232 |
2.94e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTsPgkvKEGEILFQNENVLSK 80
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ-P---DSGEILIDGKPVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKElrSIR-GnqISLISQDPMsaLNPVvkigkqMT--EVII------RHQKVKKREAQNIAVNLLKQVGLS-SPEERVr 150
Cdd:COG3845 73 SPRD--AIAlG--IGMVHQHFM--LVPN------LTvaENIVlgleptKGGRLDRKAARARIRELSERYGLDvDPDAKV- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 151 qypHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALdvTIQ--AQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIV 228
Cdd:COG3845 140 ---EDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTV 213
|
....
gi 1078707892 229 MYGG 232
Cdd:COG3845 214 LRRG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-247 |
3.40e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.61 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLkTSFFIE--DGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSP-GKVKEGEI--------LFQ 73
Cdd:PRK13631 21 ILRVKNL-YCVFDEkqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKyGTIQVGDIyigdkknnHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 74 NENVLSKSEKELRSIRgNQISLISQDPMSALNpvvkigKQMTEVIIRHQ----KVKKREAQNIAVNLLKQVGLSSPeeRV 149
Cdd:PRK13631 100 ITNPYSKKIKNFKELR-RRVSMVFQFPEYQLF------KDTIEKDIMFGpvalGVKKSEAKKLAKFYLNKMGLDDS--YL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 150 RQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVM 229
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVM 249
|
250
....*....|....*...
gi 1078707892 230 YGGLIMEEGHVLDIFQSP 247
Cdd:PRK13631 250 DKGKILKTGTPYEIFTDQ 267
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-238 |
3.74e-23 |
|
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: 95.29 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 18 EDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEIlfqnenvlsksekelrSIRGNQISLIs 97
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLR-LLAGIYPP---DSGTV----------------TVRGRVSSLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 98 qDPMSALNPvvkigkQMTeviirhqkvkKREaqNIAVNLLKQvGLSSPE-------------------ERVRQYphelSG 158
Cdd:cd03220 90 -GLGGGFNP------ELT----------GRE--NIYLNGRLL-GLSRKEidekideiiefselgdfidLPVKTY----SS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-238 |
4.41e-23 |
|
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: 95.38 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVlskSEKEL 85
Cdd:cd03251 1 VEFKNV--TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDV---RDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQDpmsalnpvvkigkqmteVIIRHQKVkkreAQNIAVNLLkqvglSSPEERVRQ-----YPHE----- 155
Cdd:cd03251 72 ASLR-RQIGLVSQD-----------------VFLFNDTV----AENIAYGRP-----GATREEVEEaaraaNAHEfimel 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 --------------LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVT----IQAQILDLMKnlknetNMSLLLITHDLG 217
Cdd:cd03251 125 pegydtvigergvkLSGGQRQRIAIARALLKDPPILILDEATSALDTEserlVQAALERLMK------NRTTFVIAHRLS 198
|
250 260
....*....|....*....|.
gi 1078707892 218 IVaQNCTRVIVMYGGLIMEEG 238
Cdd:cd03251 199 TI-ENADRIVVLEDGKIVERG 218
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
6-237 |
4.60e-23 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 95.96 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFqNENVLSKSekel 85
Cdd:NF040729 2 LKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKT----TLLTIIAGFQNATSGEILV-NGNEVTKP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsirGNQISLISQDpmSALNPVVKIGKQMtEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEervRQYPHELSGGMKQRVM 165
Cdd:NF040729 73 ----GPDRGFVFQN--YALFPWMTVKENI-EYPMKQQKMPKQEREKRLNELLEMAQLTGKE---NLYPHQISGGMKQRTA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMY--GGLIMEE 237
Cdd:NF040729 143 VIRALACKPEVLLMDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSrdKGKILED 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-240 |
7.37e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.56 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFQNENVLSKSEKELRSIRgNQISLISQD 99
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLK----LICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 PMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAvnlLKQVGLSspeERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIA 179
Cdd:PRK10908 88 HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAA---LDKVGLL---DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 180 DEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLiMEEGHV 240
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGH-LHGGVG 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-253 |
1.10e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 15 FFIEDGEVeaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALV-TSPGKVK-EGEILFQNENVLSKSEKELRsirgNQ 92
Cdd:PRK14246 18 LYINDKAI--LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeIYDSKIKvDGKVLYFGKDIFQIDAIKLR----KE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 93 ISLISQDPMSAlnPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGL-SSPEERVRQYPHELSGGMKQRVMIAMAMS 171
Cdd:PRK14246 92 VGMVFQQPNPF--PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 172 CNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtnMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPY 251
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
..
gi 1078707892 252 TK 253
Cdd:PRK14246 248 TE 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-247 |
1.39e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTsPGKvkeGEILFQNENVLSKSEKEL 85
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-PTA---GTVLVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsirGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQNIAVN-LLKQVGLSSPEERVRQyphELSGGMKQRV 164
Cdd:PRK09536 76 ----SRRVASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVT---SLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLItHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIF 244
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
...
gi 1078707892 245 QSP 247
Cdd:PRK09536 228 TAD 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
1.53e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLktSFFIEDGeVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSKSE 82
Cdd:PRK13647 2 DNIIEVEDL--HFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYL----PQRGRVKVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSirgnQISLISQDP-----MSALNPVVKIGKQmteviirHQKVKKREAQNIAVNLLKQVGLSSPEERVrqyPHELS 157
Cdd:PRK13647 75 KWVRS----KVGLVFQDPddqvfSSTVWDDVAFGPV-------NMGLDKDEVERRVEEALKAVRMWDFRDKP---PYHLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:PRK13647 141 YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
.
gi 1078707892 238 G 238
Cdd:PRK13647 220 G 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-245 |
1.60e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKEGEILFQNenvlSKSEKELRSIRgNQISLISQDPMS 102
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSS----TSKQKEIKPVR-KKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 103 AL--NPVVKigkqmtEVIIRHQK--VKKREAQNIAVNLLKQVGLSspEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLI 178
Cdd:PRK13643 96 QLfeETVLK------DVAFGPQNfgIPKEKAEKIAAEKLEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 179 ADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQ 245
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-247 |
1.68e-22 |
|
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: 96.32 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPgkvkEGEILFqNENVLSKSEK------ELRsirgnQISLISQDPm 101
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD----SGRIRL-GGEVLQDSARgiflppHRR-----RIGYVFQEA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 102 sALNPvvkigkqmteviirHQKVKKreaqniavNLL-------KQVGLSSPEERV---------RQYPHELSGGMKQRVM 165
Cdd:COG4148 87 -RLFP--------------HLSVRG--------NLLygrkrapRAERRISFDEVVellgighllDRRPATLSGGERQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQ 245
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
..
gi 1078707892 246 SP 247
Cdd:COG4148 224 RP 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-229 |
1.96e-22 |
|
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: 97.74 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKEL 85
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKS----TLLNLLLGFVDPTEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSirgnQISLISQDPmsalnpvvkigkQMTEVIIrhqkvkkreAQNIA-----------VNLLKQVGLSSPEERVRQY-- 152
Cdd:TIGR02857 395 RD----QIAWVPQHP------------FLFAGTI---------AENIRlarpdasdaeiREALERAGLDEFVAALPQGld 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 153 ------PHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNetNMSLLLITHDLGIVAqNCTRV 226
Cdd:TIGR02857 450 tpigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRI 526
|
...
gi 1078707892 227 IVM 229
Cdd:TIGR02857 527 VVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-232 |
2.33e-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: 91.89 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGKvkeGEILFQNENVLSKSEKEL 85
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLAR-LILGLLRPTS---GRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIrgnqislisqdpmsalnpvvkIGKQMTEVIIRHQKVkkreAQNIavnllkqvglsspeervrqypheLSGGMKQRVM 165
Cdd:cd03246 75 GDH---------------------VGYLPQDDELFSGSI----AENI-----------------------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQnCTRVIVMYGG 232
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-238 |
2.44e-22 |
|
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: 93.20 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtSPGKvkeGEILFQNENVlSKSEKE 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL-EPDA---GFATVDGFDV-VKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSirgnQISLISQ-----DPMSAlnpvvkigKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGG 159
Cdd:cd03266 76 ARR----RLGFVSDstglyDRLTA--------RENLEYFAGLYGLKGDELTARLEELADRLGM---EELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-248 |
2.60e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.56 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEK-LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLS 79
Cdd:PRK11432 1 MTQKnFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLVAGLEKPTEGQIFIDGEDVTH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 80 ksekelRSIRGNQISLISQDpmSALNPVVKIGKQMtEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGG 159
Cdd:PRK11432 73 ------RSIQQRDICMVFQS--YALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEALELVDLAGFEDR---YVDQISGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGS 220
|
....*....
gi 1078707892 240 VLDIFQSPN 248
Cdd:PRK11432 221 PQELYRQPA 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-239 |
3.31e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.20 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK11160 338 SLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSirgnQISLISQ--DPMSA-LNPVVKIGKQmteviirhqkvKKREAQNIAVnlLKQVGLS----SPE-------ERVR 150
Cdd:PRK11160 412 LRQ----AISVVSQrvHLFSAtLRDNLLLAAP-----------NASDEALIEV--LQQVGLEklleDDKglnawlgEGGR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 151 QypheLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMknLKNETNMSLLLITHDLGIVAQnCTRVIVMY 230
Cdd:PRK11160 475 Q----LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQ-FDRICVMD 547
|
....*....
gi 1078707892 231 GGLIMEEGH 239
Cdd:PRK11160 548 NGQIIEQGT 556
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-252 |
5.17e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKEGEILFQNENVLS 79
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlNPEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 80 KSEK--ELRsirgNQISLISQDP----MSALNPVVkIGkqmteviIRHQKVKKREAQNIAV-NLLKQvglSSPEERVRQY 152
Cdd:PRK14239 77 PRTDtvDLR----KEIGMVFQQPnpfpMSIYENVV-YG-------LRLKGIKDKQVLDEAVeKSLKG---ASIWDEVKDR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 153 PHE----LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMslLLITHDLGIVAQNCTRVIV 228
Cdd:PRK14239 142 LHDsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGF 219
|
250 260
....*....|....*....|....
gi 1078707892 229 MYGGLIMEEGHVLDIFQSPNHPYT 252
Cdd:PRK14239 220 FLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-238 |
5.71e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 21 EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMA--LVTSPGKVK-EGEILFQNENVLSKsekelrsirgnQISLI- 96
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIK-MLTgiLVPTSGEVRvLGYVPFKRRKEFAR-----------RIGVVf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 97 ---SQ---DpmsaLnPVV---KIGKQMTEViirhqkVKKREAQNIA--VNLLkQVG--LSSPeerVRQypheLSGGMKQR 163
Cdd:COG4586 102 gqrSQlwwD----L-PAIdsfRLLKAIYRI------PDAEYKKRLDelVELL-DLGelLDTP---VRQ----LSLGQRMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 164 VMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-249 |
5.74e-22 |
|
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: 92.53 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSV--MALVTSPGKVKEGE----------ILFQNENVLSksekeLRSIRGNq 92
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIsgLAQPTSGGVILEGKqitepgpdrmVVFQNYSLLP-----WLTVREN- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 93 ISLisqdpmsALNPVVKigkqmteviirhqKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGGMKQRVMIAMAMSC 172
Cdd:TIGR01184 75 IAL-------AVDRVLP-------------DLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSI 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 173 NPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDI-FQSPNH 249
Cdd:TIGR01184 132 RPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-238 |
6.58e-22 |
|
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: 92.35 E-value: 6.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLS-KSEK 83
Cdd:COG0410 3 MLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL----PPRSGSIRFDGEDITGlPPHR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 84 ELRsiRGnqISLISQDPMsalnpvvkIGKQMT-----EVIIRHQKVKKREAQNIAVNL-----LKqvglsspeERVRQYP 153
Cdd:COG0410 75 IAR--LG--IGYVPEGRR--------IFPSLTveenlLLGAYARRDRAEVRADLERVYelfprLK--------ERRRQRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 154 HELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVAQNCTRVIVMYGGL 233
Cdd:COG0410 135 GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGR 213
|
....*
gi 1078707892 234 IMEEG 238
Cdd:COG0410 214 IVLEG 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-246 |
8.77e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.15 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 12 KTSFfiedgEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLS--KSEKELRSIR 89
Cdd:PRK13645 19 KTPF-----EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIIS----ETGQTIVGDYAIPAnlKKIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 90 gNQISLISQDPMSALNPVVkIGKQMTEVIIrHQKVKKREAQNIAVNLLKQVGLssPEERVRQYPHELSGGMKQRVMIAMA 169
Cdd:PRK13645 90 -KEIGLVFQFPEYQLFQET-IEKDIAFGPV-NLGENKQEAYKKVPELLKLVQL--PEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 170 MSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQS 246
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-252 |
2.05e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.08 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTS-PGKVKEGEILFQNENVLS-KSEKELRSIRGNQISLISQDPMSALN 105
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGYRYSGDVLLGGRSIFNyRDVLEFRRRVGMLFQRPNPFPMSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 106 PVVKigkqmteVIIRHQKVKKREAQNIAVNLLKQVGL-SSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTT 184
Cdd:PRK14271 120 NVLA-------GVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 185 ALDVTIQAQILDLMKNLKNEtnMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPYT 252
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-238 |
2.28e-21 |
|
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: 90.39 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKEl 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE----EPTSGRIYIGGRDVTDLPPKD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsiRGnqISLISQDpmSALNPvvkigkqmteviirHQKVkkreAQNIAVNL-LKQVGLSSPEERVRQ------------- 151
Cdd:cd03301 72 ---RD--IAMVFQN--YALYP--------------HMTV----YDNIAFGLkLRKVPKDEIDERVREvaellqiehlldr 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 152 YPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHD------LGivaqncTR 225
Cdd:cd03301 127 KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqveamtMA------DR 200
|
250
....*....|...
gi 1078707892 226 VIVMYGGLIMEEG 238
Cdd:cd03301 201 IAVMNDGQIQQIG 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-248 |
3.15e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.48 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEIlfqneNVLSKSEKelRSIRGNQISLISQD---- 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKI-----SILGQPTR--QALQKNLVAYVPQSeevd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 ---PMsALNPVVKIGKQMTEVIIRHQKVKKREAQNIAvnlLKQVGLSspEERVRQYpHELSGGMKQRVMIAMAMSCNPDL 176
Cdd:PRK15056 91 wsfPV-LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAA---LARVDMV--EFRHRQI-GELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 177 LIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRViVMYGGLIMEEGHVLDIFQSPN 248
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAEN 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-216 |
3.24e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.91 E-value: 3.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVK-----------EGEILFQNENVLSksekeLRSIRGN 91
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyQHGSITldgkpvegpgaERGVVFQNEGLLP-----WRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 92 qislisqdpmsalnpvVKIGKQMteviirhQKVKKREAQNIAVNLLKQVGLSSPEERvrqYPHELSGGMKQRVMIAMAMS 171
Cdd:PRK11248 91 ----------------VAFGLQL-------AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1078707892 172 CNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDL 216
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-238 |
3.72e-21 |
|
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: 90.47 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 11 LKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKegeilfQNENVLSKSEKELRSir 89
Cdd:cd03267 23 LKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVR------VAGLVPWKRRKKFLR-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 90 gnQISLI-SQDPMSALNPVVKIGKQMTEVIIRhqkVKKREAQNiavNLLKQVGLSSPEERVRQYPHELSGGMKQRVMIAM 168
Cdd:cd03267 95 --RIGVVfGQKTQLWWDLPVIDSFYLLAAIYD---LPPARFKK---RLDELSELLDLEELLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 169 AMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-238 |
4.66e-21 |
|
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: 90.24 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 23 EAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSV-----------------MALVTSPGKVKEGEILFQnENVLSKsekel 85
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyvpengrvlvdghdLALADPAWLRRQVGVVLQ-ENVLFN----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGNqISLisQDPMSALNPVVKIGKQMTEviirHQKVKK-REAQNIAVNllkQVGLSspeervrqypheLSGGMKQRV 164
Cdd:cd03252 90 RSIRDN-IAL--ADPGMSMERVIEAAKLAGA----HDFISElPEGYDTIVG---EQGAG------------LSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKN-LKNETnmsLLLITHDLGIVaQNCTRVIVMYGGLIMEEG 238
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDiCAGRT---VIIIAHRLSTV-KNADRIIVMEKGRIVEQG 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-243 |
5.23e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.53 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFFIEDG-EVEAVRGVSFSLKKGEVVGIVGESGSGKSVMaksvMALVTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:COG1101 2 LELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTL----LNAIAGSLPPDSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 lrsiRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQK------VKKREAQNIAvNLLKQVGLSSpEERVRQYPHELSG 158
Cdd:COG1101 78 ----RAKYIGRVFQDPMMGTAPSMTIEENLALAYRRGKRrglrrgLTKKRRELFR-ELLATLGLGL-ENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITH------DLGivaqncTRVIVMYGG 232
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeqalDYG------NRLIMMHEG 225
|
250
....*....|.
gi 1078707892 233 LImeeghVLDI 243
Cdd:COG1101 226 RI-----ILDV 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-253 |
7.38e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.90 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVK-EGEILFQNENVLSKSEKE 84
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARvEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRgnQISLISQDPmsalNPV--------VKIGKQMTEVIirhqKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHEL 156
Cdd:PRK14267 81 IEVRR--EVGMVFQYP----NPFphltiydnVAIGVKLNGLV----KSKKELDERVEWALKKAALWDEVKDRLNDYPSNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 SGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtnMSLLLITHDLGIVAQNCTRVIVMYGGLIME 236
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250
....*....|....*..
gi 1078707892 237 EGHVLDIFQSPNHPYTK 253
Cdd:PRK14267 229 VGPTRKVFENPEHELTE 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-243 |
8.76e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.55 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAlVTSPgkvKEGEILFQNENVlskSEKEL 85
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG-ILAP---DSGEVLWDGEPL---DPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSI------RGnqislisqdpmsaLNPVVKIGKQMTEVIIRHQkVKKREAQNIAVNLLKQVGLSS-PEERVRqyphELSG 158
Cdd:COG4152 71 RRIgylpeeRG-------------LYPKMKVGEQLVYLARLKG-LSKAEAKRRADEWLERLGLGDrANKKVE----ELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDVtIQAQIL-DLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDP-VNVELLkDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
....*.
gi 1078707892 238 GHVLDI 243
Cdd:COG4152 211 GSVDEI 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-248 |
1.04e-20 |
|
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: 89.37 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTS---PGKVKEGEIL---FQNENVLsksekELRSirgnQI 93
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLITGdlpPTYGNDVRLFgerRGGEDVW-----ELRK----RI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 94 SLISQD-------PMSALNpVVKIGKqmTEVIIRHQKVKKREAQnIAVNLLKQVGLSSPEERvrqYPHELSGGMKQRVMI 166
Cdd:COG1119 81 GLVSPAlqlrfprDETVLD-VVLSGF--FDSIGLYREPTDEQRE-RARELLELLGLAHLADR---PFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 167 AMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQS 246
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
..
gi 1078707892 247 PN 248
Cdd:COG1119 234 EN 235
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-238 |
1.11e-20 |
|
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: 88.80 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVlskSEKEL 85
Cdd:cd03245 3 IEFRNV--SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDI---RQLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGNqISLISQDPmsalnpVVKIGKQMTEVIIRHQKVKKREaqniavnLLKQVGLSSPEERVRQYPH----------- 154
Cdd:cd03245 74 ADLRRN-IGYVPQDV------TLFYGTLRDNITLGAPLADDER-------ILRAAELAGVTDFVNKHPNgldlqigergr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETnmSLLLITHDLGIVaQNCTRVIVMYGGLI 234
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
....
gi 1078707892 235 MEEG 238
Cdd:cd03245 217 VADG 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-306 |
1.34e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.05 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfieDGEvEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEILFQNENvLSKSEKE 84
Cdd:PRK11607 19 LLEIRNLTKSF---DGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLR-MLAGFEQP---TAGQIMLDGVD-LSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIrgnqiSLISQDpmSALNPVVKIgKQMTEVIIRHQKVKKREaqnIAVNLLKQVGLSSPEERVRQYPHELSGGMKQRV 164
Cdd:PRK11607 90 QRPI-----NMMFQS--YALFPHMTV-EQNIAFGLKQDKLPKAE---IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTI----QAQILDLMKNLknetNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHV 240
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 241 LDIFQSPNHPYTKGLLNSLPKISNGVKERLAP---IQgvTPNLLHPPK---------GCPF--AERcPHKMDICEKerPP 306
Cdd:PRK11607 235 EEIYEHPTTRYSAEFIGSVNVFEGVLKERQEDglvID--SPGLVHPLKvdadasvvdNVPVhvALR-PEKIMLCEE--PP 309
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-258 |
1.53e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKEL 85
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP----QSGTVFLGDKPISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsirGNQISLISQDPMS----ALNPVVKIGK--------QMTEViiRHQKVKKREAQNIAVNLlkqvglssPEERVRqyp 153
Cdd:PRK11231 75 ----ARRLALLPQHHLTpegiTVRELVAYGRspwlslwgRLSAE--DNARVNQAMEQTRINHL--------ADRRLT--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 154 hELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNmSLLLITHDLGIVAQNCTRVIVMYGGL 233
Cdd:PRK11231 138 -DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGH 215
|
250 260
....*....|....*....|....*
gi 1078707892 234 IMEEGhvldifqSPNHPYTKGLLNS 258
Cdd:PRK11231 216 VMAQG-------TPEEVMTPGLLRT 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-247 |
2.04e-20 |
|
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: 87.98 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVlSKSEKEL 85
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGKILLDGQDI-TKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGnqISLISQDPmsalnpvvKIGKQMT-----EVIIRHQKVKKREAQNIAVNLLKQVGLsspeERVR-QYPHELSGG 159
Cdd:cd03218 72 RARLG--IGYLPQEA--------SIFRKLTveeniLAVLEIRGLSKKEREEKLEELLEEFHI----THLRkSKASSLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHD----LGIvaqnCTRVIVMYGGLIM 235
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNvretLSI----TDRAYIIYEGKVL 212
|
250
....*....|..
gi 1078707892 236 EEGHVLDIFQSP 247
Cdd:cd03218 213 AEGTPEEIAANE 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-238 |
2.06e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.79 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSV---MAKSV-------------MAL----------- 58
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVlmhVLRGMdqyeptsgriiyhVALcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 59 -VTSPGKVKEGEILFQNENVLSKSEKELRSIRgNQISLISQDPMsAL----NPVVKIGKQMTEViirhqKVKKREAQNIA 133
Cdd:TIGR03269 77 kVGEPCPVCGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALygddTVLDNVLEALEEI-----GYEGKEAVGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 134 VNLLKQVGLsspEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLIT 213
Cdd:TIGR03269 150 VDLIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTS 226
|
250 260
....*....|....*....|....*
gi 1078707892 214 HDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEG 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-253 |
2.15e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVeaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVK-EGEILFQNENVLSKSEKE 84
Cdd:PRK14258 8 IKVNNL--SFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRvEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRgnQISLISQDP----MSALNPVVkigkQMTEVIIRHQKVkkrEAQNIAVNLLKQVGL-SSPEERVRQYPHELSGG 159
Cdd:PRK14258 84 NRLRR--QVSMVHPKPnlfpMSVYDNVA----YGVKIVGWRPKL---EIDDIVESALKDADLwDEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYG-----GLI 234
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQL 234
|
250
....*....|....*....
gi 1078707892 235 MEEGHVLDIFQSPNHPYTK 253
Cdd:PRK14258 235 VEFGLTKKIFNSPHDSRTR 253
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-232 |
3.91e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.74 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQnenvlsk 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKT----TVFNCLTGFYKPTGGTILLR------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 sEKELRSIRGNQISLIS-----QDpmsalnpvVKIGKQMTEV----IIRHQKVK----------------KREAQNIAVN 135
Cdd:PRK11300 66 -GQHIEGLPGHQIARMGvvrtfQH--------VRLFREMTVIenllVAQHQQLKtglfsgllktpafrraESEALDRAAT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 136 LLKQVGLSSPEERvrqYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHD 215
Cdd:PRK11300 137 WLERVGLLEHANR---QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
250
....*....|....*..
gi 1078707892 216 LGIVAQNCTRVIVMYGG 232
Cdd:PRK11300 214 MKLVMGISDRIYVVNQG 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-228 |
4.10e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.62 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmalVTS---PGKVKEGEILFQNEnvlsks 81
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMK-----VLSgvyPHGSYEGEILFDGE------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 EKELRSIRGNQ---ISLISQDpmSALNPVVKIgkqmTEVI-IRHQKVKK-----REAQNIAVNLLKQVGLS-SPEERVRq 151
Cdd:NF040905 66 VCRFKDIRDSEalgIVIIHQE--LALIPYLSI----AENIfLGNERAKRgvidwNETNRRARELLAKVGLDeSPDTLVT- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 152 yphELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIV 228
Cdd:NF040905 139 ---DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITV 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-214 |
4.79e-20 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 87.77 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmALVTSPG-KVKEGEILFQNENVLS 79
Cdd:CHL00131 3 KNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSK---VIAGHPAyKILEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 80 KsEKELRSIRGnqISLISQDPmsalnpvVKIGKQMTEVIIRHQKVKKREAQN-----------IAVNLLKQVGLsSPEER 148
Cdd:CHL00131 76 L-EPEERAHLG--IFLAFQYP-------IEIPGVSNADFLRLAYNSKRKFQGlpeldplefleIINEKLKLVGM-DPSFL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 149 VRQYPHELSGGMKQRVMI-AMAMScNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNmSLLLITH 214
Cdd:CHL00131 145 SRNVNEGFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITH 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-248 |
9.26e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.62 E-value: 9.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENV----L 78
Cdd:COG1137 1 MMTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGRIFLDGEDIthlpM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 79 SKsekelRSIRGnqISLISQDPmSalnpvvkIGKQMT-----EVIIRHQKVKKREAQNIAVNLLKQVGLsspeERVRQYP 153
Cdd:COG1137 73 HK-----RARLG--IGYLPQEA-S-------IFRKLTvedniLAVLELRKLSKKEREERLEELLEEFGI----THLRKSK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 154 -HELSGGMKQRVMIAMAMSCNPDLLIADEPTTALD-VTIqAQILDLMKNLKNEtNMSlLLIT-HD----LGIvaqnCTRV 226
Cdd:COG1137 134 aYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIG-VLITdHNvretLGI----CDRA 206
|
250 260
....*....|....*....|..
gi 1078707892 227 IVMYGGLIMEEGHVLDIFQSPN 248
Cdd:COG1137 207 YIISEGKVLAEGTPEEILNNPL 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-238 |
9.27e-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: 85.06 E-value: 9.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVlSKSEKEL 85
Cdd:cd03247 1 LSINNV--SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQQGEITLDGVPV-SDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSirgnQISLISQDPMSalnpvvkigkqmteviirhqkvkkreaqnIAVNLLKQVGLsspeervrqyphELSGGMKQRVM 165
Cdd:cd03247 74 SS----LISVLNQRPYL-----------------------------FDTTLRNNLGR------------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLM-KNLKNETnmsLLLITHDL-GIvaQNCTRVIVMYGGLIMEEG 238
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIfEVLKDKT---LIWITHHLtGI--EHMDKILFLENGKIIMQG 178
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-238 |
1.21e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.78 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 21 EVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVlskSEKELRSIRgNQISLISQDP 100
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKS----TVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLH-RQVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 101 msalnpvVKIGKQMTEVIIRH-QKVKKREAQNIAVnllkqvgLSSPEERVRQYPH-----------ELSGGMKQRVMIAM 168
Cdd:TIGR00958 565 -------VLFSGSVRENIAYGlTDTPDEEIMAAAK-------AANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 169 AMSCNPDLLIADEPTTALDVTIQAqildLMKNLKNETNMSLLLITHDLGIVaQNCTRVIVMYGGLIMEEG 238
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMG 695
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-239 |
1.91e-19 |
|
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: 84.77 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFFIEDGEVeaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVlskSEKEL 85
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL----EAEEGKIEIDGIDI---STIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQDP---MSALNPVVKIGKQMTEVIIrhqkvkkREAQNIavnllKQVGLSspeervrqypheLSGGMKQ 162
Cdd:cd03369 78 EDLR-SSLTIIPQDPtlfSGTIRSNLDPFDEYSDEEI-------YGALRV-----SEGGLN------------LSQGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQIldlMKNLKNE-TNMSLLLITHDLGIVAqNCTRVIVMYGGLIMEEGH 239
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALI---QKTIREEfTNSTILTIAHRLRTII-DYDKILVMDAGEVKEYDH 206
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-270 |
3.68e-19 |
|
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: 86.39 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 40 IVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVlSKSEKELRSIrgnqiSLISQDpmSALNPvvkigkQMT--EV 117
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLAGFEQPDSGSIMLDGEDV-TNVPPHLRHI-----NMVFQS--YALFP------HMTveEN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 118 IIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDL 197
Cdd:TIGR01187 63 VAFGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707892 198 MKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHPYTKGLLNSLPKISNGVKERL 270
Cdd:TIGR01187 143 LKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERK 215
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-238 |
4.44e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.77 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFQNENVlskSEKEL 85
Cdd:PRK11176 342 IEFRNV--TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN----LLTRFYDIDEGEILLDGHDL---RDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgNQISLISQDpMSALNPVV--KIGKQMTEVIIRHQKVKKREAQNiAVNLLKQV--GLSS--PEERVrqyphELSGG 159
Cdd:PRK11176 413 ASLR-NQVALVSQN-VHLFNDTIanNIAYARTEQYSREQIEEAARMAY-AMDFINKMdnGLDTviGENGV-----LLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDV----TIQAQILDLMKnlknetNMSLLLITHDLGIVaQNCTRVIVMYGGLIM 235
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTeserAIQAALDELQK------NRTSLVIAHRLSTI-EKADEILVVEDGEIV 557
|
...
gi 1078707892 236 EEG 238
Cdd:PRK11176 558 ERG 560
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-234 |
7.47e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 83.67 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKELRSirgnQISLISQDP-MSA 103
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKS----TVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS----KVSLVGQEPvLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 104 LNPVVKIGKQMTEVIIrhQKVKkrEAQNIA-----VNLLKQvglsSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLI 178
Cdd:cd03248 102 RSLQDNIAYGLQSCSF--ECVK--EAAQKAhahsfISELAS----GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 179 ADEPTTALDVTIQAQILDLMKNlkNETNMSLLLITHDLGIVaQNCTRVIVMYGGLI 234
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-237 |
7.61e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 23 EAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtspGKVKEGEILFQNENVLSKSEK-----------ELR----- 86
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGL----RPARGGRIMLNGKEINALSTAqrlarglvylpEDRqssgl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 ----SIRGNQISLISQDPMSALNPvvkigKQMTEVIIRHqkvkkREAQNIAvnllkqvgLSSPEERVRQypheLSGGMKQ 162
Cdd:PRK15439 353 yldaPLAWNVCALTHNRRGFWIKP-----ARENAVLERY-----RRALNIK--------FNHAEQAART----LSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-239 |
9.53e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.94 E-value: 9.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 19 DGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVmAKSVMALVTSPgkvKEGEILFQNENVLSKSEKELRsirgNQISLISQ 98
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKST-LINLLQRVFDP---QSGRILIDGTDIRTVTRASLR----RNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 99 DPMsALNPVV----KIGKQ-MTEVIIRhQKVKKREAQN-IAVNLLK---QVGlsspeERVRQypheLSGGMKQRVMIAMA 169
Cdd:PRK13657 417 DAG-LFNRSIedniRVGRPdATDEEMR-AAAERAQAHDfIERKPDGydtVVG-----ERGRQ----LSGGERQRLAIARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 170 MSCNPDLLIADEPTTALDVTIQAQILDLMKNL-KNETNmslLLITHDLGIVaQNCTRVIVMYGGLIMEEGH 239
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELmKGRTT---FIIAHRLSTV-RNADRILVFDNGRVVESGS 552
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-237 |
1.10e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSffiedgeveAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSE 82
Cdd:PRK10762 255 EVRLKVDNLSGP---------GVNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGALPRTSGYVTLDGHEVVTRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KE-LRsirgNQISLISQD--------------PMS--ALNPVVKIGKQmteviIRHQkvkkreAQNIAVN---LLKQVGL 142
Cdd:PRK10762 322 QDgLA----NGIVYISEDrkrdglvlgmsvkeNMSltALRYFSRAGGS-----LKHA------DEQQAVSdfiRLFNIKT 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 143 SSPEERVRqyphELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQN 222
Cdd:PRK10762 387 PSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGM 461
|
250
....*....|....*
gi 1078707892 223 CTRVIVMYGGLIMEE 237
Cdd:PRK10762 462 SDRILVMHEGRISGE 476
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-238 |
1.45e-18 |
|
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: 82.54 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 34 KGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKEGEI--------------LFQNENVLSKSEkelrsirgnqislISQ 98
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETpQSGRVLINGVdvtaappadrpvsmLFQENNLFAHLT-------------VEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 99 DPMSALNPVVKIGKQmteviiRHQKVKKreaqniavnLLKQVGLSSPEERVrqyPHELSGGMKQRVMIAMAMSCNPDLLI 178
Cdd:cd03298 90 NVGLGLSPGLKLTAE------DRQAIEV---------ALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 179 ADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-238 |
1.78e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvTSPGkvkEGEILFQNENVLSK 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM-TSPD---AGKITVLGVPVPAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SekelRSIRGnQISLISQdpMSALNPVVKIGKQMTeVIIRHQKVKKREAQNIAVNLLKQVGLSSPEE-RVRqyphELSGG 159
Cdd:PRK13536 109 A----RLARA-RIGVVPQ--FDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLESKADaRVS----DLSGG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-237 |
2.95e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLkTSFfiedgEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSE 82
Cdd:PRK09700 263 ETVFEVRNV-TSR-----DRKKVRDISFSVCRGEILGFAGLVGSGRT----ELMNCLFGVDKRAGGEIRLNGKDISPRSP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 keLRSIRgNQISLISQDPMS-------------ALNPVVKIGKQMTEVIIRHQKVKKREAQNiavnllKQVGLSSPEERV 149
Cdd:PRK09700 333 --LDAVK-KGMAYITESRRDngffpnfsiaqnmAISRSLKDGGYKGAMGLFHEVDEQRTAEN------QRELLALKCHSV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 150 RQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVM 229
Cdd:PRK09700 404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVF 482
|
....*...
gi 1078707892 230 YGGLIMEE 237
Cdd:PRK09700 483 CEGRLTQI 490
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-238 |
3.71e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.73 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKELrsirGNQISLISQD 99
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP----AHGHVWLDGEHIQHYASKEV----ARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 PMSALNPVVKigkqmtEVIIR----HQKVKKR---EAQNIAVNLLKQVGLSspeERVRQYPHELSGGMKQRVMIAMAMSC 172
Cdd:PRK10253 90 ATTPGDITVQ------ELVARgrypHQPLFTRwrkEDEEAVTKAMQATGIT---HLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 173 NPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-247 |
4.05e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFQNENVLSKSEKELrsirGNQISLISQDPMSA---- 103
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK----MLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQQLPAAegmt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 104 LNPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLlkqVGLSSPEERVRQyphELSGGMKQRVMIAMAMSCNPDLLIADEPT 183
Cdd:PRK10575 102 VRELVAIGRYPWHGALGRFGAADREKVEEAISL---VGLKPLAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 184 TALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSP 247
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-234 |
7.19e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLkTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMaksVMALVTS-PGKvKEGEILFQNENVlsKS 81
Cdd:PRK13549 257 EVILEVRNL-TAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTEL---VQCLFGAyPGR-WEGEIFIDGKPV--KI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 EKELRSIRgNQISLISQD-PMSALNPVVKIGKQMTEVIIRH-------QKVKKREAQNIAVNLLKqVGLSSPEERVRQyp 153
Cdd:PRK13549 330 RNPQQAIA-QGIAMVPEDrKRDGIVPVMGVGKNITLAALDRftggsriDDAAELKTILESIQRLK-VKTASPELAIAR-- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 154 heLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGL 233
Cdd:PRK13549 406 --LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
.
gi 1078707892 234 I 234
Cdd:PRK13549 483 L 483
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-243 |
1.65e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.49 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGkvkeGEILFQNENvLSKSEKEL 85
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSA----GELLAGTAP-LAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RsirgnqisLISQDpmSALNPVVKIGKQMTEVIIRHQKVKKREAqniavnlLKQVGLsspEERVRQYPHELSGGMKQRVM 165
Cdd:PRK11247 84 R--------LMFQD--ARLLPWKKVIDNVGLGLKGQWRDAALQA-------LAAVGL---ADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIvmyggLImEEGHV-LDI 243
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL-----LI-EEGKIgLDL 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-232 |
1.99e-17 |
|
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: 82.57 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtSPGKVKEGEILFQNENVLSKSeke 84
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV--YPHGTWDGEIYWSGSPLKASN--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQISLISQDPMsaLNPVVKIGKQM---TEVIIRHQKVKKREAQNIAVNLLKQVGLssPEERVRQYPHELSGGMK 161
Cdd:TIGR02633 72 IRDTERAGIVIIHQELT--LVPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQL--DADNVTRPVGDYGGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 162 QRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:TIGR02633 148 QLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-247 |
2.28e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.67 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSeklLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSK 80
Cdd:PRK10851 1 MS---IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ----TSGHIRFHGTDVSRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKElrsirgNQISLISQDpmSALNpvvkigKQMT---------EVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERvrq 151
Cdd:PRK10851 70 HARD------RKVGFVFQH--YALF------RHMTvfdniafglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 152 YPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYG 231
Cdd:PRK10851 133 YPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQ 212
|
250
....*....|....*.
gi 1078707892 232 GLIMEEGHVLDIFQSP 247
Cdd:PRK10851 213 GNIEQAGTPDQVWREP 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-216 |
3.47e-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: 82.02 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGkvkeGEILFQNENVLSKSEKEL 85
Cdd:TIGR02868 335 LELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ----GEVTLDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIrgnqISLISQDPM---SALNPVVKIGK------QMTEViirhqkvkkreaqniavnlLKQVGLsspEERVRQYPH-- 154
Cdd:TIGR02868 408 RRR----VSVCAQDAHlfdTTVRENLRLARpdatdeELWAA-------------------LERVGL---ADWLRALPDgl 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 155 ---------ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMknLKNETNMSLLLITHDL 216
Cdd:TIGR02868 462 dtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-252 |
4.26e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.15 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVlSKSEKE 84
Cdd:PRK09452 14 LVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIAGFETPDSGRIMLDGQDI-THVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRsirgnQISLISQDpmSALNPvvkigkQMT--EVI---IRHQKVKKREAQNIAVNLLKQVGLsspEERVRQYPHELSGG 159
Cdd:PRK09452 85 NR-----HVNTVFQS--YALFP------HMTvfENVafgLRMQKTPAAEITPRVMEALRMVQL---EEFAQRKPHQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGH 239
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
250
....*....|...
gi 1078707892 240 VLDIFQSPNHPYT 252
Cdd:PRK09452 229 PREIYEEPKNLFV 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
28-215 |
5.02e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtSPgkvKEGEILFQNENVLSKSEKELRsirgNQISLISQDPMSALNPV 107
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLI-SP---TSGTLLFEGEDISTLKPEIYR----QQVSYCAQTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 108 vkigkqMTEVIIRHQKVKKREAQNIAVNLLKQVGLssPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALD 187
Cdd:PRK10247 98 ------YDNLIFPWQIRNQQPDPAIFLDDLERFAL--PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180
....*....|....*....|....*...
gi 1078707892 188 VTIQAQILDLMKNLKNETNMSLLLITHD 215
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-240 |
6.11e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 4 KLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTsP--GKVKEGEilfqneNVlsks 81
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE-PdsGTVKLGE------TV---- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 ekelrsirgnQISLISQDpMSALNP-------VVKIGKQMTEVIIRhqkvkkreaqniavNLLKQVGLSSpeERVRQYPH 154
Cdd:COG0488 379 ----------KIGYFDQH-QEELDPdktvldeLRDGAPGGTEQEVR--------------GYLGRFLFSG--DDAFKPVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDV-TIQAqILDLMKNLKNetnmSLLLITHDLGIVAQNCTRVIVmyggl 233
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFPG----TVLLVSHDRYFLDRVATRILE----- 501
|
....*..
gi 1078707892 234 iMEEGHV 240
Cdd:COG0488 502 -FEDGGV 507
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-239 |
8.47e-17 |
|
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: 77.92 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSKSEKEL 85
Cdd:cd03244 3 IEFKNVSLRY--RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSirgnQISLISQDPM-------SALNPvvkIGKQMTEVIIrhqkvkkreaqniavNLLKQVGLsspEERVRQYPHEL-- 156
Cdd:cd03244 77 RS----RISIIPQDPVlfsgtirSNLDP---FGEYSDEELW---------------QALERVGL---KEFVESLPGGLdt 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 ---------SGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILD-LMKNLKNETnmsLLLITHDLGIVAQnCTRV 226
Cdd:cd03244 132 vveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKtIREAFKDCT---VLTIAHRLDTIID-SDRI 207
|
250
....*....|...
gi 1078707892 227 IVMYGGLIMEEGH 239
Cdd:cd03244 208 LVLDKGRVVEFDS 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-238 |
1.02e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.09 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 29 SFSLKKGEVVGIVGESGSGKSVMAkSVMA-----------------LVTSPGKvKEGEILFQNENVLSKsekelRSIRGN 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL-NLIAgfltpasgsltlngqdhTTTPPSR-RPVSMLFQENNLFSH-----LTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 92 qISLisqdpmsALNPVVKIGKQmteviirhqkvKKREAQNIAvnllKQVGLSSPEERVrqyPHELSGGMKQRVMIAMAMS 171
Cdd:PRK10771 92 -IGL-------GLNPGLKLNAA-----------QREKLHAIA----RQMGIEDLLARL---PGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 172 CNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-240 |
1.03e-16 |
|
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: 77.82 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtSPGKvkeGEILFQNENVlskSEKEL 85
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIL-RPTS---GEIIFDGHPW---TRKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRgnqiSLISQDPMsalnpvvkigkqmTEVIIRHQKVKKReAQNIAV------NLLKQVGLSSPEE-RVRQYphelSG 158
Cdd:TIGR03740 70 HKIG----SLIESPPL-------------YENLTARENLKVH-TTLLGLpdsridEVLNIVDLTNTGKkKAKQF----SL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALD-VTIQaQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:TIGR03740 128 GMKQRLGIAIALLNHPKLLILDEPTNGLDpIGIQ-ELRELIRSFP-EQGITVILSSHILSEVQQLADHIGIISEGVLGYQ 205
|
...
gi 1078707892 238 GHV 240
Cdd:TIGR03740 206 GKI 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-227 |
2.11e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.12 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMAlvtspgkvkegeilfqneNVLSKSEKELRSIRGNQISLISQdpMSA 103
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLK-VLA------------------GVLRPTSGTVRRAGGARVAYVPQ--RSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 104 LNP--------VVKIGKQMTEVIIRHQKvkkREAQNIAVNLLKQVGLSspEERVRQYpHELSGGMKQRVMIAMAMSCNPD 175
Cdd:NF040873 66 VPDslpltvrdLVAMGRWARRGLWRRLT---RDDRAAVDDALERVGLA--DLAGRQL-GELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 176 LLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVI 227
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEH-ARGATVVVVTHDLELVRRADPCVL 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-243 |
2.95e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGKvkeGEILFQNENvLSK 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMK-VLSGIHEPTK---GTITINNIN-YNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSIRGnqISLISQDpMSALNPV-----VKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLS-SPEERVRqyph 154
Cdd:PRK09700 72 LDHKLAAQLG--IGIIYQE-LSVIDELtvlenLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKvDLDEKVA---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSS 223
|
....*....
gi 1078707892 235 MEEGHVLDI 243
Cdd:PRK09700 224 VCSGMVSDV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-232 |
3.62e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.10 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLkTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAlvTSPGKVkEGEILFQNENVLSKSE 82
Cdd:TIGR02633 255 DVILEARNL-TCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGKF-EGNVFINGKPVDIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 keLRSIRGNqISLISQD-PMSALNPVVKIGKQMTEVIIRHQKVKKR-----EAQNI--AVNLLKqVGLSSPEERVRQyph 154
Cdd:TIGR02633 331 --AQAIRAG-IAMVPEDrKRHGIVPILGVGKNITLSVLKSFCFKMRidaaaELQIIgsAIQRLK-VKTASPFLPIGR--- 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 155 eLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:TIGR02633 404 -LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-267 |
4.15e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 12 KTSFFIEDGeVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSE-KELRSIRG 90
Cdd:PRK13644 6 NVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL----RPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 91 nqisLISQDPMSALnpvvkIGKQMTE--------VIIRHQKVKKREAQNIAvnllkQVGLsspEERVRQYPHELSGGMKQ 162
Cdd:PRK13644 81 ----IVFQNPETQF-----VGRTVEEdlafgpenLCLPPIEIRKRVDRALA-----EIGL---EKYRHRSPKTLSGGQGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLITHDLGIVaQNCTRVIVMYGGLIMEEGHVLD 242
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPEN 221
|
250 260
....*....|....*....|....*
gi 1078707892 243 IFQSPNHPYTKGLLNSLPKISNGVK 267
Cdd:PRK13644 222 VLSDVSLQTLGLTPPSLIELAENLK 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-215 |
9.41e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 26 RGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTspGKVK--EGEILFQnenvlsksekelrsiRGNQISLISQDP--- 100
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKS----TLLKILA--GELEpdSGEVSIP---------------KGLRIGYLPQEPpld 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 101 ---------MSALNPVVKIGKQMTEV----------IIRHQKVKKR-------EAQNIAVNLLKQVGLssPEERVRQYPH 154
Cdd:COG0488 74 ddltvldtvLDGDAELRALEAELEELeaklaepdedLERLAELQEEfealggwEAEARAEEILSGLGF--PEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDV-TIQ--AQILdlmKNLKNetnmSLLLITHD 215
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwlEEFL---KNYPG----TVLVVSHD 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-214 |
1.87e-15 |
|
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: 73.35 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGkvKEGEILFqneNVLSKSEKELRSIrgnqISLISQDpmsal 104
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG--VSGEVLI---NGRPLDKRSFRKI----IGYVPQD----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 105 npvvkigkqmtEVIIRHQKVkkREAQNIAVNLlkqvglsspeervRQypheLSGGMKQRVMIAMAMSCNPDLLIADEPTT 184
Cdd:cd03213 91 -----------DILHPTLTV--RETLMFAAKL-------------RG----LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190
....*....|....*....|....*....|
gi 1078707892 185 ALDVTIQAQILDLMKNLKNeTNMSLLLITH 214
Cdd:cd03213 141 GLDSSSALQVMSLLRRLAD-TGRTIICSIH 169
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-238 |
1.93e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.61 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvTSPgkvKEGEILFQNENVLSK 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-THP---DAGSISLCGEPVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SekelRSIRgNQISLISQdpMSALNPVVKIGKQMtEVIIRHQKVKKREAQNIAVNLLKQVGLSS-PEERVRqyphELSGG 159
Cdd:PRK13537 75 A----RHAR-QRVGVVPQ--FDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENkADAKVG----ELSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEG 238
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-239 |
4.71e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 7 EVKNLKTSFFIEDGEVE--AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtsPGKVKEGEILFQNENVlskseke 84
Cdd:COG2401 26 RVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL--KGTPVAGCVDVPDNQF------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 lrsirGNQISLISQdpmsalnpvvkigkqmteviirhqkVKKREAQNIAVNLLKQVGLSSPEERVRQYpHELSGGMKQRV 164
Cdd:COG2401 97 -----GREASLIDA-------------------------IGRKGDFKDAVELLNAVGLSDAVLWLRRF-KELSTGQKFRF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTiQAQILDL-MKNLKNETNMSLLLITHDLGIVA--QNCTRVIVMYGGLIMEEGH 239
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDdlQPDLLIFVGYGGVPEEKRR 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-229 |
5.48e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 70.94 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVeaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVM-ALVTSPGKVKEGeilfqnenvlskseke 84
Cdd:cd03221 1 IELENL--SKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 lrsirgnqislisqdpmsalnPVVKIGkqmteviirhqkvkkreaqniavnllkqvglsspeervrqYPHELSGGMKQRV 164
Cdd:cd03221 61 ---------------------STVKIG----------------------------------------YFEQLSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNetnmSLLLITHDLGIVAQNCTRVIVM 229
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-234 |
6.62e-15 |
|
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: 75.17 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmALV----TSPGKVK-EGEILFQNEnvlsk 80
Cdd:COG4618 331 LSVENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLAR---LLVgvwpPTAGSVRlDGADLSQWD----- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 sekelRSIRGNQISLISQDPmsalnpvvkigkqmteviirhqkvkkrE------AQNIA----------VNLLKQVG--- 141
Cdd:COG4618 401 -----REELGRHIGYLPQDV---------------------------ElfdgtiAENIArfgdadpekvVAAAKLAGvhe 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 142 --LSSP---EERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDL 216
Cdd:COG4618 449 miLRLPdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP 527
|
250
....*....|....*...
gi 1078707892 217 GIVAQnCTRVIVMYGGLI 234
Cdd:COG4618 528 SLLAA-VDKLLVLRDGRV 544
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-201 |
8.76e-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: 72.30 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 18 EDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpGKVKEGEILFQNENVlskSEKELRSIrgnqISLIS 97
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG-GGTTSGQILFNGQPR---KPDQFQKC----VAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 98 QDpmSALNPVVKIGKQMT-EVIIRHQ--KVKKREAQNIAVNLLKQVGLSSPEERVRQYpheLSGGMKQRVMIAMAMSCNP 174
Cdd:cd03234 88 QD--DILLPGLTVRETLTyTAILRLPrkSSDAIRKKRVEDVLLRDLALTRIGGNLVKG---ISGGERRRVSIAVQLLWDP 162
|
170 180
....*....|....*....|....*..
gi 1078707892 175 DLLIADEPTTALDVTIQAQILDLMKNL 201
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-248 |
1.94e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.65 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 7 EVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTSPgkvKEGEILFQNENVLSKSEKELr 86
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRLLPP---DSGEVLVDGLDVATTPSREL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 sirGNQISLISQDPMSALNPVVK----IGK------QMTEviIRHQKVkkREAqniavnlLKQVGLSSPEERvrqYPHEL 156
Cdd:COG4604 74 ---AKRLAILRQENHINSRLTVRelvaFGRfpyskgRLTA--EDREII--DEA-------IAYLDLEDLADR---YLDEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 SGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIME 236
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVA 216
|
250
....*....|..
gi 1078707892 237 EGHVLDIFQSPN 248
Cdd:COG4604 217 QGTPEEIITPEV 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-253 |
3.26e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 2 SEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVT-SPGKVKEGEILFQNENVLSK 80
Cdd:PRK14243 7 TETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGFRVEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 --SEKELRSirgnQISLISQDPmsalNPvvkIGKQMTEVIIRHQKVK--KREAQNIAVNLLKQVGL-SSPEERVRQYPHE 155
Cdd:PRK14243 83 dvDPVEVRR----RIGMVFQKP----NP---FPKSIYDNIAYGARINgyKGDMDELVERSLRQAALwDEVKDKLKQSGLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtnMSLLLITHDLgivaQNCTRVIVM------ 229
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNM----QQAARVSDMtaffnv 225
|
250 260 270
....*....|....*....|....*....|..
gi 1078707892 230 --------YGGLImEEGHVLDIFQSPNHPYTK 253
Cdd:PRK14243 226 eltegggrYGYLV-EFDRTEKIFNSPQQQATR 256
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-219 |
4.25e-14 |
|
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: 69.69 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKtsffIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVlskseKEL 85
Cdd:TIGR01189 1 LAARNLA----CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL----RPDSGEVRWNGTPL-----AEQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGNQISLISQDPmsALNPVVKIGKQMTEVIIRHQkvkkrEAQNIAVNLLKQVGLSSPEERVrqyPHELSGGMKQRVM 165
Cdd:TIGR01189 68 RDEPHENILYLGHLP--GLKPELSALENLHFWAAIHG-----GAQRTIEDALAAVGLTGFEDLP---AAQLSAGQQRRLA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIV 219
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-248 |
4.31e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.96 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSvmakSVM-ALVtspGKVK-EGEILFQNEnvlsksekELRSI-----RgNQISLISQDP 100
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKT----SLLnALL---GFLPyQGSLKINGI--------ELRELdpeswR-KHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 101 M---SALNPVVKIGK-QMTEVIIrHQKVKKREAQNIaVNLLKQvGLSSP--EERVRqypheLSGGMKQRVMIAMAMSCNP 174
Cdd:PRK11174 433 QlphGTLRDNVLLGNpDASDEQL-QQALENAWVSEF-LPLLPQ-GLDTPigDQAAG-----LSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 175 DLLIADEPTTALDVTIQAQIldlMKNLKNETN-MSLLLITHDLGIVAQnCTRVIVMYGGLIMEEGHVLDIFQSPN 248
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLV---MQALNAASRrQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-238 |
4.78e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.81 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpGKVKEGEI-----LFQNENV 77
Cdd:PRK09984 2 QTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITG-DKSAGSHIellgrTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 LSKSEKELRSIRG---NQISLISQdpMSALNPVVkIGKQMTEVIIRH-QKVKKREAQNIAVNLLKQVGLSS-PEERVRQy 152
Cdd:PRK09984 77 LARDIRKSRANTGyifQQFNLVNR--LSVLENVL-IGALGSTPFWRTcFSWFTREQKQRALQALTRVGMVHfAHQRVST- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 153 pheLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:PRK09984 153 ---LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
....*.
gi 1078707892 233 LIMEEG 238
Cdd:PRK09984 230 HVFYDG 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-248 |
6.22e-14 |
|
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: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 27 GVSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTsPGkvkEGEILFQNENVLSKSEKELRSIRGnqiSLISQDPMSALNP 106
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLL-ARMAGLL-PG---QGEILLNGRPLSDWSAAELARHRA---YLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 107 VVkigkqmtEVIIRHQKVKKREAQNIAV--NLLKQVGLSSPEERvrqyP-HELSGGMKQRVMIAMAM-----SCNPD--L 176
Cdd:COG4138 86 VF-------QYLALHQPAGASSEAVEQLlaQLAEALGLEDKLSR----PlTQLSGGEWQRVRLAAVLlqvwpTINPEgqL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 177 LIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPN 248
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-232 |
6.67e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTsPGkvkEGEILFQNENVLSKSEKELRSIRGnqiSLISQDPMSALNPV 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLL-ARMAGLL-PG---SGSIQFAGQPLEAWSAAELARHRA---YLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 108 VkigkQMTEviiRHQKVKKREAQNIAV--NLLKQVGLSSPEERVRQyphELSGGMKQRVMIAMAM-----SCNPD--LLI 178
Cdd:PRK03695 87 F----QYLT---LHQPDKTRTEAVASAlnEVAEALGLDDKLGRSVN---QLSGGEWQRVRLAAVVlqvwpDINPAgqLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 179 ADEPTTALDVTiQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:PRK03695 157 LDEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-238 |
7.01e-14 |
|
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: 72.46 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 23 EAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFQNENVLSKSEKELRSIrgnqISLISQDPms 102
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAK----LLVGFFQARSGEILLNGFSLKDIDRHTLRQF----INYLPQEP-- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 103 alnpVVKIGKQMTEVIIRHQKVKKREaqniavNLLKQVGLSSPEERVRQYPH-----------ELSGGMKQRVMIAMAMS 171
Cdd:TIGR01193 558 ----YIFSGSILENLLLGAKENVSQD------EIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 172 CNPDLLIADEPTTALDVTIQAQILDLMKNLKNETnmsLLLITHDLGiVAQNCTRVIVMYGGLIMEEG 238
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDKT---IIFVAHRLS-VAKQSDKIIVLDHGKIIEQG 690
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-244 |
8.96e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 15 FFIEDGEVeaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNEnVLSKSEKELRSIRgNQIS 94
Cdd:PRK13638 9 FRYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLL----RPQKGAVLWQGK-PLDYSKRGLLALR-QQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 95 LISQDPMSAL---NPVVKIGKQMTEVIIRHQKVKKREAQniAVNLLKQvglsspeERVRQYPHE-LSGGMKQRVMIAMAM 170
Cdd:PRK13638 81 TVFQDPEQQIfytDIDSDIAFSLRNLGVPEAEITRRVDE--ALTLVDA-------QHFRHQPIQcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 171 SCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNmSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIF 244
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-243 |
9.61e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.85 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 11 LKTSFF-IEDGEVE-AVRGVSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTSPGKvkeGEIlfqnenvlsksekelrSI 88
Cdd:PRK13545 24 LKDLFFrSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLS-NLIAGVTMPNK---GTV----------------DI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 89 RGNQiSLISQDpmSALNPVVKiGKQMTEVIIRHQKVKKREAQNIAVNLLK--QVG--LSSPeerVRQYphelSGGMKQRV 164
Cdd:PRK13545 84 KGSA-ALIAIS--SGLNGQLT-GIENIELKGLMMGLTKEKIKEIIPEIIEfaDIGkfIYQP---VKTY----SSGMKSRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDI 243
Cdd:PRK13545 153 GFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-247 |
1.57e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfieDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSKSEKEl 85
Cdd:PRK11650 4 LKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLER----ITSGEIWIGGRVVNELEPAD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 rsiRGnqISLISQDpmSALNPvvkigkqmteviirHQKVkkreAQNIAVNLlKQVGLSSPE--ERVRQY----------- 152
Cdd:PRK11650 76 ---RD--IAMVFQN--YALYP--------------HMSV----RENMAYGL-KIRGMPKAEieERVAEAarileleplld 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 153 --PHELSGGMKQRVmiAM--AMSCNPDLLIADEPTTALD----VTIQAQILDLMKNLKNETnmslLLITHD------Lgi 218
Cdd:PRK11650 130 rkPRELSGGQRQRV--AMgrAIVREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKTTS----LYVTHDqveamtL-- 201
|
250 260
....*....|....*....|....*....
gi 1078707892 219 vAQnctRVIVMYGGLIMEEGHVLDIFQSP 247
Cdd:PRK11650 202 -AD---RVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-247 |
2.26e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 37 VVGIVGESGSGKSVMAKSVMALvTSPgkvKEGEILFqNENVLSKSEK------ELRsirgnQISLISQDpmSALNPvvki 110
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGL-TRP---QKGRIVL-NGRVLFDAEKgiclppEKR-----RIGYVFQD--ARLFP---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 111 gkqmteviirHQKVKKR----EAQNIAVNLLKQVGLSSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTAL 186
Cdd:PRK11144 90 ----------HYKVRGNlrygMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 187 DVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSP 247
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-219 |
5.29e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEIlfqnenvlsKSEKE 84
Cdd:PRK09544 4 LVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAP----DEGVI---------KRNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRsirgnqISLISQ----DPMSALNpvvkIGKQMTeviiRHQKVKKREAqniaVNLLKQVglssPEERVRQYP-HELSGG 159
Cdd:PRK09544 67 LR------IGYVPQklylDTTLPLT----VNRFLR----LRPGTKKEDI----LPALKRV----QAGHLIDAPmQKLSGG 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIV 219
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-243 |
6.81e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFfieDGeVEAVRGVSFSLKKGEVVGIVGESGSGKSVMaksvMALVTSPGKVKEGEILFQNENVLSKSE 82
Cdd:PRK10762 2 QALLQLKGIDKAF---PG-VKALSGAALNVYPGRVMALVGENGAGKSTM----MKVLTGIYTRDAGSILYLGKEVTFNGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KElrsirgNQ---ISLISQDpmsaLN--PVVKI------GKQMTEVI--IRHQKVKKReaqniAVNLLKQVGLS-SPEER 148
Cdd:PRK10762 74 KS------SQeagIGIIHQE----LNliPQLTIaeniflGREFVNRFgrIDWKKMYAE-----ADKLLARLNLRfSSDKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 149 VrqypHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIV 228
Cdd:PRK10762 139 V----GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTV 213
|
250
....*....|....*
gi 1078707892 229 MYGGLIMEEGHVLDI 243
Cdd:PRK10762 214 FRDGQFIAEREVADL 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-227 |
6.93e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 30 FSLKKGEVVGIVGESGSGKS----VMAKSVMalvtspgkVKEGEILFQNENVLSKSEKEL-RSIRGN------------- 91
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKStlmkILNGEVL--------LDDGRIIYEQDLIVARLQQDPpRNVEGTvydfvaegieeqa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 92 -------QIS-LISQDPMSalnpvvKIGKQMTEV--IIRHQKVKKREAQNIAVnlLKQVGLSsPEERVRqyphELSGGMK 161
Cdd:PRK11147 96 eylkryhDIShLVETDPSE------KNLNELAKLqeQLDHHNLWQLENRINEV--LAQLGLD-PDAALS----SLSGGWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 162 QRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNetnmSLLLITHDLGIVAQNCTRVI 227
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIV 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-219 |
1.29e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 4 KLLEVKNLKTSFFIEDgEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQN-ENVLSKSE 82
Cdd:PTZ00265 381 KKIQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP----TEGDIIINDsHNLKDINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSirgnQISLISQDPM-------------------------------------------------SALNPVVKI--G 111
Cdd:PTZ00265 456 KWWRS----KIGVVSQDPLlfsnsiknnikyslyslkdlealsnyynedgndsqenknkrnscrakcaGDLNDMSNTtdS 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 112 KQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEER----VRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALD 187
Cdd:PTZ00265 532 NELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
250 260 270
....*....|....*....|....*....|..
gi 1078707892 188 VTIQAQILDLMKNLKNETNMSLLLITHDLGIV 219
Cdd:PTZ00265 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-216 |
1.38e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFS-------------LKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKELRSIRgN 91
Cdd:PRK11831 10 MRGVSFTrgnrcifdnisltVPRGKITAIMGPSGIGKT----TLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 92 QISLISQD-----PMSALNPV---VKIGKQMTEVIIRHQKVKKREAqniavnllkqVGLSSPEERVrqyPHELSGGMKQR 163
Cdd:PRK11831 85 RMSMLFQSgalftDMNVFDNVaypLREHTQLPAPLLHSTVMMKLEA----------VGLRGAAKLM---PSELSGGMARR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1078707892 164 VMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDL 216
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
3-232 |
1.59e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAkSVMALVTSPGKVKEGEILFqNENVLSKSE 82
Cdd:TIGR00955 19 SWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLM-NALAFRSPKGVKGSGSVLL-NGMPIDAKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSirgnqiSLISQDPM-------------SALnpvVKIGKQMTeviirhqKVKKREAQNiavNLLKQVGLSSPEERV 149
Cdd:TIGR00955 97 MRAIS------AYVQQDDLfiptltvrehlmfQAH---LRMPRRVT-------KKEKRERVD---EVLQALGLRKCANTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 150 RQYPHE---LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRV 226
Cdd:TIGR00955 158 IGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKI 237
|
....*.
gi 1078707892 227 IVMYGG 232
Cdd:TIGR00955 238 ILMAEG 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-238 |
1.79e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 67.92 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 19 DGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKELRSirgnQISLISQ 98
Cdd:COG5265 368 DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY----DVTSGRILIDGQDIRDVTQASLRA----AIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 99 DpmsalnpVV-------------KIGKQMTEViirhqkvkkREAQNIA-----VNLLKQ-----VGlsspeER-VRqyph 154
Cdd:COG5265 440 D-------TVlfndtiayniaygRPDASEEEV---------EAAARAAqihdfIESLPDgydtrVG-----ERgLK---- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 eLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNL-KNETNmslLLITHDLGIVAqNCTRVIVMYGGL 233
Cdd:COG5265 495 -LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVaRGRTT---LVIAHRLSTIV-DADEILVLEAGR 569
|
....*
gi 1078707892 234 IMEEG 238
Cdd:COG5265 570 IVERG 574
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-249 |
2.90e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVK----EGEILFQNENVLSKSEKELRSIRgnqiSLISQD- 99
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRgarvTGDVTLNGEPLAAIDAPRLARLR----AVLPQAa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 ----PMSAlNPVVKIGKQMTeviIRHQKVKKREAQNIAVNLLKQVGLSSpeeRVRQYPHELSGGMKQRVMIAMAMS---- 171
Cdd:PRK13547 93 qpafAFSA-REIVLLGRYPH---ARRAGALTHRDGEIAWQALALAGATA---LVGRDVTTLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 172 -----CNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQs 246
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT- 244
|
...
gi 1078707892 247 PNH 249
Cdd:PRK13547 245 PAH 247
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-237 |
1.04e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLkTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAlvTSPGKVKEGEILfqnenvLSKSE 82
Cdd:NF040905 255 EVVFEVKNW-TVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGRNISGTVF------KDGKE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSIR---GNQISLISQDPMSA-LNPVVKIGKQMT----EVIIRHQKVKKREAQNIAVNLLKQVGLSSPEerVRQYPH 154
Cdd:NF040905 326 VDVSTVSdaiDAGLAYVTEDRKGYgLNLIDDIKRNITlanlGKVSRRGVIDENEEIKVAEEYRKKMNIKTPS--VFQKVG 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHD----LGIvaqnCTRVIVMY 230
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSElpelLGM----CDRIYVMN 478
|
....*..
gi 1078707892 231 GGLIMEE 237
Cdd:NF040905 479 EGRITGE 485
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-231 |
1.14e-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: 63.97 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 31 SLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEILFQNENVLSKSEKelrsirgnqislisqdpmsalnpvVKI 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIK-MLAGVLKP---DEGDIEIELDTVSYKPQY------------------------IKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 111 GKQMTEVIIRHQKVKKREAQN-IAVNLLKQVGLSSPEERvrQYPhELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVT 189
Cdd:cd03237 73 DYEGTVRDLLSSITKDFYTHPyFKTEIAKPLQIEQILDR--EVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1078707892 190 IQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYG 231
Cdd:cd03237 150 QRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-241 |
1.38e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSvmaLVTSPgKVKEGEILFQNENVlsk 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGT---LCGDP-RATSGRIVFDGKDI--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 81 SEKELRSIRGNQISLISQDPMSALNPVVKIGKQMTEVIIRHQKVKKREAQniAVNLLKQVglsspEERVRQYPHELSGGM 160
Cdd:PRK11614 70 TDWQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKW--VYELFPRL-----HERRIQRAGTMSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 161 KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLithdlgiVAQNCTRVIVMYG-GLIMEEGH 239
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFL-------VEQNANQALKLADrGYVLENGH 214
|
..
gi 1078707892 240 VL 241
Cdd:PRK11614 215 VV 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-247 |
1.47e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.12 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKELRSirgnQISLISQDPMSA 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS----RLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 104 LNPVvkigkqmteviirhqkvkkreAQNIAVNL-------LKQVG-LSSPEERVRQYPH-----------ELSGGMKQRV 164
Cdd:PRK10789 402 SDTV---------------------ANNIALGRpdatqqeIEHVArLASVHDDILRLPQgydtevgergvMLSGGQKQRI 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILdlmKNLKNETNMSLLLIT-HDLGIVAQnCTRVIVMYGGLIMEEGHVLDI 243
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQIL---HNLRQWGEGRTVIISaHRLSALTE-ASEILVMQHGHIAQRGNHDQL 536
|
....
gi 1078707892 244 FQSP 247
Cdd:PRK10789 537 AQQS 540
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-229 |
1.58e-11 |
|
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: 62.51 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKtsffIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKEL 85
Cdd:cd03231 1 LEADELT----CERDGRALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIrgnqISLISQDPMSALNPVVkigkqmtEVIIRHQKVKKREAQNIAvnlLKQVGLSSPEERVrqyPHELSGGMKQRVM 165
Cdd:cd03231 73 RGL----LYLGHAPGIKTTLSVL-------ENLRFWHADHSDEQVEEA---LARVGLNGFEDRP---VAQLSAGQQRRVA 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIvAQNCTRVIVM 229
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGL-SEAGARELDL 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-238 |
2.14e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGkvkeGEILFQNENVLSKSEKELRsirgNQISLISQDPM--- 101
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCG----GEIRVNGREIGAYGLRELR----RQFSMIPQDPVlfd 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 102 ----SALNPVVKIGKQmtEVIIRHQKVKKREaqniavnllkQVGLSSP--EERVrqypheLSGGMK----QRVMIAMA-- 169
Cdd:PTZ00243 1398 gtvrQNVDPFLEASSA--EVWAALELVGLRE----------RVASESEgiDSRV------LEGGSNysvgQRQLMCMAra 1459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 170 -MSCNPDLLIADEPTT----ALDVTIQAQIldlMKNLKNETnmsLLLITHDLGIVAQnCTRVIVMYGGLIMEEG 238
Cdd:PTZ00243 1460 lLKKGSGFILMDEATAnidpALDRQIQATV---MSAFSAYT---VITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-245 |
3.25e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVlSKSEKELRSIRGnqISLISQDPmSAL 104
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPR----DAGNIIIDDEDI-SLLPLHARARRG--IGYLPQEA-SIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 105 NPVVKIGKQMTEVIIRHQkVKKREAQNIAVNLLKQVGLSSPEERVRQyphELSGGMKQRVMIAMAMSCNPDLLIADEPTT 184
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDD-LSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 185 ALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQ 245
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-238 |
9.77e-11 |
|
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: 63.04 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMaksVMALVTSPGKVkEGEIlfqnenvlsksekelrSIRGN-----QIS 94
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMDKV-EGHV----------------HMKGSvayvpQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 95 LISQDpmsALNPVVKIGKQMTEViiRHQKVKKreaqniAVNLLKQVGL--SSPEERVRQYPHELSGGMKQRVMIAMAMSC 172
Cdd:TIGR00957 709 WIQND---SLRENILFGKALNEK--YYQQVLE------ACALLPDLEIlpSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 173 NPDLLIADEPTTALDVTIQAQILDL----MKNLKNETNmslLLITHDLGIVAQnCTRVIVMYGGLIMEEG 238
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIFEHvigpEGVLKNKTR---ILVTHGISYLPQ-VDVIIVMSGGKISEMG 843
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-232 |
2.02e-10 |
|
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: 59.41 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVEA---VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMA-LVTSPGKVK-EGEILF-------Q 73
Cdd:cd03250 1 ISVEDA--SFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSvPGSIAYvsqepwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 74 N----ENVL--SKSEKEL--RSIRGnqislisqdpmSALNPVVKI--GKQMTEVIIRhqkvkkreaqniavnllkqvGLS 143
Cdd:cd03250 79 NgtirENILfgKPFDEERyeKVIKA-----------CALEPDLEIlpDGDLTEIGEK--------------------GIN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 144 speervrqypheLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILD--LMKNLKNetNMSLLLITHDLGIVAQ 221
Cdd:cd03250 128 ------------LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH 193
|
250
....*....|.
gi 1078707892 222 nCTRVIVMYGG 232
Cdd:cd03250 194 -ADQIVVLDNG 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-240 |
2.68e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSgkSVMAKSVMALVTSPGKVKEG---EILFQNENVLSKSE 82
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GA--A**RGALPAHV*GPDAGRRPwrf*TWCANRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KELRSIRGNQISLISqdpmsalnpvvkiGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVRQyphELSGGMKQ 162
Cdd:NF000106 88 G*HRPVR*GRRESFS-------------GRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 163 RVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHV 240
Cdd:NF000106 152 RLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-262 |
2.71e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAL--VTSpgkvkeGEILFQNENVLSKSEKElrsiRGnqISLIS 97
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLedITS------GDLFIGEKRMNDVPPAE----RG--VGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 98 QDpmSALNPVVKIGKQMTeVIIRHQKVKKREAQ---NIAVNLLKqvgLSSPEERvrqYPHELSGGMKQRVMIAMAMSCNP 174
Cdd:PRK11000 82 QS--YALYPHLSVAENMS-FGLKLAGAKKEEINqrvNQVAEVLQ---LAHLLDR---KPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 175 DLLIADEPTTALD----VTIQAQILDLMKNLKNetnmSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFQSPNHP 250
Cdd:PRK11000 153 SVFLLDEPLSNLDaalrVQMRIEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANR 228
|
250
....*....|..
gi 1078707892 251 YTKGLLNSlPKI 262
Cdd:PRK11000 229 FVAGFIGS-PKM 239
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-241 |
2.92e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 27 GVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVkeGEILFQNENVLSKSEKelrsirgnQISLISQDPMsaLNP 106
Cdd:PLN03211 86 GVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT--GTILANNRKPTKQILK--------RTGFVTQDDI--LYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 107 VVKIGKQMTEV-IIRHQK-VKKREAQNIAVNLLKQVGLSSPEERV--RQYPHELSGGMKQRVMIAMAMSCNPDLLIADEP 182
Cdd:PLN03211 154 HLTVRETLVFCsLLRLPKsLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 183 TTALDVTIQAQILDLMKNLKNEtNMSLLLITHdlgivaQNCTRVIVMYGG-LIMEEGHVL 241
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH------QPSSRVYQMFDSvLVLSEGRCL 286
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-268 |
3.83e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVM-ALVTSPGKV-KEGEILFQNENV-LSKSEKELRSIRGNQISL-ISQD 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGgSLSPTVGKVdRNGEVSVIAISAgLSGQLTGIENIEFKMLCMgFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 PMSALNPVVKIGKQMTEVIirHQKVKKreaqniavnllkqvglsspeervrqypheLSGGMKQRVMIAMAMSCNPDLLIA 179
Cdd:PRK13546 119 EIKAMTPKIIEFSELGEFI--YQPVKK-----------------------------YSSGMRAKLGFSINITVNPDILVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 180 DEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEEGHVLDIFqspnhPYTKGLLNSL 259
Cdd:PRK13546 168 DEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLNDF 241
|
....*....
gi 1078707892 260 PKISNGVKE 268
Cdd:PRK13546 242 KKKSKAEQK 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-231 |
6.52e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 32 LKKGEVVGIVGESGSGKSVMAKsVMAlvtspgkvkeGEILFQNENVLSKSEKE--LRSIRGNQIslisQDPMSAL----- 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-ILS----------GELIPNLGDYEEEPSWDevLKRFRGTEL----QNYFKKLyngei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 105 NPVVKIgkQMTEVIIRHQKVKKREA------QNIAVNLLKQVGLSSPEER-VRqyphELSGGMKQRVMIAMAMSCNPDLL 177
Cdd:PRK13409 161 KVVHKP--QYVDLIPKVFKGKVRELlkkvdeRGKLDEVVERLGLENILDRdIS----ELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 178 IADEPTTALDVTIQAQILDLMKNLKNetNMSLLLITHDLGI---VAQNctrVIVMYG 231
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVldyLADN---VHIAYG 286
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-232 |
6.89e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.04 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 14 SFFIEDGEVEA--VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSPGKVkEGEILFQNENVlskseKELRSIRGN 91
Cdd:cd03233 10 SFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV-EGDIHYNGIPY-----KEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 92 QISLISQDPmsalnpvVKIgKQMTeviirhqkVkkREAQNIAVNLlkqvglsspeeRVRQYPHELSGGMKQRVMIAMAMS 171
Cdd:cd03233 84 EIIYVSEED-------VHF-PTLT--------V--RETLDFALRC-----------KGNEFVRGISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707892 172 CNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITH--DLGIVAQnCTRVIVMYGG 232
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDL-FDKVLVLYEG 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-214 |
7.20e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 16 FIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVK-EGEILFQNE-----------------NV 77
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKS----TVMSLLMRFYDLKnDHHIVFKNEhtndmtneqdyqgdeeqNV 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 LSKSEKE---------------------------------LRSIRgNQISLISQDPM---SALNPVVKIGKQMTEviirh 121
Cdd:PTZ00265 1251 GMKNVNEfsltkeggsgedstvfknsgkilldgvdicdynLKDLR-NLFSIVSQEPMlfnMSIYENIKFGKEDAT----- 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 122 QKVKKREAQNIAVNLLKQVGLSSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNL 201
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250
....*....|...
gi 1078707892 202 KNETNMSLLLITH 214
Cdd:PTZ00265 1405 KDKADKTIITIAH 1417
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-236 |
9.80e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKELRSIrgnqISLISQDPMsAL 104
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV----ELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPV-LF 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 105 NPVVKIGkqmTEVIIRHQKVKKREAQNIAvnLLKQVGLSSP---EERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADE 181
Cdd:PLN03232 1323 SGTVRFN---IDPFSEHNDADLWEALERA--HIKDVIDRNPfglDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 182 PTTALDVTIQAQIldlMKNLKNE-TNMSLLLITHDLGIVAqNCTRVIVMYGGLIME 236
Cdd:PLN03232 1398 ATASVDVRTDSLI---QRTIREEfKSCTMLVIAHRLNTII-DCDKILVLSSGQVLE 1449
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-231 |
1.25e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 29 SFSL------KKGEVVGIVGESGSGKSVmaksvmALvtspgKVKEGEI---LFQNENVLSKsEKELRSIRGNQIslisQD 99
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKST------AL-----KILSGELkpnLGDYDEEPSW-DEVLKRFRGTEL----QD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 PMSAL-----NPVVKIgkQMTEVIIRHQKVKKREA------QNIAVNLLKQVGLSSPEER-VRqyphELSGGMKQRVMIA 167
Cdd:COG1245 151 YFKKLangeiKVAHKP--QYVDLIPKVFKGTVRELlekvdeRGKLDELAEKLGLENILDRdIS----ELSGGELQRVAIA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 168 MAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGI---VAQNctrVIVMYG 231
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAIldyLADY---VHILYG 287
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-231 |
1.28e-09 |
|
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: 57.76 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 29 SFSL------KKGEVVGIVGESGSGKSVMAKsVMAlvtspGKVKEGEILFQNEnvlSKSEKELRSIRGNQIslisQDPMS 102
Cdd:cd03236 14 SFKLhrlpvpREGQVLGLVGPNGIGKSTALK-ILA-----GKLKPNLGKFDDP---PDWDEILDEFRGSEL----QNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 103 AL-----NPVVK------IGKQMT-EVIIRHQKVKKREAQNIavnLLKQVGLSSPEERVRQyphELSGGMKQRVMIAMAM 170
Cdd:cd03236 81 KLlegdvKVIVKpqyvdlIPKAVKgKVGELLKKKDERGKLDE---LVDQLELRHVLDRNID---QLSGGELQRVAIAAAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 171 SCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNmSLLLITHDLGIVAQNCTRVIVMYG 231
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-231 |
1.74e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 1 MSEKLLEVKNLKTSFfiEDGEVEAVRGvsfSLKKGEVVGIVGESGSGKSVMAKsVMALVTSP--GKVKEG-EILFQNENV 77
Cdd:COG1245 337 EEETLVEYPDLTKSY--GGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFAK-ILAGVLKPdeGEVDEDlKISYKPQYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 LSKSEKELRSIRGNqislisqdpmsalnpvvKIGKQMTEVIIRHQKVKKREAQNIavnLLKQVGlsspeervrqyphELS 157
Cdd:COG1245 411 SPDYDGTVEEFLRS-----------------ANTDDFGSSYYKTEIIKPLGLEKL---LDKNVK-------------DLS 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 158 GGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYG 231
Cdd:COG1245 458 GGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-212 |
3.22e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 29 SFSLKKGEVVGIVGESGSGKSVMAKsvmALvtspgkvkegeilfQNENVLSKSEKELRSIRGNQIS------LISQ---- 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALAR---AL--------------AGELPLLSGERQSQFSHITRLSfeqlqkLVSDewqr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 99 ---DPMSALNPvvKIGKQMTEVIIRHQKVKKREAQniavnLLKQVGLSSPEERVRQYpheLSGGMKQRVMIAMAMSCNPD 175
Cdd:PRK10938 86 nntDMLSPGED--DTGRTTAEIIQDEVKDPARCEQ-----LAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPD 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1078707892 176 LLIADEPTTALDVTIQAQILDLMKNLkNETNMSLLLI 212
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLV 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
156-268 |
4.31e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILD--LMKNLKNETNmslLLITHDLGIVAQnCTRVIVMYGGL 233
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGKTR---VLVTNQLHFLSQ-VDRIILVHEGM 816
|
90 100 110
....*....|....*....|....*....|....*
gi 1078707892 234 IMEEGHVLDIfqSPNHPYTKGLLNSLPKISNGVKE 268
Cdd:PLN03130 817 IKEEGTYEEL--SNNGPLFQKLMENAGKMEEYVEE 849
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
156-246 |
4.59e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILD--LMKNLKNETNmslLLITHDLGIVAQnCTRVIVMYGGL 233
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTR---VLVTNQLHFLPL-MDRIILVSEGM 816
|
90
....*....|...
gi 1078707892 234 IMEEGHVLDIFQS 246
Cdd:PLN03232 817 IKEEGTFAELSKS 829
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-261 |
4.62e-09 |
|
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: 57.65 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKELRSirgnQISLISQDpmsal 104
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES----AEGEIIIDGLNIAKIGLHDLRF----KITIIPQD----- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 105 nPVVKIGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEE---RVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADE 181
Cdd:TIGR00957 1369 -PVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKldhECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 182 PTTALDVT----IQAQILDLMKNLknetnmSLLLITHDLGIVaQNCTRVIVMYGGLIMEEGHVLDIFQSpnhpytKGLLN 257
Cdd:TIGR00957 1448 ATAAVDLEtdnlIQSTIRTQFEDC------TVLTIAHRLNTI-MDYTRVIVLDKGEVAEFGAPSNLLQQ------RGIFY 1514
|
....
gi 1078707892 258 SLPK 261
Cdd:TIGR00957 1515 SMAK 1518
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-239 |
4.85e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVV--------------GIVGESGSGKSVMAKSVMALVTspgkVKEGEILFQNENVLSKSEKELRsir 89
Cdd:PRK10790 342 DIDNVSFAYRDDNLVlqninlsvpsrgfvALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 90 gNQISLISQDPMSALNPV---VKIGKQMTEviirhQKVKKreaqniavnLLKQVGLSspeERVRQYP-----------HE 155
Cdd:PRK10790 415 -QGVAMVQQDPVVLADTFlanVTLGRDISE-----EQVWQ---------ALETVQLA---ELARSLPdglytplgeqgNN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETnmSLLLITHDLGIVAQNCTrVIVMYGGLIM 235
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVEADT-ILVLHRGQAV 553
|
....
gi 1078707892 236 EEGH 239
Cdd:PRK10790 554 EQGT 557
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-229 |
5.04e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLKtsffIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKEL 85
Cdd:PRK13539 3 LEGEDLA----CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL----PPAAGTIKLDGGDIDDPDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRGNQislisqdpmSALNPVVKIgkqmTEVIIRHQKVKKREAQNIAVNLlKQVGLSSPEERVRQYpheLSGGMKQRVM 165
Cdd:PRK13539 75 CHYLGHR---------NAMKPALTV----AENLEFWAAFLGGEELDIAAAL-EAVGLAPLAHLPFGY---LSAGQKRRVA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMK-NLknETNMSLLLITH-DLGIvaqNCTRVIVM 229
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDAAAVALFAELIRaHL--AQGGIVIAATHiPLGL---PGARELDL 198
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-214 |
5.59e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLktSFFIEDGEVeAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtSP-GkvkEGEILF-QNENVLsksek 83
Cdd:COG4178 363 LALEDL--TLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL--WPyG---SGRIARpAGARVL----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 84 elrsirgnqisLISQDP-------MSAL---NPVvkigKQMTEVIIRHqkvkkreaqniavnLLKQVGLSSPEER---VR 150
Cdd:COG4178 430 -----------FLPQRPylplgtlREALlypATA----EAFSDAELRE--------------ALEAVGLGHLAERldeEA 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 151 QYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETnmSLLLITH 214
Cdd:COG4178 481 DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT--TVISVGH 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-237 |
8.16e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 21 EVEAVRG------VSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKElrSIRGNqIS 94
Cdd:PRK11288 259 RLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGAT----RRTAGQVYLDGKPIDIRSPRD--AIRAG-IM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 95 LISQD-------PMSALNPVVKIGKQmteviiRHQKV------KKREAQNIA--VNLLKqVGLSSPEERVRQypheLSGG 159
Cdd:PRK11288 332 LCPEDrkaegiiPVHSVADNINISAR------RHHLRagclinNRWEAENADrfIRSLN-IKTPSREQLIMN----LSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 160 MKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGGLIMEE 237
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-231 |
8.42e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 29 SFSL-------KKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEIlfqnenvlsksEKELRsirgnqislISQDPM 101
Cdd:PRK13409 352 DFSLeveggeiYEGEVIGIVGPNGIGKTTFAK-LLAGVLKP---DEGEV-----------DPELK---------ISYKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 102 salnpVVKIGKQMT-EVIIRhqKVKKREAQN-IAVNLLKQVGLsspEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIA 179
Cdd:PRK13409 408 -----YIKPDYDGTvEDLLR--SITDDLGSSyYKSEIIKPLQL---ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 180 DEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYG 231
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-234 |
9.19e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSFfiedGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGKvkeGEIlfqneNVLSKSEKE 84
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMK-IIAGIVPPDS---GTL-----EIGGNPCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIRGNQ--ISLISQDPMSALNPVVKigkqmtEVII----RHQKVKKREAQniavnLLKQVGlsspeerVRQYPHELSG 158
Cdd:PRK15439 78 LTPAKAHQlgIYLVPQEPLLFPNLSVK------ENILfglpKRQASMQKMKQ-----LLAALG-------CQLDLDSSAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 159 GM----KQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGGLI 234
Cdd:PRK15439 140 SLevadRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-238 |
9.38e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKTSffIEDGEVeaVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMAlvTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK09580 1 MLSIKDLHVS--VEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 lRSirGNQISLISQDPM------------SALNPVVKIGKQmtEVIIRHQKVKKREAQniaVNLLKQvglssPEERV-RQ 151
Cdd:PRK09580 75 -RA--GEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPLDRFDFQDLMEEK---IALLKM-----PEDLLtRS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 152 YPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQ-NCTRVIVMY 230
Cdd:PRK09580 142 VNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYiKPDYVHVLY 220
|
....*...
gi 1078707892 231 GGLIMEEG 238
Cdd:PRK09580 221 QGRIVKSG 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-216 |
9.59e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.03 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 15 FFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKELRSIRGNQIS 94
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKS----SLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 95 LISQDPMsALNPVVKigkqmtEVIIRHQKVKKREAQNI--AVNLLKQVGL--SSPEERVRQYPHELSGGMKQRVMIAMAM 170
Cdd:cd03290 83 YAAQKPW-LLNATVE------ENITFGSPFNKQRYKAVtdACSLQPDIDLlpFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 171 SCNPDLLIADEPTTALDV-----TIQAQILDLMKNLKNetnmSLLLITHDL 216
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-225 |
3.47e-08 |
|
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: 51.99 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 34 KGEVVGIVGESGSGKSVMAKSVMALVTSPGKvkegeilfqnenvlsksekelrsirgnqislisqdpmsalnPVVKIGkq 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-----------------------------------------GVIYID-- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 114 mteviirhqkvkkreaqniAVNLLKQVGLSSPEERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQ 193
Cdd:smart00382 38 -------------------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|....*..
gi 1078707892 194 ILDL-----MKNLKNETNMSLLLITHDLGIVAQNCTR 225
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-238 |
3.72e-08 |
|
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: 52.33 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 17 IEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmalvtspgkvkegEILfqnenvlsKSEKELRsirgnqisLI 96
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGL--------YASGKAR--------LI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 97 SQDPMSALNPVVKIGKqmteviirhqkvkkreaqniaVNLLKQVGLSS-PEERVRQyphELSGGMKQRVMIA--MAMSCN 173
Cdd:cd03238 52 SFLPKFSRNKLIFIDQ---------------------LQFLIDVGLGYlTLGQKLS---TLSGGELQRVKLAseLFSEPP 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 174 PDLLIADEPTTALDVTIQAQILDLMKNLKNETNmSLLLITHDLGIVaQNCTRVIVM------YGGLIMEEG 238
Cdd:cd03238 108 GTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-232 |
5.65e-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: 54.63 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFQNENVLSksekelrsirgnQISLISQD---- 99
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFK----MLTGDTTVTSGDATVAGKSILT------------NISDVHQNmgyc 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 100 -PMSALNPVVKiGKQMTEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEERVrqyPHELSGGMKQRVMIAMAMSCNPDLLI 178
Cdd:TIGR01257 2018 pQFDAIDDLLT-GREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 179 ADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-213 |
6.27e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 20 GEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEIlfqneNVLSK--SEKELRSIRGNQISLIS 97
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKS----SLLSLIAGARKIQQGRV-----EVLGGdmADARHRRAVCPRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 98 QDpmsalnpvvkIGKQ--MT----EVIIRH-----QKVKKREAQnIAvNLLKQVGLSSPEERvrqyPH-ELSGGMKQRVM 165
Cdd:NF033858 83 QG----------LGKNlyPTlsvfENLDFFgrlfgQDAAERRRR-ID-ELLRATGLAPFADR----PAgKLSGGMKQKLG 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1078707892 166 IAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNET-NMSLLLIT 213
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-232 |
7.25e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 22 VEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvKEGEILFQNENVLSKSEKELRSirgNQISLISQDpm 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQK----DSGSILFQGKEIDFKSSKEALE---NGISMVHQE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 102 saLNPVVK--------IGKQMTEVIIRHQKVKKREAQNIAVNLLKQVglsSPEERVRqyphELSGGMKQRVMIAMAMSCN 173
Cdd:PRK10982 82 --LNLVLQrsvmdnmwLGRYPTKGMFVDQDKMYRDTKAIFDELDIDI---DPRAKVA----TLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 174 PDLLIADEPTTALDVTIQAQILDLMKNLKnETNMSLLLITHDLGIVAQNCTRVIVMYGG 232
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-228 |
9.66e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 22 VEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPGkvkEGEILFQNENVLSKSEKElrSIRGNqISLISQDpm 101
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLK-ILSGNYQPD---AGSILIDGQEMRFASTTA--ALAAG-VAIIYQE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 102 saLNPVvkigKQMT--EVII------RHQKVKKREAQNIAVNLLKQVGLS-SPEERVRqyphELSGGMKQRVMIAMAMSC 172
Cdd:PRK11288 88 --LHLV----PEMTvaENLYlgqlphKGGIVNRRLLNYEAREQLEHLGVDiDPDTPLK----YLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 173 NPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHDLGIVAQNCTRVIV 228
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-188 |
1.03e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 14 SFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSvMALVTSPGKVKEGEILFQNENVLSKS------------ 81
Cdd:PLN03073 182 NFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRY-MAMHAIDGIPKNCQILHVEQEVVGDDttalqcvlntdi 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 82 ------EKELRSI---RGNQISLISQDPMSALNPVVK---IGKQMTEVIIRHQKVKKREAQNIAVNLLkqVGLSSPEERV 149
Cdd:PLN03073 261 ertqllEEEAQLVaqqRELEFETETGKGKGANKDGVDkdaVSQRLEEIYKRLELIDAYTAEARAASIL--AGLSFTPEMQ 338
|
170 180 190
....*....|....*....|....*....|....*....
gi 1078707892 150 RQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDV 188
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
152-214 |
1.91e-07 |
|
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: 50.23 E-value: 1.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 152 YP--HELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKnetnMSLLLITH 214
Cdd:cd03223 86 YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-236 |
1.96e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 27 GVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVtspgKVKEGEILFQNENVLSKSEKELRSIrgnqISLISQ-------- 98
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIV----ELERGRILIDGCDISKFGLMDLRKV----LGIIPQapvlfsgt 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 99 -----DPMSALNPVvkigkQMTEVIIR-HQK-VKKREAQniavnllkqvGLsspEERVRQYPHELSGGMKQRVMIAMAMS 171
Cdd:PLN03130 1329 vrfnlDPFNEHNDA-----DLWESLERaHLKdVIRRNSL----------GL---DAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707892 172 CNPDLLIADEPTTALDVTIQAQIldlMKNLKNE-TNMSLLLITHDLGIVAqNCTRVIVMYGGLIME 236
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALI---QKTIREEfKSCTMLIIAHRLNTII-DCDRILVLDAGRVVE 1452
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-231 |
2.92e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 32 LKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvkEGEilfqnenvlsksekelrsirgnqislisQDPMSALNPVVKig 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVK-ILAGQLIP----NGD----------------------------NDEWDGITPVYK-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 112 kqmteviirHQKVKkreaqniavnllkqvglsspeervrqypheLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQ 191
Cdd:cd03222 67 ---------PQYID------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1078707892 192 AQILDLMKNLKNETNMSLLLITHDLGIVAQNCTRVIVMYG 231
Cdd:cd03222 108 LNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-205 |
4.21e-07 |
|
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: 50.63 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMA-LVTSPGKVKE-GEILFQNENvlskSEKELRSIRGNQISLISQDPMS 102
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKIKHsGRISFSSQF----SWIMPGTIKENIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 103 ALNpVVKiGKQMTEVIirhqkVKKREAQNIavnLLKQVGLSspeervrqypheLSGGMKQRVMIAMAMSCNPDLLIADEP 182
Cdd:cd03291 129 YKS-VVK-ACQLEEDI-----TKFPEKDNT---VLGEGGIT------------LSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180
....*....|....*....|....*
gi 1078707892 183 TTALDVTIQAQILD--LMKNLKNET 205
Cdd:cd03291 187 FGYLDVFTEKEIFEscVCKLMANKT 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-216 |
4.39e-07 |
|
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: 51.45 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMA-LVTSPGKVKE-GEILF--QNENVLSKsekelrSIRGNQISLISQDP 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIKHsGRISFspQTSWIMPG------TIKDNIIFGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 101 MSaLNPVVKiGKQMTEVIirhqkVKKREAQNIavnLLKQVGLSspeervrqypheLSGGMKQRVMIAMAMSCNPDLLIAD 180
Cdd:TIGR01271 516 YR-YTSVIK-ACQLEEDI-----ALFPEKDKT---VLGEGGIT------------LSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190
....*....|....*....|....*....|....*...
gi 1078707892 181 EPTTALDVTIQAQILD--LMKNLKNETNmslLLITHDL 216
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEscLCKLMSNKTR---ILVTSKL 608
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
145-215 |
4.43e-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: 49.53 E-value: 4.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707892 145 PEERVRqypheLSGGMKQ------RVMIAMAMSCNPDLLIADEPTTALDV-TIQAQILDLMKNLKNETNMSLLLITHD 215
Cdd:cd03240 110 LDMRGR-----CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-192 |
5.38e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.09 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLKTSF----FIEDgeveavrgVSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFqnenvl 78
Cdd:TIGR03719 320 DKVIEAENLTKAFgdklLIDD--------LSFKLPPGGIVGVIGPNGAGKSTLFR----MITGQEQPDSGTIEI------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 79 sksekelrsirGNQISLISQDPM-SALNPvvkiGKQMTEVI---IRHQKVKKREaqniaVNLLKQVGL-----SSPEERV 149
Cdd:TIGR03719 382 -----------GETVKLAYVDQSrDALDP----NKTVWEEIsggLDIIKLGKRE-----IPSRAYVGRfnfkgSDQQKKV 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1078707892 150 RQypheLSGGMKQRVMIAMAMSCNPDLLIADEPTTALDV-TIQA 192
Cdd:TIGR03719 442 GQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-214 |
5.53e-07 |
|
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: 51.45 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLkTSFFIEDGEvEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvkEGEILFQNENVLSKSEKEL 85
Cdd:TIGR01271 1218 MDVQGL-TAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-----EGEIQIDGVSWNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRG---NQISLISQDPMSALNPvvkigkqmteviirHQKVKKREAQNIAvnllKQVGLSSpeeRVRQYPHE------- 155
Cdd:TIGR01271 1291 RKAFGvipQKVFIFSGTFRKNLDP--------------YEQWSDEEIWKVA----EEVGLKS---VIEQFPDKldfvlvd 1349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707892 156 ----LSGGMKQRVMIAMAMSCNPDLLIADEPTTALD-VTIQAqildLMKNLKNE-TNMSLLLITH 214
Cdd:TIGR01271 1350 ggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQI----IRKTLKQSfSNCTVILSEH 1410
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-215 |
6.27e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 35 GEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKELRSIrgnqislisqdPMSALNPVV------ 108
Cdd:PRK10636 27 GQKVGLVGKNGCGKS----TLLALLKNEISADGGSYTFPGNWQLAWVNQETPAL-----------PQPALEYVIdgdrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 109 -KIGKQMTEVIIR---------HQKVKKREAQNI---AVNLLKQVGLSspEERVRQYPHELSGGMKQRVMIAMAMSCNPD 175
Cdd:PRK10636 92 rQLEAQLHDANERndghaiatiHGKLDAIDAWTIrsrAASLLHGLGFS--NEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1078707892 176 LLIADEPTTALDVTiqaQILDLMKNLKNETNmSLLLITHD 215
Cdd:PRK10636 170 LLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHD 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-234 |
1.45e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 3 EKLLEVKNLkTSFfiedgEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALvtspGKVKEGEILFQNENVLSKSE 82
Cdd:PRK10982 248 EVILEVRNL-TSL-----RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGI----REKSAGTITLHGKKINNHNA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 83 KElrSIRgNQISLISQDPMS---------ALNPVV-KIGKQMTEVIIRHQKVKKREAQNIAVNLlkqvglsspeeRVRQY 152
Cdd:PRK10982 318 NE--AIN-HGFALVTEERRStgiyayldiGFNSLIsNIRNYKNKVGLLDNSRMKSDTQWVIDSM-----------RVKTP 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 153 PHE-----LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNEtNMSLLLITHD----LGIvaqnC 223
Cdd:PRK10982 384 GHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEmpelLGI----T 458
|
250
....*....|.
gi 1078707892 224 TRVIVMYGGLI 234
Cdd:PRK10982 459 DRILVMSNGLV 469
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-229 |
2.74e-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: 47.93 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 6 LEVKNLkTSFFIEDGEVeAVRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTSpgkvkEGEILFQNENVLSKSEKEL 85
Cdd:cd03289 3 MTVKDL-TAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-----EGDIQIDGVSWNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 86 RSIRG---NQISLISQDPMSALNPVvkiGKQMTEVIIRhqkvkkreaqniavnLLKQVGLSSPEErvrQYPHE------- 155
Cdd:cd03289 76 RKAFGvipQKVFIFSGTFRKNLDPY---GKWSDEEIWK---------------VAEEVGLKSVIE---QFPGQldfvlvd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 ----LSGGMKQRVMIAMAMSCNPDLLIADEPTTALD-VTIQAqildLMKNLKNE-TNMSLLLITHDLGIVAQnCTRVIVM 229
Cdd:cd03289 135 ggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQV----IRKTLKQAfADCTVILSEHRIEAMLE-CQRFLVI 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
155-233 |
3.74e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 155 ELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDV-TIQ--AQILdlmknlkNETNMSLLLITHDLGIVAQNCTRVIVM-Y 230
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDInTIRwlEDVL-------NERNSTMIIISHDRHFLNSVCTHMADLdY 227
|
...
gi 1078707892 231 GGL 233
Cdd:PRK15064 228 GEL 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-215 |
4.00e-06 |
|
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: 48.39 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 23 EAVRGVSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEILFQ----------------NENVLSKSEKELR 86
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVDKD---FNGEARPQpgikvgylpqepqldpTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 87 SIRG-----NQISLISQDPMSALNpvvKIGKQMTEV--IIRHQKVKKREAQ-NIAVNLLKqvgLSSPEERVRqyphELSG 158
Cdd:TIGR03719 95 EIKDaldrfNEISAKYAEPDADFD---KLAAEQAELqeIIDAADAWDLDSQlEIAMDALR---CPPWDADVT----KLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 159 GMKQRVMIAMAMSCNPDLLIADEPTTALDvtiqAQILDLMKNLKNETNMSLLLITHD 215
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-201 |
5.49e-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: 46.47 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 9 KNLKTSFFIEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSVMAksvmalvtspgkvkegeilfqneNVLSKsEKELRSI 88
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLL-----------------------DVLAG-RKTAGVI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 89 RGNqISLISQDPMSALNPVVKIGKQMtEVIIRHQKVkkREAQNIAVNLLkqvGLSsPEERvrqyphelsggmkQRVMIAM 168
Cdd:cd03232 63 TGE-ILINGRPLDKNFQRSTGYVEQQ-DVHSPNLTV--REALRFSALLR---GLS-VEQR-------------KRLTIGV 121
|
170 180 190
....*....|....*....|....*....|...
gi 1078707892 169 AMSCNPDLLIADEPTTALDVTIQAQILDLMKNL 201
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
154-220 |
9.76e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 9.76e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 154 HELSGGMKQRVMIAMAM---SCNPD-LLIADEPTTALDVTIQAQILDLMKNLKNETNMsLLLITHDLGIVA 220
Cdd:cd03227 76 LQLSGGEKELSALALILalaSLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLPELAE 145
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-216 |
9.79e-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: 47.32 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 8 VKNLKTSFfiEDGEVEAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVlsksEKELRS 87
Cdd:TIGR01257 931 VKNLVKIF--EPSGRPAVDRLNITFYENQITAFLGHNGAGKT----TTLSILTGLLPPTSGTVLVGGKDI----ETNLDA 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 88 IRgNQISLISQDPMSALNPVVkigkqmTEVIIRHQKVKKR---EAQNIAVNLLKQVGLsspEERVRQYPHELSGGMKQRV 164
Cdd:TIGR01257 1001 VR-QSLGMCPQHNILFHHLTV------AEHILFYAQLKGRsweEAQLEMEAMLEDTGL---HHKRNEEAQDLSGGMQRKL 1070
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 165 MIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMknLKNETNMSLLLITHDL 216
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-247 |
1.68e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 25 VRGVSFSLKKGEVVGIVGESGSGKSVMAKSVMalvtSPGKVKEGEILFQnenvlsksekelRSI--------------RG 90
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLL----SQFEISEGRVWAE------------RSIayvpqqawimnatvRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 91 NqISLISQDPMSALNPVVKigkqmteviirhqkVKKREAQniavnlLKQVGlSSPEERVRQYPHELSGGMKQRVMIAMAM 170
Cdd:PTZ00243 740 N-ILFFDEEDAARLADAVR--------------VSQLEAD------LAQLG-GGLETEIGEKGVNLSGGQKARVSLARAV 797
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 171 SCNPDLLIADEPTTALDVTIQAQILD--LMKNLKNETNmslLLITHDLGIVAQnCTRVIVMYGGLIMEEGHVLDIFQSP 247
Cdd:PTZ00243 798 YANRDVYLLDDPLSALDAHVGERVVEecFLGALAGKTR---VLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-198 |
1.73e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 5 LLEVKNLKtsfFIEDGEVeAVRGVSFSLKKGEVVGIVGESGSGKSvmakSVMALVTSPGKVKEGEILFQNENVLSKSEKE 84
Cdd:PRK13538 1 MLEARNLA---CERDERI-LFSGLSFTLNAGELVQIEGPNGAGKT----SLLRILAGLARPDAGEVLWQGEPIRRQRDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 85 LRSIR--GNQISLisQDPMSALnpvvkigkqmtEVIIRHQKVKKREAQNIAVNLLKQVGLSSPEE-RVRQypheLSGGMK 161
Cdd:PRK13538 73 HQDLLylGHQPGI--KTELTAL-----------ENLRFYQRLHGPGDDEALWEALAQVGLAGFEDvPVRQ----LSAGQQ 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 1078707892 162 QRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLM 198
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-53 |
1.86e-04 |
|
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: 42.86 E-value: 1.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1078707892 6 LEVKNLKTSFFIEDGEveavRG-----VSFSLKKGEVVGIVGESGSGKSVMAK 53
Cdd:COG4615 328 LELRGVTYRYPGEDGD----EGftlgpIDLTIRRGELVFIVGGNGSGKSTLAK 376
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
136-214 |
3.03e-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: 42.43 E-value: 3.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707892 136 LLKQVGLSSpeerVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQaqilDLMKNLKNETNMSLLLITH 214
Cdd:TIGR00954 567 LEREGGWSA----VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
156-215 |
5.33e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.86 E-value: 5.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 156 LSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVtiqaQILDLMKNLKNETNMSLLLITHD 215
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-221 |
7.48e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 7.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707892 156 LSGGMKQRVMIAMAMS---CNPDLLIADEPTTAL---DVtiqAQILDLMKNLKNETNmSLLLITHDLGIVAQ 221
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGN-TVVVIEHNLDVIKT 897
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
151-187 |
1.50e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 1.50e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1078707892 151 QYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALD 187
Cdd:NF033858 393 ALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-192 |
1.55e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 4 KLLEVKNLKTSF----FIEDgeveavrgVSFSLKKGEVVGIVGESGSGKSVMAKSVMALVTsP--GKVKEGEILfqnenv 77
Cdd:PRK11819 323 KVIEAENLSKSFgdrlLIDD--------LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQ-PdsGTIKIGETV------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 78 lsksekelrsirgnQISLISQDpMSALNPvvkiGKQMTEVI------IrhqKVKKREA---------------QNiavnl 136
Cdd:PRK11819 388 --------------KLAYVDQS-RDALDP----NKTVWEEIsggldiI---KVGNREIpsrayvgrfnfkggdQQ----- 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707892 137 lKQVGlsspeervrqyphELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDV-TIQA 192
Cdd:PRK11819 441 -KKVG-------------VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVeTLRA 483
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
136-238 |
1.73e-03 |
|
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: 39.52 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 136 LLKQVGLSSPeeRVRQYPHELSGGMKQRVMIAMAMScNPD----LLIADEPTTAL---DVtiqAQILDLMKNLKNETNmS 208
Cdd:cd03271 152 TLCDVGLGYI--KLGQPATTLSGGEAQRIKLAKELS-KRStgktLYILDEPTTGLhfhDV---KKLLEVLQRLVDKGN-T 224
|
90 100 110
....*....|....*....|....*....|....*.
gi 1078707892 209 LLLITHDLGIVAqNCTRVIVM------YGGLIMEEG 238
Cdd:cd03271 225 VVVIEHNLDVIK-CADWIIDLgpeggdGGGQVVASG 259
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-215 |
3.16e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 28 VSFSLKKGEVVGIVGESGSGKSVMAKsVMALVTSPgkvKEGEIlfqnenVLSKSEKeLRSIRGNQISLISQDPmSALNPV 107
Cdd:PRK10636 331 IKLNLVPGSRIGLLGRNGAGKSTLIK-LLAGELAP---VSGEI------GLAKGIK-LGYFAQHQLEFLRADE-SPLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 108 VKIGKQMTEVIIRhqkvkkreaqniavNLLKQVGLSSpeERVRQYPHELSGGMKQRVMIAMAMSCNPDLLIADEPTTALD 187
Cdd:PRK10636 399 ARLAPQELEQKLR--------------DYLGGFGFQG--DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170 180
....*....|....*....|....*...
gi 1078707892 188 VTIQAQILDLMKNLKNetnmSLLLITHD 215
Cdd:PRK10636 463 LDMRQALTEALIDFEG----ALVVVSHD 486
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-238 |
3.24e-03 |
|
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: 38.39 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 26 RGVSFSLKKGEVVGIVGESGSGKSVMAksvMALVTSPGKVKEGEIL--FQNENVLSKSEKELRSIRG--NQISL----IS 97
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSLA---FDTIYAEGQRRYVESLsaYARQFLGQMDKPDVDSIEGlsPAIAIdqktTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 98 QDPMSALNPVVKIGKQMtEVIIRHQKVKKReaqniaVNLLKQVGLS--SPEERVRQypheLSGGMKQRVMIAMAMSCNPD 175
Cdd:cd03270 89 RNPRSTVGTVTEIYDYL-RLLFARVGIRER------LGFLVDVGLGylTLSRSAPT----LSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707892 176 --LLIADEPTTALDVTIQAQILDLMKNLKNETNmSLLLITHDLGIVaQNCTRVIVM------YGGLIMEEG 238
Cdd:cd03270 158 gvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTI-RAADHVIDIgpgagvHGGEIVAQG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
157-245 |
4.83e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.94 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 157 SGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMKNLKNETNMSLLLITHDlgiVAQNC----TRVIVMYGG 232
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQ---CSQDAyelfDKVIVLYEG 287
|
90
....*....|....*.
gi 1078707892 233 LIMEEG---HVLDIFQ 245
Cdd:TIGR00956 288 YQIYFGpadKAKQYFE 303
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-87 |
5.10e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 38.41 E-value: 5.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707892 24 AVRGVSFSLKKGEVVGIVGESGSGKSVMAKsvmaLVTSPGKVKEGEILFQNENVLSKSEKELRS 87
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAM----LLTGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
121-214 |
9.07e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.69 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707892 121 HQKVKKREaQNIAVNLLKQVGLSSpeeRVRQYP-HELSGGMKQRVMIAMAMSCNPDLLIADEPTTALDVTIQAQILDLMK 199
Cdd:PRK10938 370 YQAVSDRQ-QKLAQQWLDILGIDK---RTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD 445
|
90
....*....|....*
gi 1078707892 200 NLKNETNMSLLLITH 214
Cdd:PRK10938 446 VLISEGETQLLFVSH 460
|
|
| |
