|
Name |
Accession |
Description |
Interval |
E-value |
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-337 |
0e+00 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 784.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 8 TAPQAQQQNNLLLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKFNG 87
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 88 REILNLPEHELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPH 167
Cdd:PRK09473 81 REILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 248 MEYGKARDVFYQPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLEEFAPGRLR 327
Cdd:PRK09473 241 MEYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFGPGRLR 320
|
330
....*....|
gi 556427173 328 ACFKPQEELV 337
Cdd:PRK09473 321 ACFKPVEELL 330
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-335 |
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: 556.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKFNGREILNLPEHEL 98
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVM 178
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFY 258
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 259 QPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC-NSAPPLEEFAPGRLRACFKPQEE 335
Cdd:COG0444 241 NPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCrEEEPPLREVGPGHRVACHLYEEE 318
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-294 |
7.68e-147 |
|
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: 424.48 E-value: 7.68e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVI-GGSAKFNGREILNLPEHE 97
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHpSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRV 177
Cdd:COG4172 86 LRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 556427173 258 YQPAHPYSIGLLNAVPRLDAegeslLTIPGNPPNLLR 294
Cdd:COG4172 246 AAPQHPYTRKLLAAEPRGDP-----RPVPPDAPPLLE 277
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-251 |
7.32e-125 |
|
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: 357.20 E-value: 7.32e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREILNLPEhEL 98
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK---PTSGSIIFDGKDLLKLSR-RL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEEsVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVM 178
Cdd:cd03257 77 RKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKE-AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-334 |
2.58e-123 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 357.12 E-value: 2.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTF-------KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIL 91
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTS---GEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 92 NLPEHELNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKM-PEARKRmrmFPHEFS 170
Cdd:COG4608 84 GLSGRELRPLRR-RMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR---YPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 251 GKARDVFYQPAHPYSIGLLNAVPRLDAEGES---LLTipGNPPNLLRLPKGCPFQPRCPHAMEIC-NSAPPLEEFAPGRL 326
Cdd:COG4608 240 APRDELYARPLHPYTQALLSAVPVPDPERRReriVLE--GDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLREVGPGHQ 317
|
....*...
gi 556427173 327 RACFKPQE 334
Cdd:COG4608 318 VACHLAEE 325
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-278 |
3.33e-109 |
|
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: 327.63 E-value: 3.33e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKT-PDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHE 97
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS---GSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARkrMRMFPHEFSGGMRQRV 177
Cdd:COG1123 337 LRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDL--ADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
250 260
....*....|....*....|.
gi 556427173 258 YQPAHPYSIGLLNAVPRLDAE 278
Cdd:COG1123 494 ANPQHPYTRALLAAVPSLDPA 514
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-332 |
6.26e-108 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 317.84 E-value: 6.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANG-VIGGSAKFNGREILNLPEHE 97
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRV 177
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 258 YQPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLEEFAPGRLRACFKP 332
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKCHYP 317
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-295 |
1.24e-107 |
|
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: 323.78 E-value: 1.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKFNGREILNLPEHel 98
Cdd:COG1123 4 LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 nkLRAEQISMIFQDPMTSLNPyMRVGEQLMEVLMLHkGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVM 178
Cdd:COG1123 80 --LRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENL-GLSRAEARARVLELLEAVGLERRLDR---YPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFY 258
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 556427173 259 QPAhpysigLLNAVPRLDAEGESLLTIPGNPPNLLRL 295
Cdd:COG1123 233 APQ------ALAAVPRLGAARGRAAPAAAAAEPLLEV 263
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-276 |
2.70e-98 |
|
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: 300.45 E-value: 2.70e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 8 TAPQAQQQNNLLLDVKDLRVTFKTPDG-------DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngviG 80
Cdd:COG4172 264 DPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS----E 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 81 GSAKFNGREILNLPEHELNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHK-GLGKAEAFEESVKMLDAVKM-PEA 158
Cdd:COG4172 340 GEIRFDGQDLDGLSRRALRPLRR-RMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 159 RKRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDK 238
Cdd:COG4172 419 RHR---YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHR 495
|
250 260 270
....*....|....*....|....*....|....*...
gi 556427173 239 VLVMYAGRTMEYGKARDVFYQPAHPYSIGLLNAVPRLD 276
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-294 |
9.92e-98 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 298.93 E-value: 9.92e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVI--GGSAKFNGREILNLPEH 96
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 ELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQR 176
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 556427173 257 FYQPAHPYSIGLLNAVPRLDAegeslLTIPGNPPNLLR 294
Cdd:PRK15134 245 FSAPTHPYTQKLLNSEPSGDP-----VPLPEPASPLLD 277
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-277 |
1.78e-93 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 290.60 E-value: 1.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKF----NGREILNLP 94
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 95 EH---ELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSG 171
Cdd:PRK10261 92 EQsaaQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|....*.
gi 556427173 252 KARDVFYQPAHPYSIGLLNAVPRLDA 277
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQLGA 277
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-331 |
4.95e-93 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 280.05 E-value: 4.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 14 QQNNLLLDVKDLRVTFKTPDGD---------VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAK 84
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD---GEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 85 FNGREILNLPEHELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVL-MLHKGLGKAEAFEESVKMLDAVKM-PEARKRm 162
Cdd:PRK15079 80 WLGKDLLGMKDDEWRAVRSD-IQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLlPNLINR- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 163 rmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:PRK15079 158 --YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 243 YAGRTMEYGKARDVFYQPAHPYSIGLLNAVPRLDAEGESLLTI---PGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLE 319
Cdd:PRK15079 236 YLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIqllEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL 315
|
330
....*....|..
gi 556427173 320 EFAPGRLRACFK 331
Cdd:PRK15079 316 EGSFRHAVSCLK 327
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-336 |
9.24e-91 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 274.15 E-value: 9.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 15 QNNLLLDVKDL-------RVTFKtPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMgllaangVI----GGSA 83
Cdd:PRK11308 1 SQQPLLQAIDLkkhypvkRGLFK-PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-------MIetptGGEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 84 KFNGREILNlPEHELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKM-PEARKRm 162
Cdd:PRK11308 73 YYQGQDLLK-ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 163 rmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:PRK11308 151 --YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 243 YAGRTMEYGKARDVFYQPAHPYSIGLLNAVPRLDAEGESL-LTIPGNPPNLLRLPKGCPFQPRCPHAMEICNS-APPLEE 320
Cdd:PRK11308 229 YLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLNPDDRRErIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQeQPQLRD 308
|
330
....*....|....*.
gi 556427173 321 FApGRLRACFKPQEEL 336
Cdd:PRK11308 309 YD-GRLVACFAVEQDE 323
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-278 |
2.92e-90 |
|
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: 270.14 E-value: 2.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlpEHEL 98
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS---GEVTFDGRPV----TRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkglGKAEAFEESVKMLDAVKMPEA-RKRmrmFPHEFSGGMRQRV 177
Cdd:COG1124 74 RKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLPPSfLDR---YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250 260
....*....|....*....|.
gi 556427173 258 YQPAHPYSIGLLNAVPRLDAE 278
Cdd:COG1124 228 AGPKHPYTRELLAASLAFERA 248
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-319 |
3.03e-90 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 272.93 E-value: 3.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIggSA---KFNGREILNLPE 95
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHV--TAdrfRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 96 HELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGK-----AEAFEESVKMLDAVKMPEARKRMRMFPHEFS 170
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 251 GKARDVFYQPAHPYSIGLLNAVP--RLDAEGESLL-TIPGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLE 319
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPdfRQPLPHKSRLnTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLR 312
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
38-271 |
5.20e-78 |
|
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: 238.42 E-value: 5.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVI-GGSAKFNGREILNLpehelnKLRAEQISMIFQDPMTS 116
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQtSGEILLDGRPLLPL------SIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 117 LNPYMRVGEQLMEVLMLHKGLGKaEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPYSIGLLNA 271
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-332 |
1.99e-74 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 232.77 E-value: 1.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GVIGGSAKFNGREILNLPEHE 97
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVL--MLHKG-------LGKAEAFEesvkMLDAVKMPEARKRMRMFPHE 168
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgWTYKGrwwqrfgWRKRRAIE----LLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 249 EYGKARDVFYQPAHPYSIGLLNAVP---RLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLEEfAPGR 325
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPdfgSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTG-AKNH 317
|
....*..
gi 556427173 326 LRACFKP 332
Cdd:PRK15093 318 LYACHFP 324
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
19-271 |
1.24e-66 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 210.46 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDG-----DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnl 93
Cdd:COG4167 4 LLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTS---GEILINGHKL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 pEHELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKM-PEarkRMRMFPHEFSGG 172
Cdd:COG4167 78 -EYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPE---HANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
250
....*....|....*....
gi 556427173 253 ARDVFYQPAHPYSIGLLNA 271
Cdd:COG4167 234 TAEVFANPQHEVTKRLIES 252
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
19-272 |
3.35e-64 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 203.89 E-value: 3.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAAN-GVIGGSAKFNGRE-----ILN 92
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLYFDlAPTSGSVYYRDRDggprdLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 93 LPEHELNKLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKGLGKAEAFEesvkMLDAVKMPEARkrMRMFP 166
Cdd:COG4107 84 LSEAERRRLRRTDWGMVYQNPRDGLR--MDVsaggniAERLMAAGERHYGDIRARALE----WLERVEIPLER--IDDLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG4107 156 RTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGR 235
|
250 260
....*....|....*....|....*.
gi 556427173 247 TMEYGKARDVFYQPAHPYSIGLLNAV 272
Cdd:COG4107 236 VVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-269 |
3.74e-64 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 211.87 E-value: 3.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 9 APQAQQQNNLLLDVKDLRVTF-------KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGg 81
Cdd:PRK15134 265 PVPLPEPASPLLDVEQLQVAFpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIW- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 82 sakFNGREILNLPEHELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLH-KGLGKAEAFEESVKMLDAVKM-PEAR 159
Cdd:PRK15134 344 ---FDGQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLdPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 160 KRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 239
Cdd:PRK15134 420 HR---YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
|
250 260 270
....*....|....*....|....*....|
gi 556427173 240 LVMYAGRTMEYGKARDVFYQPAHPYSIGLL 269
Cdd:PRK15134 497 IVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-246 |
4.92e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 197.19 E-value: 4.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAAngVIGGSAKFNGREILNLPEHEL 98
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLDR--PTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAEQISMIFQDPmtSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQRVM 178
Cdd:COG1136 81 ARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGR 246
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-276 |
4.05e-61 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 205.86 E-value: 4.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 10 PQAQQQNNL----LLDVKDLRVTFKTPDG-------DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGv 78
Cdd:PRK10261 300 PPIEQDTVVdgepILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 79 igGSAKFNGREILNLPEHELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGLGKAEAFEESVK-MLDAVKM-P 156
Cdd:PRK10261 379 --GEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVH-GLLPGKAAAARVAwLLERVGLlP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 157 EARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGIC 236
Cdd:PRK10261 455 EHAWR---YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERIS 531
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 556427173 237 DKVLVMYAGRTMEYGKARDVFYQPAHPYSIGLLNAVPRLD 276
Cdd:PRK10261 532 HRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVAD 571
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-246 |
9.69e-60 |
|
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: 191.16 E-value: 9.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAAngVIGGSAKFNGREILNLPEHELN 99
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDR--PTSGEVRVDGTDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAEQISMIFQDPmtSLNPYMRVGEQLMeVLMLHKGLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQRVMI 179
Cdd:cd03255 78 AFRRRHIGFVFQSF--NLLPDLTALENVE-LPLLLAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGR 246
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
35-271 |
9.36e-55 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 179.51 E-value: 9.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 35 DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvigGSAKFNGREILNLPEHELNKLRAEQISMIFQDPM 114
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA-----GVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 115 TSLNPYMRVGEQLMEVLmlhKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10418 90 SAFNPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPYSIGLLNA 271
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-256 |
5.06e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.79 E-value: 5.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGvigGSAKFNGREIlnlpEHEL 98
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIrMLLGLLRPTS---GEVRVLGEDV----ARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHkGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVM 178
Cdd:COG1131 69 AEVRR-RIGYVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRK---VGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-295 |
1.29e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 174.11 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLaaNG---VIGGSAKFNGREILNLPEHEL 98
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-T---LIRCI--NLlerPTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAeQISMIFQDP--MTSLN-------PymrvgeqlMEVLmlhkGLGKAEAfEESVK-MLDAVKMPEARKRmrmFPHE 168
Cdd:COG1135 78 RAARR-KIGMIFQHFnlLSSRTvaenvalP--------LEIA----GVPKAEI-RKRVAeLLELVGLSDKADA---YPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 556427173 249 EYGKARDVFYQPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPN--LLRL 295
Cdd:COG1135 221 EQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGGgrLVRL 269
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
19-272 |
1.99e-51 |
|
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: 170.78 E-value: 1.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGR-----EILNL 93
Cdd:TIGR02323 3 LLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDH---GTATYIMRsgaelELYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHELNKLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKGLGKAEAfeesVKMLDAVKMPeaRKRMRMFPH 167
Cdd:TIGR02323 76 SEAERRRLMRTEWGFVHQNPRDGLR--MRVsaganiGERLMAIGARHYGNIRATA----QDWLEEVEID--PTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....*
gi 556427173 248 MEYGKARDVFYQPAHPYSIGLLNAV 272
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
22-260 |
2.80e-51 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 169.68 E-value: 2.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGviGGSAKFNGREILNLPEHELNKL 101
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPT--SGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 102 RAeQISMIFQ--DPMTSLNpymrVGEQLMEVLMLHkGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMI 179
Cdd:cd03258 81 RR-RIGMIFQhfNLLSSRT----VFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKADA---YPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQ 259
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
.
gi 556427173 260 P 260
Cdd:cd03258 232 P 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-264 |
1.60e-50 |
|
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: 168.23 E-value: 1.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHEL 98
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS---GEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAeQISMIFQDP--MTSLNpymrVGEQLMEVLMLHKGLGKAEAfEESVKM-LDAVKMPEARKRMrmfPHEFSGGMRQ 175
Cdd:COG1127 78 YELRR-RIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEI-RELVLEkLELVGLPGAADKM---PSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALD-VTVqAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAR 254
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|
gi 556427173 255 DVFyQPAHPY 264
Cdd:COG1127 228 ELL-ASDDPW 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
14-249 |
9.18e-50 |
|
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: 165.68 E-value: 9.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 14 QQNNLLLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAanG---VIGGSAKFNGREI 90
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLLA--GldrPTSGTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 91 LNLPEHELNKLRAEQISMIFQDPMtsLNPYMRVGEQLMEVLMLhkgLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFS 170
Cdd:COG4181 77 FALDEDARARLRARHVGFVFQSFQ--LLPTLTALENVMLPLEL---AGRRDARARARALLERVGLGH---RLDHYPAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTME 249
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRLVE 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-265 |
1.52e-49 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 166.25 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGR-----EILNL 93
Cdd:PRK11701 6 LLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA---GEVHYRMRdgqlrDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHELNKLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKGLGKAEAfeesVKMLDAVKMPEARkrMRMFPH 167
Cdd:PRK11701 79 SEAERRRLLRTEWGFVHQHPRDGLR--MQVsaggniGERLMAVGARHYGDIRATA----GDWLERVEIDAAR--IDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|....*...
gi 556427173 248 MEYGKARDVFYQPAHPYS 265
Cdd:PRK11701 231 VESGLTDQVLDDPQHPYT 248
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-260 |
1.10e-48 |
|
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: 162.89 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILnlpEHELN 99
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS---GEVLVDGKDIT---KKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRaEQISMIFQDP-----MTSlnpymrVGEqlmEVL--MLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGG 172
Cdd:COG1122 72 ELR-RKVGLVFQNPddqlfAPT------VEE---DVAfgPENLGLPREEIRERVEEALELVGLEHLADR---PPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
....*...
gi 556427173 253 ARDVFYQP 260
Cdd:COG1122 218 PREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
27-246 |
1.88e-47 |
|
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: 159.17 E-value: 1.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLaanGVIGGSAKFNGREILNLPEHELnklrAEQI 106
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDLTKLSLKEL----RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPMTSL-NPymRVGEqlmEVL--MLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMAL 183
Cdd:cd03225 78 GLVFQNPDDQFfGP--TVEE---EVAfgLENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
19-328 |
1.79e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 161.03 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHEl 98
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDS---GRILLDGRDVTGLPPEK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 nklRaeQISMIFQDPmtSLNPYMRVGEQLMEVLMlHKGLGKAEAfEESVK-MLDAVKMPEARKRMrmfPHEFSGGMRQRV 177
Cdd:COG3842 77 ---R--NVGMVFQDY--ALFPHLTVAENVAFGLR-MRGVPKAEI-RARVAeLLELVGLEGLADRY---PHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 258 YQPAHPYS---IGLLNAVP-RLDAEGESLLTIPGNPpnlLRLPKGCPFQP--------RcPHAMEIcnSAPPLEEFAPGR 325
Cdd:COG3842 225 ERPATRFVadfIGEANLLPgTVLGDEGGGVRTGGRT---LEVPADAGLAAggpvtvaiR-PEDIRL--SPEGPENGLPGT 298
|
...
gi 556427173 326 LRA 328
Cdd:COG3842 299 VED 301
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-264 |
6.68e-46 |
|
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: 156.12 E-value: 6.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANGvigGSAKFNGREILNLPEHEL 98
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKS-TLLRLIvGLLRPDS---GEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAeQISMIFQDP--MTSLNpymrVGEQLMEVLMLHKGLGKAEaFEESVKM-LDAVKMPEARKRMrmfPHEFSGGMRQ 175
Cdd:cd03261 73 YRLRR-RMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEE-IREIVLEkLEAVGLRGAEDLY---PAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 556427173 256 VFyQPAHPY 264
Cdd:cd03261 224 LR-ASDDPL 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-272 |
2.33e-45 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 155.73 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKT-----PDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNL 93
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQ---GTVSFRGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEarKRMRMFPHEFSGGM 173
Cdd:TIGR02769 79 DRKQRRAFRRD-VQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKA 253
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
250
....*....|....*....
gi 556427173 254 RDVFyQPAHPYSIGLLNAV 272
Cdd:TIGR02769 236 AQLL-SFKHPAGRNLQSAV 253
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-257 |
2.50e-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: 155.20 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAAngvIGGSAKFNGREILNLPEHE 97
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKP---SSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 lnklRAEQISMIFQDPMTSLNpyMRVgeqlMEVLML----HKGLG---KAEAFEESVKMLDAVKMpeARKRMRMFpHEFS 170
Cdd:COG1120 73 ----LARRIAYVPQEPPAPFG--LTV----RELVALgrypHLGLFgrpSAEDREAVEEALERTGL--EHLADRPV-DELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
....*..
gi 556427173 251 GKARDVF 257
Cdd:COG1120 220 GPPEEVL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
19-242 |
3.64e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.86 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGvigGSAKFNGREILNLPEHe 97
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLrLIAGLEKPTS---GEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 lnklraeqISMIFQDPmtSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRV 177
Cdd:COG1116 82 --------RGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---YPHQLSGGMRQRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-262 |
1.37e-44 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 153.79 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDG-----DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGviggsakfngREILnL 93
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS----------GELL-I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHELN----KLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMpeARKRMRMFPHEF 169
Cdd:PRK15112 73 DDHPLHfgdySYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL--LPDHASYYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250
....*....|...
gi 556427173 250 YGKARDVFYQPAH 262
Cdd:PRK15112 231 RGSTADVLASPLH 243
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-242 |
6.31e-44 |
|
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: 150.31 E-value: 6.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGVI---GGSAKFNGREIlnlpeh 96
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-T---LLRIIA--GLErptSGEVLVDGEPV------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 elnKLRAEQISMIFQDPmtSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQR 176
Cdd:cd03293 69 ---TGPGPDRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-246 |
1.12e-43 |
|
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: 147.93 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEheln 99
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS---GEIKVLGKDIKKEPE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRaEQISMIFQDPmtSLNPYMRVGEQLmevlmlhkglgkaeafeesvkmldavkmpearkrmrmfphEFSGGMRQRVMI 179
Cdd:cd03230 70 EVK-RRIGYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-257 |
2.65e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAangVIGGSAKFNGREIlnlpehe 97
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP---PTSGTVRLFGKPP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 lnKLRAEQISMIFQdpMTSLNPY--MRVgeqlMEVLML----HKGLGK---AEAFEESVKMLDAVKMPE-ARKRMRmfph 167
Cdd:COG1121 71 --RRARRRIGYVPQ--RAEVDWDfpITV----RDVVLMgrygRRGLFRrpsRADREAVDEALERVGLEDlADRPIG---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMyAGRT 247
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGL 216
|
250
....*....|
gi 556427173 248 MEYGKARDVF 257
Cdd:COG1121 217 VAHGPPEEVL 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-246 |
3.14e-43 |
|
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: 148.65 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHEL 98
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTS---GEVLFNGQSLSKLSSNER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAEQISMIFQdpMTSLNPYMRVGEQLMeVLMLHKGLGKAEAFEESVKMLDAVKMpeaRKRMRMFPHEFSGGMRQRVM 178
Cdd:TIGR02211 78 AKLRNKKLGFIYQ--FHHLLPDFTALENVA-MPLLIGKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQ 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-251 |
6.90e-43 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 147.28 E-value: 6.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELN 99
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDS---GEILIDGRDVTGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klraeqISMIFQDPmtSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMI 179
Cdd:cd03259 74 ------IGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
37-272 |
9.91e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 148.68 E-value: 9.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 37 TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKLRAEqISMIFQDPMTS 116
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQ---GNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 117 LNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPE--ARKRmrmfPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsvLDKR----PPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK--ARDVFyqpAHPYSIGLLNAV 272
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPvgDKLTF---SSPAGRVLQNAV 254
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-263 |
4.02e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 146.29 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGvigGSAKFNGREIlNLPEHE 97
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLrCINLLEEPDS---GTITVDGEDL-TDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRAEqISMIFQdpmtSLN--PYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQ 175
Cdd:COG1126 72 INKLRRK-VGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMT-MVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
....*...
gi 556427173 256 VFYQPAHP 263
Cdd:COG1126 223 FFENPQHE 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-263 |
5.33e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.80 E-value: 5.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 23 KDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLaaNGVIGGSAKFNGREILNLPEHELNKLR 102
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLL--ERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 103 aEQISMIFQ--DPMTSLNPYMRVGEQLmEVlmlhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIA 180
Cdd:PRK11153 82 -RQIGMIFQhfNLLSSRTVFDNVALPL-EL----AGTPKAEIKARVTELLELVGLSDKADR---YPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQP 260
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
...
gi 556427173 261 AHP 263
Cdd:PRK11153 233 KHP 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-246 |
5.64e-42 |
|
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: 143.87 E-value: 5.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREIlNLPEHELN 99
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP---DSGSILIDGEDL-TDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRaEQISMIFQDPmtSLNPYMRVGEQLMEVLmlhkglgkaeafeesvkmldavkmpearkrmrmfphefSGGMRQRVMI 179
Cdd:cd03229 73 PLR-RRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-256 |
1.33e-41 |
|
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: 144.89 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGvigGSAKFNGREILNLPEHEL 98
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFnLISGFLRPTS---GSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKL---RAEQISMIFQDpMTSL-NpyMRVGEQLME---VLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSG 171
Cdd:cd03219 73 ARLgigRTFQIPRLFPE-LTVLeN--VMVAAQARTgsgLLLARARREEREARERAEELLERVGLADLADRP---AGELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
....*
gi 556427173 252 KARDV 256
Cdd:cd03219 226 TPDEV 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-197 |
3.41e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.86 E-value: 3.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPEHELNKlraeQISMIFQDPmtSLN 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP---TEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--QLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 119 PYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKR-MRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:pfam00005 72 PRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-251 |
4.22e-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: 141.80 E-value: 4.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 21 DVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGvigGSAKFNGREILNLPEHELN 99
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPSS---GEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAeqismifqdpmtslnpYMrvgEQLMEVL-MLHKglgkaeafeesvkmldavkmpearkRMRMFpHEFSGGMRQRVM 178
Cdd:cd03214 73 RKIA----------------YV---PQALELLgLAHL-------------------------ADRPF-NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
30-246 |
1.33e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 30 KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQtafaLMGLLAAngvI----GGSAKFNGREILNLPEHELNKLRaEQ 105
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYG---EerptSGQVLVNGQDLSRLKRREIPYLR-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDpmTSLNPYMRVGEQLMEVLMLHkGLGKAEAFEESVKMLDAVKMpeaRKRMRMFPHEFSGGMRQRVMIAMALLC 185
Cdd:COG2884 81 IGVVFQD--FRLLPDRTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-251 |
1.55e-40 |
|
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: 141.49 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlpehELN 99
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS---GTAYINGYSIRT----DRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAEqISMIFQDPMtsLNPYMRVgeqlMEVLMLH---KGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQR 176
Cdd:cd03263 72 AARQS-LGYCPQFDA--LFDELTV----REHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANK---RARTLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
34-261 |
1.15e-39 |
|
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: 139.68 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTafaLMGLLAANGVIGGSAKFNGREILNLPEHElnklraEQISMIFQDp 113
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL---LRLIAGFETPTSGEILLDGKDITNLPPHK------RPVNTVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:cd03300 81 -YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRK---PSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPA 261
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-256 |
1.88e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.42 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGvigGSAKFNGREILNLPEHE 97
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVEPTS---GEILVDGQDVTALRGRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRAeQISMIFQDPmtSLNPYMRVgeqLMEVLM-------LHKGL-------GKAEAFE--ESVKMLDavkmpEARKR 161
Cdd:COG3638 75 LRRLRR-RIGMIFQQF--NLVPRLSV---LTNVLAgrlgrtsTWRSLlglfppeDRERALEalERVGLAD-----KAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 162 mrmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 241
Cdd:COG3638 144 ----ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
250
....*....|....*
gi 556427173 242 MYAGRTMEYGKARDV 256
Cdd:COG3638 220 LRDGRVVFDGPPAEL 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
27-273 |
3.30e-39 |
|
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: 139.49 E-value: 3.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlpEHELNKLRaEQI 106
Cdd:TIGR04520 6 VSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTS---GKVTVDGLDTLD--EENLWEIR-KKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPMTSLnpymrVGEQL-------MEVLMLhkglgKAEAFEESVKM-LDAVKMPEARKRMrmfPHEFSGGMRQRVM 178
Cdd:TIGR04520 80 GMVFQNPDNQF-----VGATVeddvafgLENLGV-----PREEMRKRVDEaLKLVGMEDFRDRE---PHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKARDVFY 258
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
250
....*....|....*
gi 556427173 259 QPAHPYSIGLlnAVP 273
Cdd:TIGR04520 226 QVELLKEIGL--DVP 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-246 |
5.48e-39 |
|
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: 135.45 E-value: 5.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREILNLPEHELNKl 101
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK---PTSGEILIDGKDIAKLPLEELRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 102 raeQISMIFQdpmtslnpymrvgeqlmevlmlhkglgkaeafeesvkmldavkmpearkrmrmfpheFSGGMRQRVMIAM 181
Cdd:cd00267 74 ---RIGYVPQ---------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-256 |
1.09e-38 |
|
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: 137.31 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKtpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLaaNGVI---GGSAKFNGREILNLPEH 96
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKS----TLLRCL--NGLVeptSGSVLIDGTDINKLKGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 ELNKLRAeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKGLGKA-------EAFEESVKMLDAVKMPE-ARKRMRmfphE 168
Cdd:cd03256 72 ALRQLRR-QIGMIFQQF--NLIERLSVLENVLSGRLGRRSTWRSlfglfpkEEKQRALAALERVGLLDkAYQRAD----Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
....*...
gi 556427173 249 EYGKARDV 256
Cdd:cd03256 225 FDGPPAEL 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-242 |
1.64e-38 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 136.12 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAAngvIGGSAKFNGREILN-------L 93
Cdd:cd03235 2 VEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLKP---TSGSIRVFGKPLEKerkrigyV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHElnklraeqismifqdpmtSLNPYM--RVGEQLMEVLMLHKGLGK---AEAFEESVKMLDAVKMPE-ARKRMRmfph 167
Cdd:cd03235 74 PQRR------------------SIDRDFpiSVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLSElADRQIG---- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-251 |
2.31e-38 |
|
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: 136.53 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREilnlPEHEL 98
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS---GSILIDGED----VRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRaEQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKGLGKA--EAFEESVKMLDavkMPEARKRmRMfpHEFSGGMRQR 176
Cdd:COG4555 70 REAR-RQIGVLPDERG--LYDRLTVRENIRYFAELYGLFDEElkKRIEELIELLG---LEEFLDR-RV--GELSTGMKKK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-278 |
2.55e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 139.13 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIL-NLPEHEL 98
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDS---GRIVLNGRDLFtNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NklraeqISMIFQDPMtsLNPYMRVGEQL---MEVlmlhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQ 175
Cdd:COG1118 76 R------VGFVFQHYA--LFPHMTVAENIafgLRV----RPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
250 260
....*....|....*....|...
gi 556427173 256 VFYQPAHPYSIGLLNAVPRLDAE 278
Cdd:COG1118 221 VYDRPATPFVARFLGCVNVLRGR 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-246 |
5.34e-38 |
|
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: 133.28 E-value: 5.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKlraeQI 106
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTS---GEILIDGVDLRDLDLESLRK----NI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPmtslnpymrvgeqlmeVLmlhkglgkaeaFEESVKmldavkmpearkrmrmfphE--FSGGMRQRVMIAMALL 184
Cdd:cd03228 79 AYVPQDP----------------FL-----------FSGTIR-------------------EniLSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-264 |
1.49e-37 |
|
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: 135.08 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLaaNGVI---GGSAKFNGREILNLPEHELNKLRAEQISMIF 110
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCI--NRLIeptSGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 111 QDpmTSLNPYMRVGEQL---MEVlmlhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRP 187
Cdd:cd03294 109 QS--FALLPHRTVLENVafgLEV----QGVPRAEREERAAEALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 188 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPY 264
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
40-246 |
6.10e-37 |
|
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: 132.06 E-value: 6.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 40 NDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAAngVIGGSAKFNGREILNLPEHELNKLRaEQISMIFQDpmTSLNP 119
Cdd:TIGR02982 22 FDINLEINPGEIVILTGPSGSGKT-TLLTLIGGLRS--VQEGSLKVLGQELHGASKKQLVQLR-RRIGYIFQA--HNLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 120 YMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMpeaRKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:TIGR02982 96 FLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556427173 200 DVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGR 246
Cdd:TIGR02982 173 DSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGK 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-246 |
8.03e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.48 E-value: 8.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELN 99
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS---GEIYLDGKPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KlraeQISMIFQDPmtSLnPYMRVGEQLMEVLMLHKGLGKAEAFEEsvkMLDAVKMPEA--RKRMrmfpHEFSGGMRQRV 177
Cdd:COG4619 74 R----QVAYVPQEP--AL-WGGTVRDNLPFPFQLRERKFDRERALE---LLERLGLPPDilDKPV----ERLSGGERQRL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-256 |
1.44e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 133.31 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREI----LN--- 92
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS---GEVLWDGEPLdpedRRrig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 93 -LPEhElnklRaeqismifqdpmtSLNPYMRVGEQLMEVLMLHkGLGKAEAFEESVKMLDAVKMPEARKRMRmfpHEFSG 171
Cdd:COG4152 75 yLPE-E----R-------------GLYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANKKV---EELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 GMRQRVMIAMALLCRPKLLIADEPTTALD-VTVQAqIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
....*.
gi 556427173 251 GKARDV 256
Cdd:COG4152 211 GSVDEI 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-246 |
5.22e-36 |
|
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: 129.80 E-value: 5.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlpehELN 99
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS---GRATVAGHDVVR----EPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRaEQISMIFQDPmtSLNPYMrVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVMI 179
Cdd:cd03265 70 EVR-RRIGIVFQDL--SVDDEL-TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRL---VKTYSGGMRRRLEI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-251 |
1.62e-35 |
|
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: 128.17 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELN 99
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS---GEVLFDGKPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAEQismifqdpmtSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPE-ARKRMRmfphEFSGGMRQRVM 178
Cdd:cd03269 74 YLPEER----------GLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-256 |
2.19e-35 |
|
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: 128.07 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQT--AFALMGLLAANGVIGGSAKFNGREILNLPEHE 97
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLlrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNkLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmRMFPHEFSGGMRQR 176
Cdd:cd03260 77 LE-LRR-RVGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-256 |
3.65e-35 |
|
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: 128.18 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLlaaNGVIGGSAKFNGREILNLPEHEL 98
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL---VEPSSGSILLEGTDITKLRGKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRAeQISMIFQD-----PMTSL-NPYM-RVGEQ--LMEVLMLHKGLGKAEAFEesvkMLDAVKMPE-ARKRMRmfphE 168
Cdd:TIGR02315 75 RKLRR-RIGMIFQHynlieRLTVLeNVLHgRLGYKptWRSLLGRFSEEDKERALS----ALERVGLADkAYQRAD----Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
....*...
gi 556427173 249 EYGKARDV 256
Cdd:TIGR02315 226 FDGAPSEL 233
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
34-240 |
9.58e-35 |
|
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: 125.81 E-value: 9.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLaaNGVIGGSAKFNGREILNLPEHELNKLRAEQISMIFQDp 113
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLL--EKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQN- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVGEQLMEVLMLHKgLGKAEAFEESVKMLDAVKMpeaRKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:TIGR03608 85 -FALIENETVEENLDLGLKYKK-LSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLgVVAGICDKVL 240
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
41-260 |
1.75e-34 |
|
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: 126.30 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLLaanGVIGGSAKFNGREILNLPEHElnklraEQISMIFQDpmTSLNPY 120
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFI---KPDSGKILLNGKDITNLPPEK------RDISYVPQN--YALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 121 MRVGEQLmEVLMLHKGLGKAEAFEesvKMLDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:cd03299 86 MTVYKNI-AYGLKKRKVDKKEIER---KVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQP 260
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-246 |
2.70e-34 |
|
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: 124.95 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlNLPEHELN 99
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS---GTIIIDGLKL-TDDKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAEqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQRVMI 179
Cdd:cd03262 73 ELRQK-VGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
26-264 |
7.40e-34 |
|
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: 124.72 E-value: 7.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKTPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTafalMGLLaaNGVI---GGSAKFNGREILNLPEHELNKlr 102
Cdd:cd03295 5 NVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTT----MKMI--NRLIeptSGEIFIDGEDIREQDPVELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 103 aeQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKRMRmFPHEFSGGMRQRVMIAMA 182
Cdd:cd03295 76 --KIGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAEFADR-YPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 183 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAH 262
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
..
gi 556427173 263 PY 264
Cdd:cd03295 230 DF 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-246 |
1.06e-33 |
|
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: 123.70 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 17 NLLLDVKDLRVTFK--TPDG-DVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAAN-----GVIGGSAKFNGR 88
Cdd:COG4778 2 TTLLEVENLSKTFTlhLQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIYGNylpdsGSILVRHDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 89 EILNLPEHELNKLRAEQISMIFQdpmtSLNPYMRVG--EQLMEVLmLHKGLGKAEAFEESVKMLDAVKMPEarKRMRMFP 166
Cdd:COG4778 78 DLAQASPREILALRRRTIGYVSQ----FLRVIPRVSalDVVAEPL-LERGVDREEARARARELLARLNLPE--RLWDLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-252 |
1.60e-33 |
|
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: 129.88 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 9 APQAQQQNNLLLDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGR 88
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS---GSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 89 EILNLPEHELNKlraeQISMIFQDP----MTslnpymrvgeqLMEVLMLhkglGKAEAFEEsvKMLDAVKMPEARKRMRM 164
Cdd:COG4988 400 DLSDLDPASWRR----QIAWVPQNPylfaGT-----------IRENLRL----GRPDASDE--ELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 165 FPHEF-----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVA 233
Cdd:COG4988 459 LPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA 536
|
250
....*....|....*....
gi 556427173 234 gICDKVLVMYAGRTMEYGK 252
Cdd:COG4988 537 -QADRILVLDDGRIVEQGT 554
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
34-260 |
1.69e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.58 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL--AANGV--IGGSaKFNGREILNlpEHELNKLRaEQISMI 109
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDSGQlnIAGH-QFDFSQKPS--EKAIRLLR-QKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 110 FQDpmTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:COG4161 88 FQQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGKArDVFYQP 260
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQP 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
34-260 |
2.31e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.20 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL--AANGV--IGGSaKFNGREILNlpEHELNKLRaEQISMI 109
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRSGTlnIAGN-HFDFSKTPS--DKAIRELR-RNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 110 FQDpmTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK11124 88 FQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGKArDVFYQP 260
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQP 231
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
34-246 |
3.27e-33 |
|
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: 124.42 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEhelnKLRaEQISMIFQDP 113
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTS---GTARVAGYDVVREPR----KVR-RSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mtslnpymRVGEQL--MEVLMLHK---GLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:TIGR01188 76 --------SVDEDLtgRENLEMMGrlyGLPKDEAEERAEELLELFELGEAADRP---VGTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGR 201
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-255 |
9.46e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 127.57 E-value: 9.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 3 IIETATAPQAQQQNNLLLDvkdlRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGS 82
Cdd:COG4987 319 VTEPAEPAPAPGGPSLELE----DVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS---GS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 83 AKFNGREILNLPEHELnklrAEQISMIFQDP---MTSL--NpyMRVG------EQLMEVLmlHK-GLGK-AEAFEESvkm 149
Cdd:COG4987 392 ITLGGVDLRDLDEDDL----RRRIAVVPQRPhlfDTTLreN--LRLArpdatdEELWAAL--ERvGLGDwLAALPDG--- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 150 LDAVkMPEARKRmrmfpheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDL 229
Cdd:COG4987 461 LDTW-LGEGGRR-------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL 530
|
250 260
....*....|....*....|....*.
gi 556427173 230 gVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:COG4987 531 -AGLERMDRILVLEDGRIVEQGTHEE 555
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
26-251 |
1.18e-32 |
|
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: 128.03 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPeheLNKLRaEQ 105
Cdd:COG2274 478 NVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS---GRILIDGIDLRQID---PASLR-RQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDPM----------TSLNPYMRVgEQLMEVLMLhkglgkAEAFEESVKM---LDAVKMPEARKrmrmfpheFSGG 172
Cdd:COG2274 551 IGVVLQDVFlfsgtireniTLGDPDATD-EEIIEAARL------AGLHDFIEALpmgYDTVVGEGGSN--------LSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYG 251
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
19-263 |
1.24e-32 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 124.22 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGviGGSAKFNGREILNLPEHEL 98
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERPT--SGSVIVDGQDLTTLSNSEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRaEQISMIFQ--DPMTSLNPYMRVGEQLmEVlmlhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQR 176
Cdd:TIGR02314 78 TKAR-RQIGMIFQhfNLLSSRTVFGNVALPL-EL----DNTPKDEIKRKVTELLALVGLGDKHDS---YPSNLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:TIGR02314 149 VAIARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEI 228
|
....*..
gi 556427173 257 FYQPAHP 263
Cdd:TIGR02314 229 FSHPKTP 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-251 |
5.12e-32 |
|
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: 118.94 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 43 NFNLRA-----GETLGIVGESGSGKSQTAFALMGLLAANG---VIGGSAKFNGREILNLPEHElnklraEQISMIFQDpm 114
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGgtiVLNGTVLFDSRKKINLPPQQ------RKIGLVFQQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 115 TSLNPYMRVGEQLMEVLMLHKGLGKAEAFEEsvkMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRNREDRISVDE---LLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
27-246 |
7.16e-32 |
|
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: 118.50 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLL-AANGVIGGSAKFNGREILNLPEHELNKLRaEQ 105
Cdd:TIGR02673 7 VSKAYP-GGVAALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLyGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDpmTSLNPYMRVGEQL---MEVLmlhkGLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQRVMIAMA 182
Cdd:TIGR02673 81 IGVVFQD--FRLLPDRTVYENValpLEVR----GKKEREIQRRVGAALRQVGLEH---KADAFPEQLSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556427173 183 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-268 |
7.58e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.51 E-value: 7.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLrvTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGVIggsaKFNGREilnLPEHE 97
Cdd:PRK13635 5 IIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTI----TVGGMV---LSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRaEQISMIFQDPMTSLnpymrVGEQLMEVLmlhkglgkaeAF---------EESVKMLDavkmpEARKRMRM--F- 165
Cdd:PRK13635 76 VWDVR-RQVGMVFQNPDNQF-----VGATVQDDV----------AFglenigvprEEMVERVD-----QALRQVGMedFl 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 166 ---PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVM 242
Cdd:PRK13635 135 nrePHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM 213
|
250 260
....*....|....*....|....*.
gi 556427173 243 YAGRTMEYGKARDVFYQPAHPYSIGL 268
Cdd:PRK13635 214 NKGEILEEGTPEEIFKSGHMLQEIGL 239
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
34-275 |
1.96e-31 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 118.36 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPehelnkLRAEQISMIFQDp 113
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDS---GRIRLNGQDATRVH------ARDRKIGFVFQH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVGEQLMEVLMLHKgLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:TIGR00968 81 -YALFKHLTVRDNIAFGLEIRK-HPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVALARALAVEPQVLLLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPYSIGLLNAVP 273
Cdd:TIGR00968 156 EPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
|
..
gi 556427173 274 RL 275
Cdd:TIGR00968 236 VL 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-296 |
4.06e-31 |
|
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: 120.21 E-value: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 24 DLRVTFKTPDGDVTAvndlnfnlragetlgIVGESGSGKSQTAFALMGLL-AANG--VIGGSAKFNGREILNLPEHElnk 100
Cdd:COG4148 15 TLDVDFTLPGRGVTA---------------LFGPSGSGKTTLLRAIAGLErPDSGriRLGGEVLQDSARGIFLPPHR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 101 lRaeQISMIFQDPmtSLNPYMRVGEQLMEvlmlhkGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVMIA 180
Cdd:COG4148 77 -R--RIGYVFQEA--RLFPHLSVRGNLLY------GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQP 260
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 556427173 261 AHPYSIGLLNAVPRLDAE--------GESLLTIPGNPpnlLRLP 296
Cdd:COG4148 226 DLLPLAGGEEAGSVLEATvaahdpdyGLTRLALGGGR---LWVP 266
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
34-264 |
5.18e-31 |
|
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: 119.76 E-value: 5.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEhelnklRAEQISMIFQDp 113
Cdd:TIGR03265 15 GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTA---GTIYQGGRDITRLPP------QKRDYGIVFQS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVgEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:TIGR03265 85 -YALFPNLTV-ADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPY 264
Cdd:TIGR03265 160 EPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPF 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-246 |
5.95e-31 |
|
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: 115.22 E-value: 5.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTfktpdgdvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHEL 98
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAS---GEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRaeqISMIFQDPM-TSLNPYMRVGEQLMevlmlhkglgkaeafeesvkmldavkmpearkrmrmFPHEFSGGMRQRV 177
Cdd:cd03215 73 IRAG---IAYVPEDRKrEGLVLDLSVAENIA------------------------------------LSSLLSGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-264 |
9.38e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.02 E-value: 9.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELN 99
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTS---GEILIGGRDVTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klraeqISMIFQDPMtsLNPYMRVGEQL---MEVlmlhKGLGKAEAfEESVK-MLDAVKMPE--ARKrmrmfPHEFSGGM 173
Cdd:COG3839 77 ------IAMVFQSYA--LYPHMTVYENIafpLKL----RKVPKAEI-DRRVReAAELLGLEDllDRK-----PKQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD------LGvvagicDKVLVMYAGRT 247
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRI 212
|
250
....*....|....*..
gi 556427173 248 MEYGKARDVFYQPAHPY 264
Cdd:COG3839 213 QQVGTPEELYDRPANLF 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-269 |
1.10e-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: 116.28 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPehelnkL 101
Cdd:cd03296 5 VRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDS---GTILFGGEDATDVP------V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 102 RAEQISMIFQDpmTSLNPYMRVGEQL---MEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVM 178
Cdd:cd03296 72 QERNVGFVFQH--YALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFY 258
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 556427173 259 QPAHPYSIGLL 269
Cdd:cd03296 227 HPASPFVYSFL 237
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
249-331 |
2.25e-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: 110.53 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 249 EYGKARDVFYQPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNS-APPLEEFAPGRLR 327
Cdd:TIGR01727 4 ETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKePPALVEIAEGHRV 83
|
....
gi 556427173 328 ACFK 331
Cdd:TIGR01727 84 ACHL 87
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-245 |
5.00e-30 |
|
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: 113.51 E-value: 5.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKTPDGdVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlpehelnKLRAEQ 105
Cdd:cd03226 4 NISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESS---GSILLNGKPIKA-------KERRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDPMTSLnpYMR-VGEQLMEVLM-LHKGLGKAEafeESVKMLDAVKMPEARkrmrmfPHEFSGGMRQRVMIAMAL 183
Cdd:cd03226 73 IGYVMQDVDYQL--FTDsVREELLLGLKeLDAGNEQAE---TVLKDLDLYALKERH------PLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-251 |
7.63e-30 |
|
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: 113.36 E-value: 7.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPeheLNKLRaEQI 106
Cdd:cd03244 8 VSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL---SSGSILIDGVDISKIG---LHDLR-SRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPMT-------SLNPYMRVG-EQLMEVLmlhkglgkaeafeESVKMLDAVKMPEARKRMRMfpHE----FSGGMR 174
Cdd:cd03244 81 SIIPQDPVLfsgtirsNLDPFGEYSdEELWQAL-------------ERVGLKEFVESLPGGLDTVV--EEggenLSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE---AFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-262 |
8.91e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.10 E-value: 8.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGVIGGSAKFNGREILNlPEH 96
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYS-PRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 ELNKLRAEqISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGLGKA---EAFEESVKmlDAVKMPEARKRMRMFPHEFSGG 172
Cdd:PRK14239 80 DTVDLRKE-IGMVFQQP----NPFpMSIYENVVYGLRLKGIKDKQvldEAVEKSLK--GASIWDEVKDRLHDSALGLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
250
....*....|
gi 556427173 253 ARDVFYQPAH 262
Cdd:PRK14239 231 TKQMFMNPKH 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-262 |
1.52e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.47 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGL--LAANGVIGGSAKFNGREILNLPEHE 97
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKlraeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKGL-GKAEAFEESVKMLDAVKM-PEARKRMRMFPHEFSGGMRQ 175
Cdd:PRK14247 80 LRR----RVQMVFQIP--NPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwDEVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....*..
gi 556427173 256 VFYQPAH 262
Cdd:PRK14247 232 VFTNPRH 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-246 |
2.98e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 4 IETATAPQAQQQNNLLLDVKDLRVTfktpdgdvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSA 83
Cdd:COG1129 241 LEDLFPKRAAAPGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA---DSGEI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 84 KFNGREILN-------------LPEHelnklRAEQ-----------ISMifqdpmTSLNPYMRVGeqlmevlMLHKGLGK 139
Cdd:COG1129 310 RLDGKPVRIrsprdairagiayVPED-----RKGEglvldlsirenITL------ASLDRLSRGG-------LLDRRRER 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 140 AEAfEESVKMLDaVKMPEARKRMRmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfN 219
Cdd:COG1129 372 ALA-EEYIKRLR-IKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-G 444
|
250 260
....*....|....*....|....*..
gi 556427173 220 TAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG1129 445 KAVIVISSELPELLGLSDRILVMREGR 471
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-246 |
3.91e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFK--TPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGVI---GGSAKFNGREILNLP 94
Cdd:COG1101 2 LELKNLSKTFNpgTVN-EKRALDGLNLTIEEGDFVTVIGSNGAGKS-T---LLNAIA--GSLppdSGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 95 EHElnklRAEQISMIFQDPMTSLNPYMRVGEQLM------EVLMLHKGLGKA--EAFEESVKMLDavkMP-EARKRMRMf 165
Cdd:COG1101 75 EYK----RAKYIGRVFQDPMMGTAPSMTIEENLAlayrrgKRRGLRRGLTKKrrELFRELLATLG---LGlENRLDTKV- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 166 pHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH------DLGvvagicDKV 239
Cdd:COG1101 147 -GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeqalDYG------NRL 219
|
....*..
gi 556427173 240 LVMYAGR 246
Cdd:COG1101 220 IMMHEGR 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-251 |
6.56e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 6.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFkTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFAL-MGLLAANGvigGSAKFNGREILNLPeheLNKLRaEQ 105
Cdd:COG1132 345 VSF-SYPGDRPVLKDISLTIPPGETVALVGPSGSGKS-TLVNLlLRFYDPTS---GRILIDGVDIRDLT---LESLR-RQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDP----MTslnpymrVGEQLmevlmlhkGLGKAEAFEESVKmlDAVKMPEARKRMRMFPH-----------EFS 170
Cdd:COG1132 416 IGVVPQDTflfsGT-------IRENI--------RYGRPDATDEEVE--EAAKAAQAHEFIEALPDgydtvvgergvNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
.
gi 556427173 251 G 251
Cdd:COG1132 556 G 556
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
19-242 |
7.56e-29 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL 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 C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 110.94 E-value: 7.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPD-GDV--TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMG-LLAANGVIGGSAKFNGREILNLP 94
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQqGGVrlPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnYLPDSGRILVRHEGAWVDLAQAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 95 EHELNKLRAEQISMIFQdpmtslnpYMRVGEQL--MEVLM---LHKGLGKAEAFEESVKMLDAVKMPEarKRMRMFPHEF 169
Cdd:TIGR02324 81 PREVLEVRRKTIGYVSQ--------FLRVIPRVsaLEVVAeplLERGVPREAARARARELLARLNIPE--RLWHLPPATF 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:TIGR02324 151 SGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-228 |
8.06e-29 |
|
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: 110.26 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGvigGSAKFNGREILNLPEHe 97
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKT-TLLrILAGLLPPSA---GEVLWNGEPIRDARED- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 lnklRAEQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKGLGKAEAFEEsvkMLDAVKMPEARKRmrmFPHEFSGGMRQRV 177
Cdd:COG4133 73 ----YRRRLAYLGHADG--LKPELTVRENLRFWAALYGLRADREAIDE---ALEAVGLAGLADL---PVRQLSAGQKRRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 228
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
248-312 |
1.11e-28 |
|
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: 105.56 E-value: 1.11e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 248 MEYGKARDVFYQPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC 312
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
34-251 |
1.15e-28 |
|
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: 110.04 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLlaaNGVIGGSAKFNGREILNLPEHELNklraeqISMIFQDp 113
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL---EEPTSGRIYIGGRDVTDLPPKDRD------IAMVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVGEQLMEVLMLHKGlgKAEAFEESVKmlDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:cd03301 81 -YALYPHMTVYDNIAFGLKLRKV--PKDEIDERVR--EVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-264 |
1.42e-28 |
|
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: 113.28 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANG---VIGGSAKFNGREILNLPEHElnklRAeqISMIFQDpmTSL 117
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEgeiVLNGRTLFDSRKGIFLPPEK----RR--IGYVFQE--ARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 118 NPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMpearkrMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:TIGR02142 87 FPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 198 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPY 264
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-268 |
1.96e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.36 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLrvTFK-TPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREilnLPEHE 97
Cdd:PRK13650 4 IIEVKNL--TFKyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES---GQIIIDGDL---LTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRaEQISMIFQDPMTSLnpymrVG---EQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMR 174
Cdd:PRK13650 76 VWDIR-HKIGMVFQNPDNQF-----VGatvEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKERE---PARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGKAR 254
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPR 225
|
250
....*....|....
gi 556427173 255 DVFYQPAHPYSIGL 268
Cdd:PRK13650 226 ELFSRGNDLLQLGL 239
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
38-275 |
2.60e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.91 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlPEHELNKLRaEQISMIFQDPMTSL 117
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS---GKIIIDGVDITD-KKVKLSDIR-KKVGLVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 118 npYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMP-EARKRMRmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:PRK13637 97 --FEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKS--PFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPYSIGLlnAVPRL 275
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIGL--AVPQV 249
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-268 |
8.67e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.41 E-value: 8.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 17 NLLLDVKDLRVTFKTpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREilnLPEH 96
Cdd:PRK13642 2 NKILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE---FEGKVKIDGEL---LTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 ELNKLRaEQISMIFQDPMTSLnpymrVGEQLMEVL---MLHKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGM 173
Cdd:PRK13642 75 NVWNLR-RKIGMVFQNPDNQF-----VGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKA 253
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
250
....*....|....*
gi 556427173 254 RDVFYQPAHPYSIGL 268
Cdd:PRK13642 225 SELFATSEDMVEIGL 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-251 |
9.17e-28 |
|
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: 107.69 E-value: 9.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlpehelN 99
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS---GEITFDGKSYQK------N 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAEQISMIFQDPmtSLNPYMRVGEQLmEVLMLHKGLGKAEAFEesvkMLDAVKMPE-ARKRMRmfphEFSGGMRQRVM 178
Cdd:cd03268 68 IEALRRIGALIEAP--GFYPNLTARENL-RLLARLLGIRKKRIDE----VLDVVGLKDsAKKKVK----GFSLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-251 |
1.02e-27 |
|
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: 107.84 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPehel 98
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA---GFATVDGFDVVKEP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 nklRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVM 178
Cdd:cd03266 74 ---AEARRRLGFVSDSTGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRR---VGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-256 |
1.19e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 107.52 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREILNLPEHELN 99
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---PRSGSIRFDGRDITGLPPHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLraeQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKmpEARKRMrmfPHEFSGGMRQRVMI 179
Cdd:cd03224 74 RA---GIGYVPEGRR--IFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK--ERRKQL---AGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-256 |
1.25e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.43 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTfktPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgviGGSAKFNGREILNLPEHEl 98
Cdd:COG3845 257 VLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA---SGSIRLDGEDITGLSPRE- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 nkLRAEQISMIFQDPM-TSLNPYMRVGEQLmeVLMLH-------KGL---GKAEAF-EESVKMLDaVKMPEARKRMRMfp 166
Cdd:COG3845 330 --RRRLGVAYIPEDRLgRGLVPDMSVAENL--ILGRYrrppfsrGGFldrKAIRAFaEELIEEFD-VRTPGPDTPARS-- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 167 heFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG3845 403 --LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGR 479
|
250
....*....|
gi 556427173 247 TMEYGKARDV 256
Cdd:COG3845 480 IVGEVPAAEA 489
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
34-263 |
1.60e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.87 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGVI-GGSAKFNGREILNlPEHELNKLRAEQiSMIFQD 112
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEEItSGDLIVDGLKVND-PKVDERLIRQEA-GMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 113 pmTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PRK09493 86 --FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 193 DEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHP 263
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-256 |
2.76e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGVI---GGSAKFNGREIlnlpe 95
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKS-T---LMKILS--GVYqpdSGEILLDGEPV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 96 HELNKLRAEQ--ISMIFQDPmtSLNPYMRVGEQL-MEVLMLHKGL-GKAEAFEESVKMLDAVKMPE-ARKRMRmfphEFS 170
Cdd:COG1129 69 RFRSPRDAQAagIAIIHQEL--NLVPNLSVAENIfLGREPRRGGLiDWRAMRRRARELLARLGLDIdPDTPVG----DLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
....*.
gi 556427173 251 GKARDV 256
Cdd:COG1129 222 GPVAEL 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-268 |
2.80e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.91 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 16 NNLLLDVKDlrVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlpe 95
Cdd:PRK13648 4 KNSIIVFKN--VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKS---GEIFYNNQAITD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 96 HELNKLRaEQISMIFQDP----MTSLNPYmRVGEQLMEVLMLHKGLGK--AEAFEEsVKMLDavkmpearkRMRMFPHEF 169
Cdd:PRK13648 76 DNFEKLR-KHIGIVFQNPdnqfVGSIVKY-DVAFGLENHAVPYDEMHRrvSEALKQ-VDMLE---------RADYEPNAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTME 249
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYK 222
|
250
....*....|....*....
gi 556427173 250 YGKARDVFYQPAHPYSIGL 268
Cdd:PRK13648 223 EGTPTEIFDHAEELTRIGL 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-246 |
3.86e-27 |
|
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: 105.95 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 30 KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGV-IGGSAKFNGREILNLPEHELNKLRaEQISM 108
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELpTSGTIRVNGQDVSDLRGRAIPYLR-RKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 109 IFQDpmTSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMpeaRKRMRMFPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:cd03292 83 VFQD--FRLLPDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-263 |
3.90e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.04 E-value: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqT---AFALMGLLAANGVIGGSAKFNGREILNlPEH 96
Cdd:COG1117 12 IEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKS-TllrCLNRMNDLIPGARVEGEILLDGEDIYD-PDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 ELNKLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGLGKA---EAFEESVKML---DAVKmpearKRMRMFPHEF 169
Cdd:COG1117 86 DVVELRR-RVGMVFQKP----NPFpKSIYDNVAYGLRLHGIKSKSeldEIVEESLRKAalwDEVK-----DRLKKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVE 233
|
250
....*....|....
gi 556427173 250 YGKARDVFYQPAHP 263
Cdd:COG1117 234 FGPTEQIFTNPKDK 247
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
49-249 |
4.73e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.40 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 49 GETLGIVGESGSGKSqtafALMGLLAanGVIGGSA---KFNGREILNLPEHELNKLRAEQISMIFQDPMtsLNPYMRVGE 125
Cdd:PRK10584 36 GETIALIGESGSGKS----TLLAILA--GLDDGSSgevSLVGQPLHQMDEEARAKLRAKHVGFVFQSFM--LIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 126 QLmEVLMLHKGLGKAEAFEESVKMLDAVKMPearKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 205
Cdd:PRK10584 108 NV-ELPALLRGESSRQSRNGAKALLEQLGLG---KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556427173 206 QIMTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGRTME 249
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-260 |
5.23e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.47 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRvtFKTPDGDVtAVNDLNFNLRAGETLGIVGESGSGKSqTAFalmglLAANGVI---GGSAKFNGREIlNLPE 95
Cdd:PRK13639 1 ILETRDLK--YSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKS-TLF-----LHFNGILkptSGEVLIKGEPI-KYDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 96 HELNKLRaEQISMIFQDPMTSLnpYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQ 175
Cdd:PRK13639 71 KSLLEVR-KTVGIVFQNPDDQL--FAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
....*
gi 556427173 256 VFYQP 260
Cdd:PRK13639 224 VFSDI 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-268 |
5.58e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKFNGreiLNLPEHELNKLRaEQI 106
Cdd:PRK13640 11 VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDG---ITLTAKTVWDIR-EKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPMTSLnpymrVGEQLMEVLML---HKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAMAL 183
Cdd:PRK13640 87 GIVFQNPDNQF-----VGATVGDDVAFgleNRAVPRPEMIKIVRDVLADVGMLDYIDSE---PANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGKARDVFYQPAHP 263
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
....*
gi 556427173 264 YSIGL 268
Cdd:PRK13640 238 KEIGL 242
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-247 |
1.20e-26 |
|
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: 103.28 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLpehelN 99
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS---GEILVDGKEVSFA-----S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAEQ--ISMIFQdpmtslnpymrvgeqlmevlmlhkglgkaeafeesvkmldavkmpearkrmrmfpheFSGGMRQRV 177
Cdd:cd03216 69 PRDARRagIAMVYQ---------------------------------------------------------LSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-263 |
1.78e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.44 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGviGGSAKFNGREI--------- 90
Cdd:PRK10619 6 LNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPS--EGSIVVNGQTInlvrdkdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 91 LNLPEHELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEaRKRMRmFPHEFS 170
Cdd:PRK10619 79 LKVADKNQLRLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE-RAQGK-YPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250
....*....|...
gi 556427173 251 GKARDVFYQPAHP 263
Cdd:PRK10619 234 GAPEQLFGNPQSP 246
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-228 |
2.61e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.94 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlPEHEln 99
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS---GEITLDGVPVTG-PGAD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klRAeqisMIFQDpmTSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMI 179
Cdd:COG4525 78 --RG----VVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARR---RIWQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-264 |
2.73e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 105.94 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTfKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTafalmgLLAANGVI---GGSAKFNGREILNLPEHELNKlr 102
Cdd:COG1125 6 NVT-KRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT------LRMINRLIeptSGRILIDGEDIRDLDPVELRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 103 aeQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEA--RKRmrmFPHEFSGGMRQRVMIA 180
Cdd:COG1125 77 --RIGYVIQQ--IGLFPHMTVAENIATVPRL-LGWDKERIRARVDELLELVGLDPEeyRDR---YPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD------LGvvagicDKVLVMYAGRTMEYGKAR 254
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDidealkLG------DRIAVMREGRIVQYDTPE 222
|
250
....*....|
gi 556427173 255 DVFYQPAHPY 264
Cdd:COG1125 223 EILANPANDF 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-228 |
3.09e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 103.33 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANGVIGGSAKFNGREILNLPEHel 98
Cdd:COG4136 2 LSLENLTITL----GGRPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIaGTLSPAFSASGEVLLNGRRLTALPAE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 nklrAEQISMIFQDPMtsLNPYMRVGEQLMevLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVM 178
Cdd:COG4136 75 ----QRRIGILFQDDL--LFPHLSVGENLA--FALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
41-246 |
3.25e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 104.13 E-value: 3.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLlaaNGVIGGSAKFNGREILNLPEHELNKLRAEQISMIFQdpMTSLNPY 120
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 121 MRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMpEARKRMRmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:PRK11629 102 FTALENVAMPLLI-GKKKPAEINSRALEMLAAVGL-EHRANHR--PSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556427173 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGR 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-263 |
3.30e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL--AANGVIG-GSAKFNGREILNLPEH 96
Cdd:PRK11264 4 IEVKNLVKKFH----GQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRvGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 ELNKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQR 176
Cdd:PRK11264 79 LIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS---YPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
....*..
gi 556427173 257 FYQPAHP 263
Cdd:PRK11264 232 FADPQQP 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-252 |
3.37e-26 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 104.16 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPD-GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAfALmgLLAANGVIGGSAKFNGREILNLPeheLNKLRaEQ 105
Cdd:cd03249 6 VSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVV-SL--LERFYDPTSGEILLDGVDIRDLN---LRWLR-SQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDPMTSlnpYMRVGEQLmevlmlhkGLGKAEAFEESVKmlDAVKMPEARKRMRMFPHEF-----------SGGMR 174
Cdd:cd03249 79 IGLVSQEPVLF---DGTIAENI--------RYGKPDATDEEVE--EAAKKANIHDFIMSLPDGYdtlvgergsqlSGGQK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGK 252
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-257 |
3.61e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLrvTFKTPDGdVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREIlNLPEHEL 98
Cdd:PRK13636 5 ILKVEEL--NYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP---SSGRILFDGKPI-DYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRaEQISMIFQDP---MTSLNPYMRVGEQLMEVlmlhkGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQ 175
Cdd:PRK13636 78 MKLR-ESVGMVFQDPdnqLFSASVYQDVSFGAVNL-----KLPEDEVRKRVDNALKRTGIEHLKDKP---THCLSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
..
gi 556427173 256 VF 257
Cdd:PRK13636 229 VF 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-257 |
3.77e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHEL 98
Cdd:COG4559 1 MLEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSS---GEVRLNGRPLAAWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRA---EQISMIFqdPMTSLnpymrvgeqlmEVLML----HkGLGKAEAFEESVKMLDAVKMpeARKRMRMFPhEFSG 171
Cdd:COG4559 74 ARRRAvlpQHSSLAF--PFTVE-----------EVVALgrapH-GSSAAQDRQIVREALALVGL--AHLAGRSYQ-TLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 GMRQRVMIAMAlLC--------RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMY 243
Cdd:COG4559 137 GEQQRVQLARV-LAqlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLH 214
|
250
....*....|....
gi 556427173 244 AGRTMEYGKARDVF 257
Cdd:COG4559 215 QGRLVAQGTPEEVL 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-257 |
5.03e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 104.69 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlPEHELNKLRaEQI 106
Cdd:PRK13632 13 VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS---GEIKIDGITI---SKENLKEIR-KKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPMTSLnpymrVGeqlmevlmlhkglGKAE---AFEESVKMLDAVKMP----EARKRMRMF------PHEFSGGM 173
Cdd:PRK13632 86 GIIFQNPDNQF-----IG-------------ATVEddiAFGLENKKVPPKKMKdiidDLAKKVGMEdyldkePQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGKA 253
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKP 226
|
....
gi 556427173 254 RDVF 257
Cdd:PRK13632 227 KEIL 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-233 |
5.22e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 108.66 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA-NGVIGGSAKFNGREILNLPEHE 97
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGClDKPTSGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRAEQISMIFQdpMTSLNPYMrVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQRV 177
Cdd:PRK10535 80 LAQLRREHFGFIFQ--RYHLLSHL-TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVA 233
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAA 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-262 |
5.41e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.15 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 17 NLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAN--GVIGGSAKFNGREILNlP 94
Cdd:PRK14267 2 KFAIETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeeARVEGEVRLFGRNIYS-P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 95 EHELNKLRaEQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVK--MLDAVKMPEARKRMRMFPHEFSGG 172
Cdd:PRK14267 77 DVDPIEVR-REVGMVFQYP--NPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwaLKKAALWDEVKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
250
....*....|
gi 556427173 253 ARDVFYQPAH 262
Cdd:PRK14267 232 TRKVFENPEH 241
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-252 |
5.62e-26 |
|
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: 103.46 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGdVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALmgLLAANGVIGGSAKFNGREILNLpehELNKLRaEQI 106
Cdd:cd03253 6 VTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKS-TILRL--LFRFYDVSSGSILIDGQDIREV---TLDSLR-RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDpmTSL-NpymrvgeqlmEVLMLHKGLGKAEAFEESVkmLDAVKMPEARKRMRMFPHEF-----------SGGMR 174
Cdd:cd03253 78 GVVPQD--TVLfN----------DTIGYNIRYGRPDATDEEV--IEAAKAAQIHDKIMRFPDGYdtivgerglklSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGK 252
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-246 |
6.08e-26 |
|
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: 102.66 E-value: 6.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGeTLGIVGESGSGKSqtafALMGLLAanGVI---GGSAKFNGREILNLPEh 96
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILA--TLTppsSGTIRIDGQDVLKQPQ- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 elnKLRAeQISMIFQDPMTSlnPYMRVGEQL--MEVLmlhKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMR 174
Cdd:cd03264 69 ---KLRR-RIGYLPQEFGVY--PNFTVREFLdyIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKK---IGSLSGGMR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-252 |
1.14e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.78 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 12 AQQQNNLLLDVKDL-RVTFKTpdgdVTAVNDLNFNLRAGETLGIVGESGSGKSQTafalMGLLAanGVI---GGSAKFNG 87
Cdd:COG4586 14 YEKEPGLKGALKGLfRREYRE----VEAVDDISFTIEPGEIVGFIGPNGAGKSTT----IKMLT--GILvptSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 88 REilnlPEHELNKLrAEQISMIFqdpmtslnpymrvG--EQL------MEVLMLHK---GLGKAEA---FEESVKMLDA- 152
Cdd:COG4586 84 YV----PFKRRKEF-ARRIGVVF-------------GqrSQLwwdlpaIDSFRLLKaiyRIPDAEYkkrLDELVELLDLg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 153 --VKMPeARK-----RMRMfphEfsggmrqrvmIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMI 225
Cdd:COG4586 146 elLDTP-VRQlslgqRMRC---E----------LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLT 211
|
250 260
....*....|....*....|....*..
gi 556427173 226 THDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:COG4586 212 SHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
42-263 |
1.68e-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: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 42 LNFNL--RAGETLGIVGESGSGKSqTAFALM-GLLAAngvIGGSAKFNGREILNLPEHElnklRAeqISMIFQDpmTSLN 118
Cdd:COG3840 16 LRFDLtiAAGERVAILGPSGAGKS-TLLNLIaGFLPP---DSGRILWNGQDLTALPPAE----RP--VSMLFQE--NNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 119 PYMRVGEQLmeVLMLHKGLGKAEAFEESVK-MLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:COG3840 84 PHLTVAQNI--GLGLRPGLKLTAEQRAQVEqALERVGLAGLLDRL---PGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 198 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHP 263
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-268 |
1.73e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.24 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGD----VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlpEHELNKLR 102
Cdd:PRK13633 10 VSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE---GKVYVDGLDTSD--EENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 103 aEQISMIFQDPMTSLNPYMrVGEqlmEVLMLHKGLG-KAEAFEESV-KMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIA 180
Cdd:PRK13633 85 -NKAGMVFQNPDNQIVATI-VEE---DVAFGPENLGiPPEEIRERVdESLKKVGMYEYRRHA---PHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKARDVFYQP 260
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEV 235
|
....*...
gi 556427173 261 AHPYSIGL 268
Cdd:PRK13633 236 EMMKKIGL 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-270 |
1.89e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.92 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 10 PQAQQQNNL--LLDVKDLRVTFktpDGDvTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA-NGVIGGSAKFN 86
Cdd:PRK11607 8 PQAKTRKALtpLLEIRNLTKSF---DGQ-HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGfEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 87 GREILNLPEHElnklraEQISMIFQDpmTSLNPYMRVgEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMrmfP 166
Cdd:PRK11607 80 GVDLSHVPPYQ------RPINMMFQS--YALFPHMTV-EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---P 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
250 260
....*....|....*....|....*..
gi 556427173 247 TMEYGKARDVFYQPAHPYS---IGLLN 270
Cdd:PRK11607 228 FVQIGEPEEIYEHPTTRYSaefIGSVN 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-257 |
3.05e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPEHEL 98
Cdd:PRK13548 2 MLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSP---DSGEVRLNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRA---EQISMIFqdpmtslnPYmRVGEQlmeVLM--LHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGM 173
Cdd:PRK13548 75 ARRRAvlpQHSSLSF--------PF-TVEEV---VAMgrAPHGLSRAEDDALVAAALAQVDLAHLAGR---DYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 174 RQRVMIAMALL------CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
250
....*....|
gi 556427173 248 MEYGKARDVF 257
Cdd:PRK13548 220 VADGTPAEVL 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-251 |
3.33e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.51 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 17 NLLLDVKDLrvTFKTPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLlaaNGVIGGSAKFNGREILNLPEH 96
Cdd:PRK13647 2 DNIIEVEDL--HFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI---YLPQRGRVKVMGREVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 ELNKlraeQISMIFQDP---MTSLNPYMRV--GEQLMevlmlhkGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSG 171
Cdd:PRK13647 76 WVRS----KVGLVFQDPddqVFSSTVWDDVafGPVNM-------GLDKDEVERRVEEALKAVRMWDFRDKP---PYHLSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-277 |
4.36e-25 |
|
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: 102.96 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 54 IVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHelnkLRAeqISMIFQDpmTSLNPYMRVGEQLMEVLML 133
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS---GSIMLDGEDVTNVPPH----LRH--INMVFQS--YALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 134 hKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNE 213
Cdd:TIGR01187 70 -RKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556427173 214 LKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPYSIGLLNAVPRLDA 277
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEA 209
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
34-264 |
5.96e-25 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 103.64 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafalmgLL-AANGVI---GGSAKFNGREILNLPEHELNKLRAEQISMI 109
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKS-T------LVrCLNRLIeptAGEVLIDGEDITKLSKKELRELRRKKMSMV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 110 FQdpmtS--LNPYMRVGEQL---MEVlmlhKGLGKAEAFEESVKMLDAV--KMPEARkrmrmFPHEFSGGMRQRVMIAMA 182
Cdd:COG4175 111 FQ----HfaLLPHRTVLENVafgLEI----QGVPKAERRERAREALELVglAGWEDS-----YPDELSGGMQQRVGLARA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 183 LLCRPKLLIADEPTTALD----VTVQAQIMTLLNELKRefnTaIIMITHDL------GvvagicDKVLVMYAGRTMEYGK 252
Cdd:COG4175 178 LATDPDILLMDEAFSALDplirREMQDELLELQAKLKK---T-IVFITHDLdealrlG------DRIAIMKDGRIVQIGT 247
|
250
....*....|..
gi 556427173 253 ARDVFYQPAHPY 264
Cdd:COG4175 248 PEEILTNPANDY 259
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-248 |
8.39e-25 |
|
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: 100.48 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 25 LRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGreilNLPEHELNKLRAe 104
Cdd:cd03267 23 LKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS---GEVRVAG----LVPWKRRKKFLR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 105 QISMIFQDPmtslnpymrvgEQL------MEVLMLHK---GLGKAEA---FEESVKMLDAVKMPEARKRmrmfphEFSGG 172
Cdd:cd03267 95 RIGVVFGQK-----------TQLwwdlpvIDSFYLLAaiyDLPPARFkkrLDELSELLDLEELLDTPVR------QLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-251 |
2.23e-24 |
|
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: 98.64 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFkTPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPeheLN 99
Cdd:cd03369 7 IEVENLSVRY-APDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA---EEGKIEIDGIDISTIP---LE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRaEQISMIFQDPM-------TSLNPY-MRVGEQLMEVLMLHKGlgkaeafeesvkmldavkmpearkrmrmfPHEFSG 171
Cdd:cd03369 79 DLR-SSLTIIPQDPTlfsgtirSNLDPFdEYSDEEIYGALRVSEG-----------------------------GLNLSQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:cd03369 129 GQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE---EFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEY 204
|
.
gi 556427173 251 G 251
Cdd:cd03369 205 D 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
38-268 |
2.64e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.09 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILN-LPEHELNKLRaEQISMIFQDPMts 116
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTS---GTVTIGERVITAgKKNKKLKPLR-KKVGIVFQFPE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 117 lnpymrvgEQLMEVLMLHK--------GLGKAEAFEESVKMLDAVKMPEarKRMRMFPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK13634 96 --------HQLFEETVEKDicfgpmnfGVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 189 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPYSIGL 268
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGL 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-256 |
2.65e-24 |
|
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: 103.34 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 14 QQNNLLLDVKDLRVTFKTPD-GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgviggSAKFN---GRE 89
Cdd:TIGR03269 274 EVGEPIIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT-----SGEVNvrvGDE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 90 ILNLPEH-ELNKLRAEQ-ISMIFQDpmTSLNPYMRVGEQLMEVLMLHkgLGKAEAFEESVKMLDAVKMPE--ARKRMRMF 165
Cdd:TIGR03269 349 WVDMTKPgPDGRGRAKRyIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDEekAEEILDKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 166 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
250
....*....|.
gi 556427173 246 RTMEYGKARDV 256
Cdd:TIGR03269 505 KIVKIGDPEEI 515
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-257 |
2.83e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.08 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 17 NLLLDVKDLRVTFKTPdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL---AANGVIGGSAKFNGREILNl 93
Cdd:PRK13645 6 DIILDNVSYTYAKKTP-FEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiseTGQTIVGDYAIPANLKKIK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 pehELNKLRAEqISMIFQDPMTSLnpYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPeaRKRMRMFPHEFSGGM 173
Cdd:PRK13645 84 ---EVKRLRKE-IGLVFQFPEYQL--FQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKA 253
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
....
gi 556427173 254 RDVF 257
Cdd:PRK13645 236 FEIF 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-261 |
3.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.70 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 16 NNLLLDVKDLRVTF--KTPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANG--------VIGGSAKF 85
Cdd:PRK13631 18 DDIILRVKNLYCVFdeKQEN-ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYgtiqvgdiYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 86 NGREILNLPEHELN--KLRaEQISMIFQDPmtslnPYMRVGEQLMEVLM---LHKGLGKAEAFEESVKMLdaVKMPEARK 160
Cdd:PRK13631 97 HELITNPYSKKIKNfkELR-RRVSMVFQFP-----EYQLFKDTIEKDIMfgpVALGVKKSEAKKLAKFYL--NKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 161 RMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVL 240
Cdd:PRK13631 169 YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVI 247
|
250 260
....*....|....*....|.
gi 556427173 241 VMYAGRTMEYGKARDVFYQPA 261
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTDQH 268
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-256 |
4.27e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLM----GLLAANGvigGSAKFNGREI-LNL 93
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKS-T---LMkilyGLYQPDS---GEILIDGKPVrIRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHElnklRAEQISMIFQDPMtsLNPYMRVGEQLMevlmlhkgLGKaeafeESVKMLdAVKMPEARKRMRmfphEFSG-- 171
Cdd:COG3845 74 PRDA----IALGIGMVHQHFM--LVPNLTVAENIV--------LGL-----EPTKGG-RLDRKAARARIR----ELSEry 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 ---------------GMRQRVMIAMALLCRPKLLIADEPTTALdvTVQ--AQIMTLLNELKREfNTAIIMITHDLGVVAG 234
Cdd:COG3845 130 gldvdpdakvedlsvGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMA 206
|
250 260
....*....|....*....|..
gi 556427173 235 ICDKVLVMYAGRTMEYGKARDV 256
Cdd:COG3845 207 IADRVTVLRRGKVVGTVDTAET 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-261 |
5.34e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.79 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 7 ATAPQAQQQNNLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANGvigGSAKF 85
Cdd:PRK09452 2 KKLNKQPSSLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIaGFETPDS---GRIML 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 86 NGREILNLPehelnklrAEQ--ISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgLGKAEaFEESVkmLDAVKMPEARKRMR 163
Cdd:PRK09452 74 DGQDITHVP--------AENrhVNTVFQS--YALFPHMTVFENVAFGLRMQK-TPAAE-ITPRV--MEALRMVQLEEFAQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 164 MFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMY 243
Cdd:PRK09452 140 RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMR 219
|
250
....*....|....*...
gi 556427173 244 AGRTMEYGKARDVFYQPA 261
Cdd:PRK09452 220 DGRIEQDGTPREIYEEPK 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-278 |
8.16e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 8.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLpeHElnklRAEQISMIFQDp 113
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS---GHIRFHGTDVSRL--HA----RDRKVGFVFQH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVGEQL---MEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK10851 83 -YALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 191 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPYSIGLLN 270
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
....*...
gi 556427173 271 AVPRLDAE 278
Cdd:PRK10851 239 EVNRLQGT 246
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-264 |
1.10e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.49 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKLRAEQISMIFQDpmTSL 117
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR---GQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 118 NPYMRVgeqlMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:PRK10070 118 MPHMTV----LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 198 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPY 264
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-242 |
1.45e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 101.21 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 2 TIIETATAPQAQQQNNLLLDVKDLR---VTFKTPDGDVtAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangV 78
Cdd:TIGR02857 299 AVLDAAPRPLAGKAPVTAAPASSLEfsgVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD---P 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 79 IGGSAKFNGREILNLPEHELNKlraeQISMIFQdpmtslNPYMRVGeQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEA 158
Cdd:TIGR02857 375 TEGSIAVNGVPLADADADSWRD----QIAWVPQ------HPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 159 RKRMRMFP-----HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVA 233
Cdd:TIGR02857 444 LPQGLDTPigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA 521
|
....*....
gi 556427173 234 GiCDKVLVM 242
Cdd:TIGR02857 522 L-ADRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-256 |
1.77e-23 |
|
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: 96.59 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREILNLPEHEL 98
Cdd:COG0410 3 MLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP---PRSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRaeqISM------IFqdpmtslnPYMRVGEQLMEVLMLHKGLGKAEAfeesvkMLDAVkmpearkrMRMFP--HEF- 169
Cdd:COG0410 76 ARLG---IGYvpegrrIF--------PSLTVEENLLLGAYARRDRAEVRA------DLERV--------YELFPrlKERr 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 -------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:COG0410 131 rqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVL 209
|
250
....*....|....
gi 556427173 243 YAGRTMEYGKARDV 256
Cdd:COG0410 210 ERGRIVLEGTAAEL 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-256 |
1.84e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.92 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTafalmgLLAANGVI---GGSAKFNGREILNLPEH 96
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTL------LRAINGTLtptAGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 ELNKlraeQISMIFQDpmTSLNPYMRVgEQLMEvLMLHKGLGKAEAFEESVKMldAVKMPEARKRMRMFPH----EFSGG 172
Cdd:PRK09536 74 AASR----RVASVPQD--TSLSFEFDV-RQVVE-MGRTPHRSRFDTWTETDRA--AVERAMERTGVAQFADrpvtSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMItHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGP 222
|
....
gi 556427173 253 ARDV 256
Cdd:PRK09536 223 PADV 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-251 |
4.42e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 94.54 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTPDGDVTA--VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGViGGSAKFNGReilNLPEHE 97
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV-SGEVLINGR---PLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKlraeQISMIFQDPMtsLNPYMRVGEQLMEVLMLhKGLgkaeafeesvkmldavkmpearkrmrmfphefSGGMRQRV 177
Cdd:cd03213 80 FRK----IIGYVPQDDI--LHPTLTVRETLMFAAKL-RGL--------------------------------SGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDL-GVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-246 |
5.45e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.52 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLlAANGVIGGSAKFNGREILNLPEHEln 99
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEVTSGSILLDGEDILELSPDE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klRA-EQISMIFQDPM------------TSLNpymRVGEQLMEVLMLHKGLGKAeafeesvkmLDAVKMPEArkrmrmFP 166
Cdd:COG0396 74 --RArAGIFLAFQYPVeipgvsvsnflrTALN---ARRGEELSAREFLKLLKEK---------MKELGLDED------FL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 167 H-----EFSGGMRQRVMIA-MALLcRPKLLIADEPTTALDVTVqAQIMT-LLNELKREfNTAIIMITH-----DLGVVag 234
Cdd:COG0396 134 DryvneGFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIDA-LRIVAeGVNKLRSP-DRGILIITHyqrilDYIKP-- 208
|
250
....*....|..
gi 556427173 235 icDKVLVMYAGR 246
Cdd:COG0396 209 --DFVHVLVDGR 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-246 |
5.52e-23 |
|
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: 99.13 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllAANGVIGGSAKFNGREI-LNLPEHELnklrAEQISMIFQD-PMTS 116
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGKFEGNVFINGKPVdIRNPAQAI----RAGIAMVPEDrKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 117 LNPYMRVGEQL-MEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFP-HEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:TIGR02633 350 IVPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556427173 195 PTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-247 |
5.64e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.23 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA---NGVIGGSAKFNGREIL--NL 93
Cdd:PRK13549 5 LLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKS----TLMKVLSGvypHGTYEGEIIFEGEELQasNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHElnklrAEQISMIFQDPMtsLNPYMRVGEQ--LMEVLMLHKGLGKAEAFEESVKMLDAVKM---PEARKRmrmfphE 168
Cdd:PRK13549 77 RDTE-----RAGIAIIHQELA--LVKELSVLENifLGNEITPGGIMDYDAMYLRAQKLLAQLKLdinPATPVG------N 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRH 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-251 |
8.21e-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: 94.13 E-value: 8.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTfktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgVIGGSAKFNGREILNLPEHEln 99
Cdd:cd03217 1 LEIKDLHVS----VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYE-VTEGEILFKGEDITDLPPEE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klRAEQ-ISMIFQDPMtslnpymrvgeqlmEVlmlhkglgkaeafeESVKMLDAVkmpearkrmRMFPHEFSGGMRQRVM 178
Cdd:cd03217 74 --RARLgIFLAFQYPP--------------EI--------------PGVKNADFL---------RYVNEGFSGGEKKRNE 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI-CDKVLVMYAGRTMEYG 251
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-260 |
9.04e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.50 E-value: 9.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 35 DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLA---ANGVIGGSAKFNGREILNLPEHELNKlraeQISMIFQ 111
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 112 DPmtSLNPYMRVGEQLMEVLMLHKGLGKAEA---FEESVKMLDAVKmpEARKRMRMFPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK14246 98 QP--NPFPHLSIYDNIAYPLKSHGIKEKREIkkiVEECLRKVGLWK--EVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 189 LLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQP 260
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-257 |
1.21e-22 |
|
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: 98.67 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPEHELnklrAEQ 105
Cdd:COG4618 335 NLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP---TAGSVRLDGADLSQWDREEL----GRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDPmtslnpymrvgeqlmevlmlhkglgkaEAFEESVK-------MLDAVKMPEARKRMRMfpHEF--------- 169
Cdd:COG4618 408 IGYLPQDV---------------------------ELFDGTIAeniarfgDADPEKVVAAAKLAGV--HEMilrlpdgyd 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 ----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAgICDKV 239
Cdd:COG4618 459 trigeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKL 536
|
250
....*....|....*...
gi 556427173 240 LVMYAGRTMEYGKARDVF 257
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-246 |
1.27e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 92.66 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREILNLPEHELNKlraeQ 105
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR---PTSGRVRLDGADISQWDPNELGD----H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDpmtslnpymrvgeqlmevlmlhkglgkAEAFEESVkmLDAVkmpearkrmrmfpheFSGGMRQRVMIAMALLC 185
Cdd:cd03246 78 VGYLPQD---------------------------DELFSGSI--AENI---------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLA-SADRILVLEDGR 172
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-259 |
1.35e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.62 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILN-LPEHELNKLRaEQISMIFQDPMTS 116
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT---GTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 117 LnpYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPeaRKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:PRK13646 98 L--FEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQ 259
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-261 |
2.26e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.94 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 15 QNNLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNlp 94
Cdd:PRK11432 2 TQKNFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTE---GQIFIDGEDVTH-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 95 ehelNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVL-MLhkGLGKAEAFE---ESVKMLDAVKMpEARkrmrmFPHEFS 170
Cdd:PRK11432 73 ----RSIQQRDICMVFQS--YALFPHMSLGENVGYGLkML--GVPKEERKQrvkEALELVDLAGF-EDR-----YVDQIS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
|
250
....*....|.
gi 556427173 251 GKARDVFYQPA 261
Cdd:PRK11432 219 GSPQELYRQPA 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-251 |
2.42e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.61 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 1 MTIIETATAPQAQQQNNLLLD------VKDLRVTfkTPDGDVTAVNdLNFNLRAGETLGIVGESGSGKSQTAFALMGLLA 74
Cdd:PRK11174 325 VTFLETPLAHPQQGEKELASNdpvtieAEDLEIL--SPDGKTLAGP-LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 75 ANGviggSAKFNGREILNLpehELNKLRaEQISMIFQDPmtslnpymrvgeQLME------VLmlhkgLGKAEAFEESVK 148
Cdd:PRK11174 402 YQG----SLKINGIELREL---DPESWR-KHLSWVGQNP------------QLPHgtlrdnVL-----LGNPDASDEQLQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 149 MLDAvkmpearkrmRMFPHEF-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT 209
Cdd:PRK11174 457 QALE----------NAWVSEFlpllpqgldtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 556427173 210 LLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:PRK11174 527 ALNAASRRQTT--LMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-251 |
2.69e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.72 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 10 PQAQQQNNLLLDVKDLRVTFKTpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALmgLLAANGVIGGSAKFNGRE 89
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINL--LQRVFDPQSGRILIDGTD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 90 ILNLpehELNKLRaEQISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGLGKAEA---FEESVKMLDAVkmpeARKRMR 163
Cdd:PRK13657 399 IRTV---TRASLR-RNIAVVFQDAGlfnRSIEDNIRVGRPDATDEEMRAAAERAQAhdfIERKPDGYDTV----VGERGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 164 MFphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAGiCDKVLVMY 243
Cdd:PRK13657 471 QL----SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFD 543
|
....*...
gi 556427173 244 AGRTMEYG 251
Cdd:PRK13657 544 NGRVVESG 551
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
39-246 |
2.94e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.31 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllAANGVIGGSAKFNGREI-LNLPEHELnklrAEQISMIFQD-PMTS 116
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGRWEGEIFIDGKPVkIRNPQQAI----AQGIAMVPEDrKRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 117 LNPYMRVGE--------QLMEVLMLHKGLgKAEAFEESVKMLdAVKMPEARKRMRmfphEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK13549 352 IVPVMGVGKnitlaaldRFTGGSRIDDAA-ELKTILESIQRL-KVKTASPELAIA----RLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-246 |
3.41e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 93.04 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKlraeQI 106
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTS---GSVLLDGTDIRQLDPADLRR----NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPMTSlnpYMRVGEQLMevlmlhkgLGKAEAfeESVKMLDAVKMPEARKRMRMFPHEF-----------SGGMRQ 175
Cdd:cd03245 81 GYVPQDVTLF---YGTLRDNIT--------LGAPLA--DDERILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-251 |
3.52e-22 |
|
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: 93.06 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDlrVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA-NGVIGGSAKFNGREIlnlPEHEL 98
Cdd:cd03251 1 VEFKN--VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRfYDVDSGRILIDGHDV---RDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLRaEQISMIFQDPM----TslnpymrVGEQLMevlmlhkgLGKAEAFEESVkmLDAVKMPEARKRMRMFPHEF----- 169
Cdd:cd03251 72 ASLR-RQIGLVSQDVFlfndT-------VAENIA--------YGRPGATREEV--EEAARAANAHEFIMELPEGYdtvig 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 ------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLGVVAGIcDKVLVMY 243
Cdd:cd03251 134 ergvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRLSTIENA-DRIVVLE 210
|
....*...
gi 556427173 244 AGRTMEYG 251
Cdd:cd03251 211 DGKIVERG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
39-257 |
4.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREI-LNLPEHELNKLRaEQISMIFQDPMTSL 117
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS---GTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 118 npymrVGEQLMEVLM---LHKGLGKAEAFEESVKMLDAVKMPEarKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK13641 99 -----FENTVLKDVEfgpKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 195 PTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-252 |
8.04e-22 |
|
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: 92.16 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFK-TPDGDVtAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgviggsakfNGREILN---LPEHELNKL 101
Cdd:cd03252 5 HVRFRyKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE---------NGRVLVDghdLALADPAWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 102 RAeQISMIFQDPmTSLNPYMRVGEQLMEVLMlhkglgKAEAFEESVKMLDA----VKMPEARKRMRmfpHE----FSGGM 173
Cdd:cd03252 75 RR-QVGVVLQEN-VLFNRSIRDNIALADPGM------SMERVIEAAKLAGAhdfiSELPEGYDTIV---GEqgagLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGK 252
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
27-251 |
1.54e-21 |
|
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: 90.06 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlpeHELNKLRAEQI 106
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQ---GEITLDGVPV-----SDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPM---TSLnpYMRVGEQlmevlmlhkglgkaeafeesvkmldavkmpearkrmrmfpheFSGGMRQRVMIAMAL 183
Cdd:cd03247 78 SVLNQRPYlfdTTL--RNNLGRR------------------------------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYG 251
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-256 |
1.60e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.98 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHEL 98
Cdd:PRK11300 5 LLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG---GTILLRGQHIEGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKL---RAEQISMIFQDpMTSLNPYMRVGEQLMEVLMLHkGLGK--------AEAFEESVKMLDAVKMPEARKRMrmfPH 167
Cdd:PRK11300 78 ARMgvvRTFQHVRLFRE-MTVIENLLVAQHQQLKTGLFS-GLLKtpafrraeSEALDRAATWLERVGLLEHANRQ---AG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
....*....
gi 556427173 248 MEYGKARDV 256
Cdd:PRK11300 233 LANGTPEEI 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
37-257 |
1.91e-21 |
|
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: 91.07 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 37 TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHElnklRAE-------QISMI 109
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS---GKILLDGQDITKLPMHK----RARlgigylpQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 110 FQDpmtslnpyMRVGEQLMEVLMLHKgLGKAEAFEESVKMLDAVKMPEARKRMRMFpheFSGGMRQRVMIAMALLCRPKL 189
Cdd:cd03218 87 FRK--------LTVEENILAVLEIRG-LSKKEREEKLEELLEEFHITHLRKSKASS---LSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 190 LIADEPTTALDVTVQAQIMTLLNELKrefNTAI-IMIT-HDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILK---DRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-294 |
4.20e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.89 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANG--VIGGSAKfngreilnlpehe 97
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAgeLLAGTAP------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 LNKLRaEQISMIFQDpmTSLNPYMRVGEQLmevlmlhkGLG-KAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQR 176
Cdd:PRK11247 76 LAEAR-EDTRLMFQD--ARLLPWKKVIDNV--------GLGlKGQWRDAALQALAAVGLAD---RANEWPAALSGGQKQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTmeygkARDV 256
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-----GLDL 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 556427173 257 FYQPAHPYSIGllnaVPRLDA-EGESL---LTIPGNPPNLLR 294
Cdd:PRK11247 217 TVDLPRPRRRG----SARLAElEAEVLqrvMSRGESEPTRLR 254
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-252 |
4.81e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 89.54 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 43 NFNLRAGETLGIVGESGSGKSqtafALMGLLAanGVI---GGSAKFNGREILNLPEHElnklraEQISMIFQDpmTSLNP 119
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS----TLLNLIA--GFIepaSGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 120 YMRVGEQLmeVLMLHKGLgKAEAfEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:TIGR01277 84 HLTVRQNI--GLGLHPGL-KLNA-EQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556427173 200 DVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
34-246 |
7.72e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.16 E-value: 7.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKLRaEQISMIFQDP 113
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSA---GKIWFSGHDITRLKNREVPFLR-RQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 MTSLNpymRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEarkRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:PRK10908 89 HLLMD---RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
41-246 |
7.92e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 7.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILN-------------LPEHElnklraeQIS 107
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG---GRIMLNGKEINAlstaqrlarglvyLPEDR-------QSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 108 MIFQDPMTSLNPYMRVGEQLMevLMLHKGLGKAeAFEESVKMLDaVKMPEARKRMRmfphEFSGGMRQRVMIAMALLCRP 187
Cdd:PRK15439 351 GLYLDAPLAWNVCALTHNRRG--FWIKPARENA-VLERYRRALN-IKFNHAEQAAR----TLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 188 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-227 |
9.42e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 9.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTfkTPDGDVTaVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGL-LAANGVIGGSAkfnGREILNLPEHe 97
Cdd:COG4178 363 LALEDLTLR--TPDGRPL-LEDLSLSLKPGERLLITGPSGSGKS-TLLrAIAGLwPYGSGRIARPA---GARVLFLPQR- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 lnklraeqismifqdpmtslnPYMRVGEqLMEVLmlhkgL--GKAEAF--EESVKMLDAVKMPEARKRM---RMFPHEFS 170
Cdd:COG4178 435 ---------------------PYLPLGT-LREAL-----LypATAEAFsdAELREALEAVGLGHLAERLdeeADWDQVLS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkREFNTAIIMITH 227
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-240 |
1.20e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.40 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGVIGGSAKFngrEILNLPEHe 97
Cdd:PRK09544 4 LVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNGKL---RIGYVPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 lnklraeqismIFQDPMTSLNpymrvgeqLMEVLMLHKGLGKAEafeesvkMLDAVKMPEARKRMRMFPHEFSGGMRQRV 177
Cdd:PRK09544 76 -----------LYLDTTLPLT--------VNRFLRLRPGTKKED-------ILPALKRVQAGHLIDAPMQKLSGGETQRV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 240
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-267 |
1.24e-20 |
|
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: 92.58 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA---NGVIGGSAKFNGREilnLPE 95
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKS----TLMKILSGvypHGTWDGEIYWSGSP---LKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 96 HELNKLRAEQISMIFQDPMtsLNPYMRVGEQL-MEVLMLHKG--LGKAEAFEESVKMLDAVK---MPEARKRMrmfphEF 169
Cdd:TIGR02633 70 SNIRDTERAGIVIIHQELT--LVPELSVAENIfLGNEITLPGgrMAYNAMYLRAKNLLRELQldaDNVTRPVG-----DY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR--- 246
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQhva 221
|
250 260 270
....*....|....*....|....*....|....
gi 556427173 247 -------------TMEYGKARDVFYqPAHPYSIG 267
Cdd:TIGR02633 222 tkdmstmseddiiTMMVGREITSLY-PHEPHEIG 254
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
42-283 |
1.37e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.13 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 42 LNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANGVIggsaKFNGREILNLPEHELNKLRAeqisMIFQDPMTSLNpy 120
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLPGQGEI----LLNGRPLSDWSAAELARHRA----YLSQQQSPPFA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 121 MRVGEQLMevLMLHKGLGKAEAFEESVKMLDAVKMpeARKRMRMFpHEFSGGMRQRVMIAMALL-------CRPKLLIAD 193
Cdd:COG4138 84 MPVFQYLA--LHQPAGASSEAVEQLLAQLAEALGL--EDKLSRPL-TQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFyQP---AHPYSIglln 270
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGIT-VVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPenlSEVFGV---- 232
|
250
....*....|...
gi 556427173 271 AVPRLDAEGESLL 283
Cdd:COG4138 233 KFRRLEVEGHRWL 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
30-256 |
1.75e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.60 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 30 KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGVI---GGSAKFNGReilnlpehelnklraeqI 106
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKS-T---LLKLIA--GILeptSGRVEVNGR-----------------V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFqDPMTSLNPYMRVGEQLMEVLMLHkGLGKAE---------AFEEsvkmL-DAVKMPearkrMRMFphefSGGMRQR 176
Cdd:COG1134 90 SALL-ELGAGFHPELTGRENIYLNGRLL-GLSRKEidekfdeivEFAE----LgDFIDQP-----VKTY----SSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:COG1134 155 LAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
33-251 |
2.45e-20 |
|
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: 88.05 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 33 DGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgviGGSAKFNGREILNLPEHELNklraEQISMIFQD 112
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDIRDISRKSLR----SMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 113 PM---TSLNPYMRVGEQLM---EVLMLHKGLGKAEAFEESVKMLDAVKMPEArkrmrmfpHEFSGGMRQRVMIAMALLCR 186
Cdd:cd03254 86 TFlfsGTIMENIRLGRPNAtdeEVIEAAKEAGAHDFIMKLPNGYDTVLGENG--------GNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 187 PKLLIADEPTTALDV----TVQAQIMTLLNelkrefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:cd03254 158 PKILILDEATSNIDTetekLIQEALEKLMK------GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-253 |
2.47e-20 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 88.55 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 16 NNLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgVIGGSAKFNGREILNLPE 95
Cdd:CHL00131 4 NKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYK-ILEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 96 HElnklRAEQ-ISMIFQDPMTSlnpymrVGEQLMEVLML-----HKGLGKAEA-----FEESVKMLDAVKMpEARKRMRM 164
Cdd:CHL00131 79 EE----RAHLgIFLAFQYPIEI------PGVSNADFLRLaynskRKFQGLPELdplefLEIINEKLKLVGM-DPSFLSRN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 165 FPHEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGIC-DKVLVM 242
Cdd:CHL00131 148 VNEGFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKpDYVHVM 225
|
250
....*....|.
gi 556427173 243 YAGRTMEYGKA 253
Cdd:CHL00131 226 QNGKIIKTGDA 236
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-262 |
2.59e-20 |
|
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: 87.91 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 39 VNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAAngviggsakfngreiLNLPEHELNKLRAEQIS-------MIFQ 111
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLISG---------------LAQPTSGGVILEGKQITepgpdrmVVFQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 112 DpmTSLNPYMRVGEQL-MEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:TIGR01184 62 N--YSLLPWLTVRENIaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 191 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV-FYQPAH 262
Cdd:TIGR01184 137 LLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
38-229 |
2.60e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAanGVI---GGSAKFNGREIlnlpehelNKLRAEQiSMIFQDpm 114
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKT----TLLNLIA--GFVpyqHGSITLDGKPV--------EGPGAER-GVVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 115 TSLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 556427173 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 229
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-260 |
2.68e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKtpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHEL 98
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS---GSVLIRGEPITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NKLraeqISMIFQDPMTSLnpYMRVGEQLMEVLMLHKGLGK---AEAFEESVKMLDavkMPEARKRMrmfPHEFSGGMRQ 175
Cdd:PRK13652 77 RKF----VGLVFQNPDDQI--FSPTVEQDIAFGPINLGLDEetvAHRVSSALHMLG---LEELRDRV---PHHLSGGEKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:PRK13652 145 RVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
....*
gi 556427173 256 VFYQP 260
Cdd:PRK13652 225 IFLQP 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-246 |
2.83e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.22 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 39 VNDLNFNLRAGETLGIVGESGSGKSQtafaLMGLL-AANGVIGGSAKFNGREILNL-PEHELnklrAEQISMIFQD---- 112
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTE----LMKVLyGALPRTSGYVTLDGHEVVTRsPQDGL----ANGIVYISEDrkrd 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 113 ------------PMTSLNPYMRVGEQLmevlmlhKGLGKAEAFEESVKMLDaVKMPEARKRMRMFphefSGGMRQRVMIA 180
Cdd:PRK10762 340 glvlgmsvkenmSLTALRYFSRAGGSL-------KHADEQQAVSDFIRLFN-IKTPSMEQAIGLL----SGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-257 |
7.56e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 29 FKTPDGDVTAVNDLNFNLRAgeTLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGrEILNLPEHELNKLRaEQISM 108
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQK---GAVLWQG-KPLDYSKRGLLALR-QQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 109 IFQDPMTSLNpYMRVGEQLMEVLmlhKGLGKAEAfEESVKMLDAVKMPEArKRMRMFPHE-FSGGMRQRVMIAMALLCRP 187
Cdd:PRK13638 82 VFQDPEQQIF-YTDIDSDIAFSL---RNLGVPEA-EITRRVDEALTLVDA-QHFRHQPIQcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 188 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-229 |
1.32e-19 |
|
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: 89.34 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPEHELN 99
Cdd:TIGR02868 335 LELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP---LQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLraeqISMIFQDPM---TSLNPYMRVG------EQLMEVLmlhKGLGKAEAFEESVKMLDAVKMPEARKrmrmfpheFS 170
Cdd:TIGR02868 409 RR----VSVCAQDAHlfdTTVRENLRLArpdatdEELWAAL---ERVGLADWLRALPDGLDTVLGEGGAR--------LS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDL 229
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-251 |
1.32e-19 |
|
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: 86.05 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 23 KDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAanGVI---GGSAKFNGReilnlpeheln 99
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLLA--GIYppdSGTVTVRGR----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klraeqISMIFqDPMTSLNPYMRVGEQLMEVLMLHkGLGKAE--AFEESVKML----DAVKMPearkrMRmfphEFSGGM 173
Cdd:cd03220 85 ------VSSLL-GLGGGFNPELTGRENIYLNGRLL-GLSRKEidEKIDEIIEFselgDFIDLP-----VK----TYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-255 |
1.56e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 89.39 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlPEHELNKLRAeQI 106
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS---GQILLDGHDL---ADYTLASLRR-QV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 107 SMIFQDPM----TSLN--PYMRVGEQLMEvlMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMfphefSGGMRQRVMIA 180
Cdd:TIGR02203 409 ALVSQDVVlfndTIANniAYGRTEQADRA--EIERALAAAYAQDFVDKLPLGLDTPIGENGVLL-----SGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGRTMEYGKARD 255
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-262 |
1.70e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 37 TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGL--------LAANGVIGGSAKFNGREILNLpehelnklrAEQISM 108
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgyrYSGDVLLGGRSIFNYRDVLEF---------RRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 109 IFQDPmtslNPY-MRVGEQLMEVLMLHKGL------GKAEAFEESVKMLDAVKmpearKRMRMFPHEFSGGMRQRVMIAM 181
Cdd:PRK14271 106 LFQRP----NPFpMSIMDNVLAGVRAHKLVprkefrGVAQARLTEVGLWDAVK-----DRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPA 261
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
.
gi 556427173 262 H 262
Cdd:PRK14271 255 H 255
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-256 |
1.83e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.94 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPEHELNKlraeQ 105
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP---TSGSVRLDGADLKQWDRETFGK----H 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQD----PMTSLNPYMRVGEQLmevlmlhkglgkaeafeESVKMLDAVKMPEARKRMRMFPHEF-----------S 170
Cdd:TIGR01842 394 IGYLPQDvelfPGTVAENIARFGENA-----------------DPEKIIEAAKLAGVHELILRLPDGYdtvigpggatlS 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGIcDKVLVMYAGRTMEY 250
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGCV-DKILVLQDGRIARF 534
|
....*.
gi 556427173 251 GKARDV 256
Cdd:TIGR01842 535 GERDEV 540
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-227 |
1.99e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.40 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 29 FKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKFNGREilnlpehelnkLRAEQ--- 105
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQP-----------RKPDQfqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 -ISMIFQDpmTSLNPYMRVGEQL--MEVLMLHKGLGKA--EAFEESVKMLDAVKMPEARKRMRmfphEFSGGMRQRVMIA 180
Cdd:cd03234 82 cVAYVRQD--DILLPGLTVRETLtyTAILRLPRKSSDAirKKRVEDVLLRDLALTRIGGNLVK----GISGGERRRVSIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556427173 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 227
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-227 |
3.01e-19 |
|
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: 83.36 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKTPDGDVTaVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGVIGgsaKFNGREILNLPEHelnklrae 104
Cdd:cd03223 5 NLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWpWGSGRIG---MPEGEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 105 qismifqdpmtslnPYMRVGeQLMEVLMlhkglgkaeafeesvkmldavkmpearkrmrmFP--HEFSGGMRQRVMIAMA 182
Cdd:cd03223 73 --------------PYLPLG-TLREQLI--------------------------------YPwdDVLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556427173 183 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrefnTAIIMITH 227
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-256 |
4.24e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.98 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIggsaKFNGREILNLPEHELNKLRA---EQISMIFqdpmtsln 118
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSI----QFAGQPLEAWSAAELARHRAylsQQQTPPF-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 119 pymrvgeqLMEV---LMLHKGLGKAEAFEESV--KMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAMALL-----CRP- 187
Cdd:PRK03695 83 --------AMPVfqyLTLHQPDKTRTEAVASAlnEVAEALGLDDKLGRS---VNQLSGGEWQRVRLAAVVLqvwpdINPa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 188 -KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK03695 152 gQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
34-278 |
5.25e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELnklrAEQISMIFQDP 113
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS---GTVFLGDKPISMLSSRQL----ARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 MT------------SLNPYM----RVG---EQLMEVLMlhkglGKAEAFEESVKMLDavkmpearkrmrmfphEFSGGMR 174
Cdd:PRK11231 86 LTpegitvrelvayGRSPWLslwgRLSaedNARVNQAM-----EQTRINHLADRRLT----------------DLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAR 254
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
250 260
....*....|....*....|....
gi 556427173 255 DVFYQpahpysiGLLNAVPRLDAE 278
Cdd:PRK11231 224 EVMTP-------GLLRTVFDVEAE 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-256 |
9.68e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHEln 99
Cdd:COG1137 4 LEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS---GRIFLDGEDITHLPMHK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klRA-------EQISMIFQDpMTslnpymrVGEQLMEVLMLHKgLGKAEAFEESVKMLDAVKMPEARKRMRMfphEFSGG 172
Cdd:COG1137 75 --RArlgigylPQEASIFRK-LT-------VEDNILAVLELRK-LSKKEREERLEELLEEFGITHLRKSKAY---SLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALD-VTVqAQIMTLLNELKrEFNTAIImIT-HD----LgvvaGICDKVLVMYAGR 246
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVL-ITdHNvretL----GICDRAYIISEGK 213
|
250
....*....|
gi 556427173 247 TMEYGKARDV 256
Cdd:COG1137 214 VLAEGTPEEI 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-257 |
1.34e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.60 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLaaNGVI----GGSAKFNGREilnLP 94
Cdd:COG1119 3 LLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLI--TGDLpptyGNDVRLFGER---RG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 95 EHELNKLRAeQI---SMIFQDpmtslnpYMRVGEQLMEVLM--LHKGLG-----KAEAFEESVKMLDAVKMpeARKRMRM 164
Cdd:COG1119 70 GEDVWELRK-RIglvSPALQL-------RFPRDETVLDVVLsgFFDSIGlyrepTDEQRERARELLELLGL--AHLADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 165 FpHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG-VVAGIcDKVLVMY 243
Cdd:COG1119 140 F-GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVLLLK 217
|
250
....*....|....
gi 556427173 244 AGRTMEYGKARDVF 257
Cdd:COG1119 218 DGRVVAAGPKEEVL 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-246 |
1.55e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.09 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 43 NFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANGviggsakfnGREILNLPEHELNKLRAEQISMIFQDpmTSLNPYM 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIaGFLTPAS---------GSLTLNGQDHTTTPPSRRPVSMLFQE--NNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 122 RVGEQLmeVLMLHKGLGKAEAFEESVK-MLDAVKMPEARKRmrmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:PRK10771 87 TVAQNI--GLGLNPGLKLNAAQREKLHaIARQMGIEDLLAR---LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556427173 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
13-264 |
1.59e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 13 QQQNNLLLDVK-DLrvtfktPDGDVTAvndlnfnlragetlgIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGReIL 91
Cdd:PRK11144 8 QQLGDLCLTVNlTL------PAQGITA---------------IFGRSGAGKTSLINAISGLTRPQK---GRIVLNGR-VL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 92 NLPEHELNkLRAEQ--ISMIFQDpmTSLNPYMRV-GEqlmevlmLHKGLGK--AEAFEESVKMLDAVKMpearkrMRMFP 166
Cdd:PRK11144 63 FDAEKGIC-LPPEKrrIGYVFQD--ARLFPHYKVrGN-------LRYGMAKsmVAQFDKIVALLGIEPL------LDRYP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
250
....*....|....*....
gi 556427173 247 TMEYGKARDVFYQPA-HPY 264
Cdd:PRK11144 207 VKAFGPLEEVWASSAmRPW 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-251 |
1.75e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.23 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDlrVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGreiLNLPEHELN 99
Cdd:PRK11176 342 IEFRN--VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDE---GEILLDG---HDLRDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRaEQISMI------FQDPMTSLNPYMRvgeqlmevlmlhKGLGKAEAFEESVKMLDAV----KMPEARKRMrmfPHE- 168
Cdd:PRK11176 414 SLR-NQVALVsqnvhlFNDTIANNIAYAR------------TEQYSREQIEEAARMAYAMdfinKMDNGLDTV---IGEn 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 169 ---FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAG 245
Cdd:PRK11176 478 gvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDG 554
|
....*.
gi 556427173 246 RTMEYG 251
Cdd:PRK11176 555 EIVERG 560
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-256 |
4.23e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 4 IETATAPQAQQQNNLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GVIggs 82
Cdd:PRK13536 26 ISEAKASIPGSMSTVAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDaGKI--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 83 akfngrEILNLPEHELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMeVLMLHKGLgKAEAFEESVKMLDAVKMPEARKRM 162
Cdd:PRK13536 99 ------TVLGVPVPARARLARARIGVVPQ--FDNLDLEFTVRENLL-VFGRYFGM-STREIEAVIPSLLEFARLESKADA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 163 RMfpHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVM 242
Cdd:PRK13536 169 RV--SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVL 245
|
250
....*....|....
gi 556427173 243 YAGRTMEYGKARDV 256
Cdd:PRK13536 246 EAGRKIAEGRPHAL 259
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-252 |
4.59e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.16 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPD-GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKlraeQ 105
Cdd:TIGR00958 484 VSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG---GQVLLDGVPLVQYDHHYLHR----Q 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDPmtslnpymrvgeqlmeVLM---LHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEF-----------SG 171
Cdd:TIGR00958 557 VALVGQEP----------------VLFsgsVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYdtevgekgsqlSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAqimtLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
.
gi 556427173 252 K 252
Cdd:TIGR00958 696 T 696
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-255 |
7.39e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 35 DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllaANGVIGGSAKFNGREILnlPEHELNKLRaEQISMIFQD-- 112
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDKRAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITESrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 113 -----PMTSLNPYMRVGEQLMEvlmlhKGLGKAEA-FEESVKMLDAvkmPEARKRMRMFPH-------EFSGGMRQRVMI 179
Cdd:PRK09700 349 dngffPNFSIAQNMAISRSLKD-----GGYKGAMGlFHEVDEQRTA---ENQRELLALKCHsvnqnitELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD 255
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
38-257 |
7.71e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.10 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKLRAEQISMIFQDPMTsl 117
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ---GSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPES-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 118 npymrvgeQLMEVLMLhkglgKAEAFEES---VKMLDAVKMpeARKRMRMF----------PHEFSGGMRQRVMIAMALL 184
Cdd:PRK13649 97 --------QLFEETVL-----KDVAFGPQnfgVSQEEAEAL--AREKLALVgiseslfeknPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-257 |
7.98e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFKTPDgdvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGVIGgsakfngreILNLPEHElnK 100
Cdd:PRK15056 9 VNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVrLASGKIS---------ILGQPTRQ--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 101 LRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGL---GKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRV 177
Cdd:PRK15056 75 LQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWlrrAKKRDRQIVTAALARVDMVEFRHRQ---IGELSGGQKKRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICDKVlVMYAGRTMEYGKARDVF 257
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYT-VMVKGTVLASGPTETTF 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-256 |
1.08e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlPEHEln 99
Cdd:PRK13537 8 IDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA---GSISLCGEPV---PSRA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAEQISMIFQdpMTSLNPYMRVGEQLMeVLMLHKGLGKAEAFEESVKMLDAVKMpEARKRMRMfpHEFSGGMRQRVMI 179
Cdd:PRK13537 76 RHARQRVGVVPQ--FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKL-ENKADAKV--GELSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
44-242 |
1.12e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 80.67 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 44 FNLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGVI---GGSAKFNGREILNLPE-HELN---KLRAEQISMIFQDPMT 115
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVkvaGASPGKGWRHIGYVPQrHEFAwdfPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 116 SLNPYMRVGEqlmevlmlHKGLGKAeafeesvkmLDAVKMPEARKRmrmfP-HEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:TIGR03771 81 GWLRRPCVAD--------FAAVRDA---------LRRVGLTELADR----PvGELSGGQRQRVLVARALATRPSVLLLDE 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556427173 195 PTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:TIGR03771 140 PFTGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL 186
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-246 |
1.32e-17 |
|
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: 80.23 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 41 DLNFNLRAGETLGIVGESGSGKSqtafALMGLLAangviGGSAKFNGREILNLPEHELNKLRAEQISMIFQDpmTSLNPY 120
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKS----TLLNLIA-----GFETPQSGRVLINGVDVTAAPPADRPVSMLFQE--NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 121 MRVGEQLmeVLMLHKGLGKAEAFEESVKMLdAVKMPEARKRMRMfPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:cd03298 85 LTVEQNV--GLGLSPGLKLTAEDRQAIEVA-LARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556427173 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
34-233 |
1.74e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngVIGGSAKFNGREILNLPEHelnklraeqISMIFQDP 113
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP--TSGTVRRAGGARVAYVPQR---------SEVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 MTSlnpymrvgEQLMEV-LMLHKGLGK---AEAFEESVKMLDAVKMPEARKRMRmfpHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:NF040873 72 LTV--------RDLVAMgRWARRGLWRrltRDDRAAVDDALERVGLADLAGRQL---GELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556427173 190 LIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVA 233
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
49-280 |
4.89e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.85 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 49 GETLGIVGESGSGKSQTAFALMGLLAANGVIGgSAKFNGREIlnlpehelNKLRAEQISMIFQDPMtsLNPYMRVGEQLM 128
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTG-TILANNRKP--------TKQILKRTGFVTQDDI--LYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 129 --EVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRM--RMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ 204
Cdd:PLN03211 163 fcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 205 AQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARD-------VFYQPAHP-----YSIGLLNAV 272
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDamayfesVGFSPSFPmnpadFLLDLANGV 322
|
....*...
gi 556427173 273 PRLDAEGE 280
Cdd:PLN03211 323 CQTDGVSE 330
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-252 |
5.02e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.79 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 11 QAQQQNNLLLDVKDlrVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAAN-GVIGGSAKFNGRE 89
Cdd:PRK11160 330 STAAADQVSLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAwDPQQGEILLNGQP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 90 ILNLPEHELnklRAeQISMIFQDP---MTSLNPYMRVG------EQLMEVLMlHKGLGKaeaFEESVKMLDAVKMPEARk 160
Cdd:PRK11160 404 IADYSEAAL---RQ-AISVVSQRVhlfSATLRDNLLLAapnasdEALIEVLQ-QVGLEK---LLEDDKGLNAWLGEGGR- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 161 rmrmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGIcDKVL 240
Cdd:PRK11160 475 -------QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRIC 544
|
250
....*....|..
gi 556427173 241 VMYAGRTMEYGK 252
Cdd:PRK11160 545 VMDNGQIIEQGT 556
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-282 |
6.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKTPDGdVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgviGGSAKFNGREILNLPE-HELNKLrae 104
Cdd:PRK13644 6 NVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ---KGKVLVSGIDTGDFSKlQGIRKL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 105 qISMIFQDPMTSLnpymrVGEQLMEVLML---HKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAM 181
Cdd:PRK13644 79 -VGIVFQNPETQF-----VGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRHRS---PKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAgICDKVLVMYAGRTMEYGKARDVFYQPA 261
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDVS 227
|
250 260
....*....|....*....|.
gi 556427173 262 HPYsIGLlnAVPRLDAEGESL 282
Cdd:PRK13644 228 LQT-LGL--TPPSLIELAENL 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-256 |
8.60e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 8.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTF--KTPDgDVTAVNDLNFNLRAGETLGIVGESGSGKsqTAF-----ALmgLLAANGVI-------------GG 81
Cdd:PRK13651 5 VKNIVKIFnkKLPT-ELKALDNVSVEINQGEFIAIIGQTGSGK--TTFiehlnAL--LLPDTGTIewifkdeknkkktKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 82 SAKFNGREILNLPEHE----LNKLRaEQISMIFQdpmtsLNPYMRVGEQLMEVLM---LHKGLGKAEAFEESVKMLDAVK 154
Cdd:PRK13651 80 KEKVLEKLVIQKTRFKkikkIKEIR-RRVGVVFQ-----FAEYQLFEQTIEKDIIfgpVSMGVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 155 MPEARkrMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAG 234
Cdd:PRK13651 154 LDESY--LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLE 230
|
250 260
....*....|....*....|..
gi 556427173 235 ICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDI 252
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-251 |
1.24e-16 |
|
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: 80.63 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 5 ETATAPQAQQqnnllLDVKDLRVTFK----TPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvig 80
Cdd:COG5265 341 EVADAPDAPP-----LVVGGGEVRFEnvsfGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTS--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 81 GSAKFNGREILNLPEHELnklRAeQISMIFQDpmTSL-------N-PYmrvgeqlmevlmlhkglGKAEAFEESVkmLDA 152
Cdd:COG5265 413 GRILIDGQDIRDVTQASL---RA-AIGIVPQD--TVLfndtiayNiAY-----------------GRPDASEEEV--EAA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 153 VKMPEArkrmrmfpHEF-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNE 213
Cdd:COG5265 468 ARAAQI--------HDFieslpdgydtrvgerglklSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE 539
|
250 260 270
....*....|....*....|....*....|....*...
gi 556427173 214 LKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:COG5265 540 VAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
53-260 |
1.49e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.15 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 53 GIVGESGSGKSQTAFAL--MGLLAANGVIGGSAKFNGREILNlPEHELNKLRaEQISMIFQDPmtSLNPyMRVGEQL--- 127
Cdd:PRK14258 37 AIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNQNIYE-RRVNLNRLR-RQVSMVHPKP--NLFP-MSVYDNVayg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 128 MEVLMLHKGLGKAEAFEESVKmlDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 207
Cdd:PRK14258 112 VKIVGWRPKLEIDDIVESALK--DADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 208 MTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA-----GRTMEYGKARDVFYQP 260
Cdd:PRK14258 190 ESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
46-263 |
1.93e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 46 LRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKFNGREIlnlpehELNKLRAeqIS-MIFQDPMtsLNPYMRVG 124
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPI------DAKEMRA--ISaYVQQDDL--FIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 125 EQLMEVLML--HKGLGKAEAFEESVKMLDAVKMPEARK-------RMRmfphEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:TIGR00955 118 EHLMFQAHLrmPRRVTKKEKRERVDEVLQALGLRKCANtrigvpgRVK----GLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 196 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK---ARDVFYQPAHP 263
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSpdqAVPFFSDLGHP 264
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
38-259 |
2.92e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.85 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKLRAEQISMIFQDPMTsl 117
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTE---GKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPES-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 118 npymrvgeQLMEVLMLHK--------GLGKAEAFEESVKMLDAVKMpeARKRMRMFPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK13643 96 --------QLFEETVLKDvafgpqnfGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQ 259
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
37-257 |
5.44e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 37 TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHElnklRAEQ-ISMIFQDPmt 115
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---GNIIIDDEDISLLPLHA----RARRgIGYLPQEA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 116 SLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM---GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 196 TTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVF 257
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
34-269 |
5.54e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.76 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLlaaNGVIGGSAKFNGREILNLPEHELNklraeqISMIFQDp 113
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL---EDITSGDLFIGEKRMNDVPPAERG------VGMVFQS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVGEQLMEVLMLhKGLGKAEA---FEESVKMLDAVKMPEARkrmrmfPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK11000 84 -YALYPHLSVAENMSFGLKL-AGAKKEEInqrVNQVAEVLQLAHLLDRK------PKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 191 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPAHPYSIGLL 269
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-249 |
6.21e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.29 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLA---ANGVIGGSAKFNGREIlnlpe 95
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKS----TLMKVLSgvyPHGSYEGEILFDGEVC----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 96 hELNKLRA-EQ--ISMIFQDpmTSLNPYMRVGEQLMevlmlhkgLGK----------AEAFEESVKMLDAVKMPEArkrm 162
Cdd:NF040905 68 -RFKDIRDsEAlgIVIIHQE--LALIPYLSIAENIF--------LGNerakrgvidwNETNRRARELLAKVGLDES---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 163 rmfPHEFSG----GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDK 238
Cdd:NF040905 133 ---PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADS 208
|
250
....*....|.
gi 556427173 239 VLVMYAGRTME 249
Cdd:NF040905 209 ITVLRDGRTIE 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-246 |
6.56e-16 |
|
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: 75.59 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFKTPD-GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlNLPEHelnK 100
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG---GQVLLDGKPI-SQYEH---K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 101 LRAEQISMIFQDPMT---SLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMfphefSGGMRQRV 177
Cdd:cd03248 85 YLHSKVSLVGQEPVLfarSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL-----SGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGR 246
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-246 |
6.59e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 78.23 E-value: 6.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPEHE-LNK---LRAEQ-------- 105
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREK---SAGTITLHGKKINNHNANEaINHgfaLVTEErrstgiya 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 -ISMIFQDPMTSLNPYMRvgeqlmevlmlHKGLGKAEAFEESVK-MLDA--VKMPEARKRMrmfpHEFSGGMRQRVMIAM 181
Cdd:PRK10982 340 yLDIGFNSLISNIRNYKN-----------KVGLLDNSRMKSDTQwVIDSmrVKTPGHRTQI----GSLSGGNQQKVIIGR 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-256 |
1.03e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAN----------------------- 76
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsgriiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 77 ------GVIGGSAKFNGREILNLPEHELNKLRaEQISMIFQDPMtSLNPYMRVGEQLMEVLMlHKGLGKAEAFEESVKML 150
Cdd:TIGR03269 77 kvgepcPVCGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 151 DAVKMPEarkRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG 230
Cdd:TIGR03269 154 EMVQLSH---RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 556427173 231 VVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
34-256 |
1.34e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.12 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMG-LLAANGvigGSAKFNGREILNLPEHELnklrAEQISMIFQD 112
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLPPDS---GEVLVDGLDVATTPSREL----AKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 113 PmtSLNPYMRVGEqlmevlmL--------HKGLGKAEafeesvkmlDAVKMPEARKRMRM------FPHEFSGGMRQRVM 178
Cdd:COG4604 84 N--HINSRLTVRE-------LvafgrfpySKGRLTAE---------DREIIDEAIAYLDLedladrYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-256 |
1.48e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 12 AQQQNNLLlDVKDLRVTfktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGllaanGVI---GGSAKFNGR 88
Cdd:PRK11831 1 EQSVANLV-DMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKT-TLLRLIG-----GQIapdHGEILFDGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 89 EILNLPEHELNKLRaEQISMIFQDP--MTSLNPYMRVGEQLMEvlmlHKGLgKAEAFEESVKM-LDAVKMPEARKRMrmf 165
Cdd:PRK11831 70 NIPAMSRSRLYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQL-PAPLLHSTVMMkLEAVGLRGAAKLM--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 166 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:PRK11831 141 PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADK 220
|
250
....*....|.
gi 556427173 246 RTMEYGKARDV 256
Cdd:PRK11831 221 KIVAHGSAQAL 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-261 |
2.66e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRvtfKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA-NGVIGGSAKFNGREILNLPEHEL 98
Cdd:PRK11650 4 LKLQAVR---KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMVAGlERITSGEIWIGGRVVNELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 NklraeqISMIFQDpmTSLNPYMRVgEQLMEVLMLHKGLGKAEA---FEESVKMLDAVKMPEaRKrmrmfPHEFSGGMRQ 175
Cdd:PRK11650 77 D------IAMVFQN--YALYPHMSV-RENMAYGLKIRGMPKAEIeerVAEAARILELEPLLD-RK-----PRELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQiMTL-LNELKREFNTAIIMITHD------LGvvagicDKVLVMYAGRTM 248
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGGVAE 214
|
250
....*....|...
gi 556427173 249 EYGKARDVFYQPA 261
Cdd:PRK11650 215 QIGTPVEVYEKPA 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-250 |
4.69e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 10 PQAQQQNNLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGvigGSAKFnGR 88
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS-TLLkLLAGELEPDS---GTVKL-GE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 89 EIlnlpehelnklraeQISMIFQDpMTSLNPYMRVGEQLMEvlmlhkglGKAEAFEESV-----KML---DavkmpEARK 160
Cdd:COG0488 377 TV--------------KIGYFDQH-QEELDPDKTVLDELRD--------GAPGGTEQEVrgylgRFLfsgD-----DAFK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 161 RMRmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHDLGVVAGICDKV 239
Cdd:COG0488 429 PVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-----LEEALDDFPGTVLLVSHDRYFLDRVATRI 499
|
250
....*....|.
gi 556427173 240 LVMYAGRTMEY 250
Cdd:COG0488 500 LEFEDGGVREY 510
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-228 |
6.01e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGVI---GGSAKFNGR--------EI 90
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS-T---LLKILA--GELepdSGEVSIPKGlrigylpqEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 91 LNLPEH-----------ELNKLRAE--QISMIFQDPMTSLNPYMRVGEQLME---------VLMLHKGLG-KAEAFEESV 147
Cdd:COG0488 71 PLDDDLtvldtvldgdaELRALEAEleELEAKLAEPDEDLERLAELQEEFEAlggweaearAEEILSGLGfPEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 148 KmldavkmpearkrmrmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtVQAqIMTLLNELKReFNTAIIMITH 227
Cdd:COG0488 151 S-------------------ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLKN-YPGTVLVVSH 207
|
.
gi 556427173 228 D 228
Cdd:COG0488 208 D 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
39-246 |
6.90e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllAANGV-IGGSAKFNGREI------------------------LNL 93
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGRnISGTVFKDGKEVdvstvsdaidaglayvtedrkgygLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHelnkLRaEQISMifqdpmTSLNPYMRVGeqlmeVLMLHKGLGKAEAFeesvkmldavkmpeaRKRMRMFPH------ 167
Cdd:NF040905 354 IDD----IK-RNITL------ANLGKVSRRG-----VIDENEEIKVAEEY---------------RKKMNIKTPsvfqkv 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 168 -EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:NF040905 403 gNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGR 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-277 |
9.99e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 6 TATAPQAQQQNNLLLDVKDLRVTfktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKF 85
Cdd:PTZ00243 1297 TSAAPHPVQAGSLVFEGVQMRYR----EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE---VCGGEIRV 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 86 NGREIlnlPEHELNKLRaEQISMIFQDPM-------TSLNPYMRVGEQlmEVLMLHKGLGKAEAFEESVKMLDAvkmpea 158
Cdd:PTZ00243 1370 NGREI---GAYGLRELR-RQFSMIPQDPVlfdgtvrQNVDPFLEASSA--EVWAALELVGLRERVASESEGIDS------ 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 159 rkRMRMFPHEFSGGMRQRVMIAMALLCRPKLLI-ADEPTT----ALDVTVQAQIMTLLNelkrefNTAIIMITHDLGVVA 233
Cdd:PTZ00243 1438 --RVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVA 1509
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 556427173 234 GiCDKVLVMYAGRTMEYGKARDVFYQPAHPYSiGLLNAVPRLDA 277
Cdd:PTZ00243 1510 Q-YDKIIVMDHGAVAEMGSPRELVMNRQSIFH-SMVEALGRSEA 1551
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-242 |
1.40e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.78 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafalmgllaangviggsakfngreilnlpeheln 99
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKS------------------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klraeqismifqdpmTslnpymrvgeqLMEVLMlhkglGKAEAFEESVKMLDAVKMPearkrmrMFPHeFSGGMRQRVMI 179
Cdd:cd03221 41 ---------------T-----------LLKLIA-----GELEPDEGIVTWGSTVKIG-------YFEQ-LSGGEKMRLAL 81
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556427173 180 AMALLCRPKLLIADEPTTALDV-TVQAqimtLLNELKrEFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03221 82 AKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALK-EYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-262 |
1.64e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.51 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 10 PQAQQQNNLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQT--AFALMGLLAANGVIGGSAKFNG 87
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrCFNRLNDLIPGFRVEGKVTFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 88 REiLNLPEHELNKLRaEQISMIFQDPmtslNPYMR-------VGEQLMEvlmlHKGlGKAEAFEESVKmlDAVKMPEARK 160
Cdd:PRK14243 77 KN-LYAPDVDPVEVR-RRIGMVFQKP----NPFPKsiydniaYGARING----YKG-DMDELVERSLR--QAALWDEVKD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 161 RMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVL 240
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTA 221
|
250 260 270
....*....|....*....|....*....|.
gi 556427173 241 VMYA---------GRTMEYGKARDVFYQPAH 262
Cdd:PRK14243 222 FFNVeltegggryGYLVEFDRTEKIFNSPQQ 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-256 |
1.68e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLA-ANGVIGGSAKFNGREILNLpEHelnKLRAEQ-ISMIFQ 111
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSgIHEPTKGTITINNINYNKL-DH---KLAAQLgIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 112 -----DPMTSL-NPYmrVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMpeaRKRMRMFPHEFSGGMRQRVMIAMALLC 185
Cdd:PRK09700 88 elsviDELTVLeNLY--IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-251 |
3.57e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 70.37 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGDVTA--VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKFNGreilnLPEHELNKLRAE 104
Cdd:cd03233 9 ISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNG-----IPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 105 QISMIFQDpmTSLNPYMRVgEQLMEVLMLHKGlgkaeafEESVKmldavkmpearkrmrmfphEFSGGMRQRVMIAMALL 184
Cdd:cd03233 84 EIIYVSEE--DVHFPTLTV-RETLDFALRCKG-------NEFVR-------------------GISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVA-GICDKVLVMYAGRTMEYG 251
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQIYYG 202
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
38-245 |
6.87e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKFNGREILNLPE--HELNKLRAeQISMIFQdpmt 115
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRlaRDIRKSRA-NTGYIFQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 116 SLNPYMRVgeQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEA-----RKRMRMFPHE----FSGGMRQRVMIAMALLCR 186
Cdd:PRK09984 94 QFNLVNRL--SVLENVLI-GALGSTPFWRTCFSWFTREQKQRAlqaltRVGMVHFAHQrvstLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 187 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-261 |
1.31e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 14 QQNNLLLDVKDlrVTFKTpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNL 93
Cdd:PRK10247 2 QENSPLLQLQN--VGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS---GTLLFEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 PEHELNKlraeQISMIFQDPMTslnpymrVGEQLMEVLMLHKGL-GKAEAFEESVKMLDAVKMPEA--RKRMrmfpHEFS 170
Cdd:PRK10247 75 KPEIYRQ----QVSYCAQTPTL-------FGDTVYDNLIFPWQIrNQQPDPAIFLDDLERFALPDTilTKNI----AELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMyagrTMEY 250
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL----QPHA 214
|
250
....*....|.
gi 556427173 251 GKARDVFYQPA 261
Cdd:PRK10247 215 GEMQEARYELA 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-256 |
2.50e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.05 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 27 VTFKTPDGdvTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMG----------LLAANGVIGGSAKFNGREILNLPEh 96
Cdd:PRK10575 17 VSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGrhqppsegeiLLDAQPLESWSSKAFARKVAYLPQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 97 elnklraeqismifQDPMTSlnpymrvGEQLMEVLML-----HKGLGKAEAfEESVKMLDAVKMPEARKRMRMFPHEFSG 171
Cdd:PRK10575 93 --------------QLPAAE-------GMTVRELVAIgrypwHGALGRFGA-ADREKVEEAISLVGLKPLAHRLVDSLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
|
....*
gi 556427173 252 KARDV 256
Cdd:PRK10575 231 TPAEL 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
34-256 |
2.59e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREIlnlpEHELNKLRAEQISMIFQDP 113
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHI----QHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 MTSLNpyMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:PRK10253 91 TTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-260 |
3.03e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 28 TFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALmgLLAANGVIGGSAKFNGreiLNLPEHELNKLRAE--- 104
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS-TLLSL--IQRHFDVSEGDIRFHD---IPLTKLQLDSWRSRlav 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 105 --QISMIFQDPMTSlnpymrvgeqlmevlmlHKGLGKAEAFEESVKML--------DAVKMP-----EARKRMRMFphef 169
Cdd:PRK10789 394 vsQTPFLFSDTVAN-----------------NIALGRPDATQQEIEHVarlasvhdDILRLPqgydtEVGERGVML---- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGiCDKVLVMYAGRTME 249
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
250
....*....|.
gi 556427173 250 YGKARDVFYQP 260
Cdd:PRK10789 530 RGNHDQLAQQS 540
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-251 |
8.12e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 67.12 E-value: 8.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgVIGGSAKFNGREILNLPEHEl 98
Cdd:PRK09580 1 MLSIKDLHVSVE----DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE-VTGGTVEFKGKDLLELSPED- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 99 nklRA-EQISMIFQDPM------------TSLNPYMRVGEQlmEVLmlhKGLGKAEAFEESVKMLdavKMPEARkRMRMF 165
Cdd:PRK09580 75 ---RAgEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPL---DRFDFQDLMEEKIALL---KMPEDL-LTRSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 166 PHEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGI-CDKVLVMY 243
Cdd:PRK09580 143 NVGFSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVLY 220
|
....*...
gi 556427173 244 AGRTMEYG 251
Cdd:PRK09580 221 QGRIVKSG 228
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
39-262 |
9.60e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL----AANGV-IGGSAKFNGREILNLPEHELNKLRA-----EQISM 108
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGArVTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 109 IFQ-DPMTSLNPYMrvgeqlmevlmlHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPHEFSGGMRQRVMIAMAL---- 183
Cdd:PRK13547 97 AFSaREIVLLGRYP------------HARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 184 -----LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFy 258
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL- 243
|
....
gi 556427173 259 QPAH 262
Cdd:PRK13547 244 TPAH 247
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-256 |
1.11e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 68.76 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLrvTFKTPDGDV-TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNK 100
Cdd:PRK13545 24 LKDL--FFRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNK---GTVDIKGSAALIAISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 101 lraeQISmifqdpmtslnpymrvGEQLMEVLMLHKGLGKAEAFEESVKMLDavkMPEARKRMRMFPHEFSGGMRQRVMIA 180
Cdd:PRK13545 99 ----QLT----------------GIENIELKGLMMGLTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRLGFA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK13545 156 ISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-261 |
2.34e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.05 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 26 RVTFKT------PDGDVTaVNDLNFNLRAGETLGIVGESGSGKSQTAfalMGLLAANGVIGGSAKFNGreiLNLPEHELN 99
Cdd:TIGR00957 1284 RVEFRNyclryrEDLDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG---LNIAKIGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAeQISMIFQDPM-------TSLNPYMRVGEQlmEVLMLHKgLGKAEAFEESVKMLDAVKMPEARKRMrmfphefSGG 172
Cdd:TIGR00957 1357 DLRF-KITIIPQDPVlfsgslrMNLDPFSQYSDE--EVWWALE-LAHLKTFVSALPDKLDHECAEGGENL-------SVG 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 173 MRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTllnelkrEFNTAIIM-ITHDLGVVAGICdKVLVMYAGRT 247
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLEtdnlIQSTIRT-------QFEDCTVLtIAHRLNTIMDYT-RVIVLDKGEV 1497
|
250 260
....*....|....*....|
gi 556427173 248 MEYG------KARDVFYQPA 261
Cdd:TIGR00957 1498 AEFGapsnllQQRGIFYSMA 1517
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-246 |
2.65e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.12 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFKtPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlpEHELNKL 101
Cdd:TIGR01257 931 VKNLVKIFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS---GTVLVGGKDI----ETNLDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 102 RaEQISMIFQDPMtsLNPYMRVGEQLMEVLMLhKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAM 181
Cdd:TIGR01257 1002 R-QSLGMCPQHNI--LFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEE---AQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-246 |
5.45e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlpehelnklraeqismifqDP 113
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE---GEAWLFGQPV---------------------DA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVG---------EQL--MEVLMLHkglgkAEAFEesvkmldavkMPEARKRMRM---------------FPH 167
Cdd:NF033858 333 -GDIATRRRVGymsqafslyGELtvRQNLELH-----ARLFH----------LPAAEIAARVaemlerfdladvadaLPD 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:NF033858 397 SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMN-EAERCDRISLMHAGR 474
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-245 |
6.32e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 36 VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlpehELNKLRAEQ---ISMIFQD 112
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA---GSILYLGKEV------TFNGPKSSQeagIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 113 pmtsLN--PYMRVGEQLMevlmlhkgLGK-----------AEAFEESVKMLDAVKMPEARKRMRmfpHEFSGGMRQRVMI 179
Cdd:PRK10762 88 ----LNliPQLTIAENIF--------LGRefvnrfgridwKKMYAEADKLLARLNLRFSSDKLV---GELSIGEQQMVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
42-250 |
6.93e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREILNLPEHELNKLraeqISMIFQDPMT------ 115
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE---LEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVLfsgtvr 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 116 -SLNPYMRvgeqlmevlmlHKGLGKAEAFEESvKMLDAVKMPEARKRMRMFP--HEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PLN03232 1328 fNIDPFSE-----------HNDADLWEALERA-HIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 193 DEPTTALDVTVQAQIMTLLNElkrEFNT-AIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE---EFKScTMLVIAHRLNTIID-CDKILVLSSGQVLEY 1450
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-246 |
1.19e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 36 VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANG---VIGGSA-KF-NGREILNlpehelnklraEQISMIF 110
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAgsiLIDGQEmRFaSTTAALA-----------AGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 111 QDpmTSLNPYMRVGEQLMEVLMLHKG--LGKAEAFEESVKMLDAVKM---PEARKRmrmfphEFSGGMRQRVMIAMALLc 185
Cdd:PRK11288 86 QE--LHLVPEMTVAENLYLGQLPHKGgiVNRRLLNYEAREQLEHLGVdidPDTPLK------YLSIGQRQMVEIAKALA- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 186 RPKLLIA-DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11288 157 RNARVIAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-232 |
1.42e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL--AANGVIGGSAKFNGREIlNLpehe 97
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLydPTEGDIIINDSHNLKDI-NL---- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 98 lnKLRAEQISMIFQDPMT--------------SLNPYMRVGEQLME-VLMLHKGLGK--------AEAFEESVKMLDAVK 154
Cdd:PTZ00265 456 --KWWRSKIGVVSQDPLLfsnsiknnikyslySLKDLEALSNYYNEdGNDSQENKNKrnscrakcAGDLNDMSNTTDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 155 MPEARKRM-------------RMFPHEF-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 202
Cdd:PTZ00265 534 LIEMRKNYqtikdsevvdvskKVLIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270
....*....|....*....|....*....|
gi 556427173 203 VQAQIMTLLNELKREFNTAIIMITHDLGVV 232
Cdd:PTZ00265 614 SEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-242 |
1.52e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 37 TAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAangviggsakfngREILNLPEHELNKLRAEQISmifqdpmts 116
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLLA-------------GALKGTPVAGCVDVPDNQFG--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 117 lnpymrvgeqlmEVLMLHKGLGKAEAFEESVKMLDAVKMPEA---RKRmrmfPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:COG2401 98 ------------REASLIDAIGRKGDFKDAVELLNAVGLSDAvlwLRR----FKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556427173 194 EPTTALDVTVqAQIMTL-LNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:COG2401 162 EFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
31-227 |
1.57e-11 |
|
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: 65.16 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 31 TPDGDVTaVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngviggsakFNGReilnlpeheLNKLRAEQISMIF 110
Cdd:TIGR00954 461 TPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV---------YGGR---------LTKPAKGKLFYVP 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 111 QdpmtslNPYMRVG---EQL---MEVL-MLHKGLGKAEAfeesVKMLDAVKMPEARKR------MRMFPHEFSGGMRQRV 177
Cdd:TIGR00954 522 Q------RPYMTLGtlrDQIiypDSSEdMKRRGLSDKDL----EQILDNVQLTHILEReggwsaVQDWMDVLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITH 227
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-241 |
3.10e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMG---------LLAANGVIGGSAKF----- 85
Cdd:PTZ00265 1166 IEIMDVNFRYISRP-NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhIVFKNEHTNDMTNEqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 86 ------------------------------NGREIL----NLPEHELNKLRaEQISMIFQDPMTsLNpyMRVGEQLMevl 131
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfkNSGKILldgvDICDYNLKDLR-NLFSIVSQEPML-FN--MSIYENIK--- 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 132 mlhkgLGKAEAFEESVKMldAVKMPEARKRMRMFPHEF-----------SGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:PTZ00265 1318 -----FGKEDATREDVKR--ACKFAAIDEFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 556427173 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLV 241
Cdd:PTZ00265 1391 SNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-246 |
4.97e-11 |
|
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: 61.33 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTPDGDVTAV-NDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGRE--------I 90
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPGSIayvsqepwI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 91 LNlpehelNKLRaEQIsmIFQDPMtslNPymrvgEQLMEVLmlhkglgKAEAFEESVKMLDAVKMPEArkrmrmfpHE-- 168
Cdd:cd03250 78 QN------GTIR-ENI--LFGKPF---DE-----ERYEKVI-------KACALEPDLEILPDGDLTEI--------GEkg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 169 --FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT--LLNELKRefNTAIIMITHDLGVVAgICDKVLVMYA 244
Cdd:cd03250 126 inLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLP-HADQIVVLDN 202
|
..
gi 556427173 245 GR 246
Cdd:cd03250 203 GR 204
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
42-251 |
6.60e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKLraeqISMIFQDPMT------ 115
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELER---GRILIDGCDISKFGLMDLRKV----LGIIPQAPVLfsgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 116 -SLNPYmrvGEqlmevlmlHKGLGKAEAFEESvKMLDAVkmpeaRKRMRMFPHE-------FSGGMRQRVMIAMALLCRP 187
Cdd:PLN03130 1331 fNLDPF---NE--------HNDADLWESLERA-HLKDVI-----RRNSLGLDAEvseagenFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 188 KLLIADEPTTALDVTVQAQIMTLLNElkrEFNT-AIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIRE---EFKScTMLIIAHRLNTIID-CDRILVLDAGRVVEFD 1454
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
42-232 |
2.44e-10 |
|
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: 59.29 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREIlnlpeHELNKLRAEQISMIFQDPmtSLNPYM 121
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP---DSGEVRWNGTPL-----AEQRDEPHENILYLGHLP--GLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 122 RVGEQLMEVLMLHKGLGKA--EAFEEsVKMLDAVKMPearkrmrmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTieDALAA-VGLTGFEDLP---------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 556427173 200 DVTVQAQIMTLLNE-LKRefNTAIIMITH-DLGVV 232
Cdd:TIGR01189 159 DKAGVALLAGLLRAhLAR--GGIVLLTTHqDLGLV 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-246 |
2.92e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 43 NFNLRAGETLGIVGESGSGKSQtafaLMGLL-AANGVIGGSAKFNGREI-LNLPEHelnKLRAeQISMIFQD-------P 113
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSE----LMKLLyGATRRTAGQVYLDGKPIdIRSPRD---AIRA-GIMLCPEDrkaegiiP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 MTS----LNPYMRvGEQLMEVLMLHKGLGKAEAfEESVKMLdAVKMPEARKRMRmfphEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK11288 345 VHSvadnINISAR-RHHLRAGCLINNRWEAENA-DRFIRSL-NIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 190 LIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
34-262 |
5.12e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQtafalmGLLAANgVIGGSAkfnGREILNLPEHELNKlRAEQISMIFQDP 113
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAH-V*GPDA---GRRPWRF*TWCANR-RALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 MTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMfphEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 194 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGK---------ARDVFYQPAH 262
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKvdelktkvgGRTLQIRPAH 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-228 |
6.31e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.18 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIGGSAKfnGREILNLPEHELNKLRAEQismifqdp 113
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK--GIKLGYFAQHQLEFLRADE-------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 mTSLNPYMRVGEQLMEvLMLHKGLGkAEAFEEsvkmlDAVKMPEARkrmrmfpheFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:PRK10636 393 -SPLQHLARLAPQELE-QKLRDYLG-GFGFQG-----DKVTEETRR---------FSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....*.
gi 556427173 194 EPTTALDVTV-QAqimtlLNELKREFNTAIIMITHD 228
Cdd:PRK10636 456 EPTNHLDLDMrQA-----LTEALIDFEGALVVVSHD 486
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-260 |
8.45e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 47 RAGETLGIVGESGSGKSQTAFALMGLLAAN-GVIGGSAK-------FNGREILNLpeheLNKLRAEQISMIFQDPMTSLN 118
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNlGKFDDPPDwdeildeFRGSELQNY----FTKLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 119 PYMRVGEqlmeVLMLHKGLGKAEAFEESVKMLdavkmpEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 198
Cdd:cd03236 100 PKAVKGK----VGELLKKKDERGKLDELVDQL------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 199 LDVTVQAQIMTLLNELKREFNtAIIMITHDLGVVAGICDKVLVMYaGRTMEYGkardVFYQP 260
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY-GEPGAYG----VVTLP 225
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-256 |
1.37e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRVTFKTpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAfalmgllaanGVIGGSakfngreilnLPEHELNKL 101
Cdd:PRK13546 24 MKDALIPKHK-NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLS----------NIIGGS----------LSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 102 RAEQISMIFQDpmTSLNPYMrVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEarkrmrmFPHE----FSGGMRQRV 177
Cdd:PRK13546 83 RNGEVSVIAIS--AGLSGQL-TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGE-------FIYQpvkkYSSGMRAKL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDV 256
Cdd:PRK13546 153 GFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-232 |
2.59e-09 |
|
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: 56.35 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 42 LNFNLRAGETLGIVGESGSGKSqtafALMGLLAangviGGSAKFNGREILN-LPEHELNKLRAEQISMIFQDP--MTSLN 118
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKT----TLLRILA-----GLSPPLAGRVLLNgGPLDFQRDSIARGLLYLGHAPgiKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 119 PymrvgeqlMEVLMLHKGLGKAEAFEESVkmldavkmpeARKRMRMFPH----EFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:cd03231 90 V--------LENLRFWHADHSDEQVEEAL----------ARVGLNGFEDrpvaQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 556427173 195 PTTALDVTVQAQIMTLLNElKREFNTAIIMITH-DLGVV 232
Cdd:cd03231 152 PTTALDKAGVARFAEAMAG-HCARGGMVVLTTHqDLGLS 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-250 |
3.55e-09 |
|
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: 56.79 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLrvTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIggsaKFNGREILNLPEHELN 99
Cdd:cd03289 3 MTVKDL--TAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDI----QIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRA--EQISMIFQDPM-TSLNPYMRVGEQlmEVLMLHKGLGKAEAFEESVKMLDAVKMPEArkrmrmfpHEFSGGMRQR 176
Cdd:cd03289 77 KAFGviPQKVFIFSGTFrKNLDPYGKWSDE--EIWKVAEEVGLKSVIEQFPGQLDFVLVDGG--------CVLSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 177 VMIAMALLCRPKLLIADEPTTALD-VTVQaqimTLLNELKREFNT-AIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDpITYQ----VIRKTLKQAFADcTVILSEHRIEAMLE-CQRFLVIEENKVRQY 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-259 |
4.83e-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: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREILNLpEHELn 99
Cdd:PRK10790 341 IDIDNVSFAYRD---DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP---LTEGEIRLDGRPLSSL-SHSV- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 kLRaEQISMIFQDPMTslnpymrvgeqLMEVLMLHKGLGKaEAFEESV-KMLDAVKMPEARKRMRMFPH--------EFS 170
Cdd:PRK10790 413 -LR-QGVAMVQQDPVV-----------LADTFLANVTLGR-DISEEQVwQALETVQLAELARSLPDGLYtplgeqgnNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
250
....*....|....*
gi 556427173 251 GK------ARDVFYQ 259
Cdd:PRK10790 556 GThqqllaAQGRYWQ 570
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
42-266 |
6.78e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 55.69 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLaanGVIGGSAKFNGREILNLPEHELNklraEQISMIFQDPMT------ 115
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV---DIFDGKIVIDGIDISKLPLHTLR----SRLSIILQDPILfsgsir 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 116 -SLNPYMR-VGEQLMEVLMLHKGLGKAEAFEESvkmLDAVkMPEARKrmrmfphEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:cd03288 113 fNLDPECKcTDDRLWEALEIAQLKNMVKSLPGG---LDAV-VTEGGE-------NFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 194 EPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKARDVFYQPAHPYSI 266
Cdd:cd03288 182 EATASIDMAteniLQKVVMTAFAD------RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFAS 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-245 |
6.89e-09 |
|
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: 57.33 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREIL-NLPEHELNKLRAEQISMIfQDPMTs 116
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTT---VTSGDATVAGKSILtNISDVHQNMGYCPQFDAI-DDLLT- 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 117 lnpymrvGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMrmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:TIGR01257 2029 -------GREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556427173 197 TALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
49-250 |
1.66e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 49 GETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLPEHELNKLRAEQISMIFQDPmtslnpymRVGEQLM 128
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADG---GSYTFPGNWQLAWVNQETPALPQPALEYVIDGD--------REYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 129 EVLMLHKGLGKAEAFEESVKMLDAVKMPEARKRMRMFPH--------------EFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10636 96 AQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHglgfsneqlerpvsDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 195 PTTALDvtVQAQIMtlLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:PRK10636 176 PTNHLD--LDAVIW--LEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-217 |
2.72e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 43 NFNLRAGETLGIVGESGSGKSQTAFALMGLLAangVIGGSAKFNGREILNLPEHELNKLraeqISMIFQDPMTSLnpyMR 122
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELP---LLSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNTDM---LS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 123 VGEQlmevlmlHKGLGKAEAFEESVKMLDAVKMPEARKRM-----RMFPHeFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:PRK10938 93 PGED-------DTGRTTAEIIQDEVKDPARCEQLAQQFGItalldRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|
gi 556427173 198 ALDVTVQAQIMTLLNELKRE 217
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQS 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-227 |
4.96e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFkTPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGVIggsaKFNGreiLNLPEHELN 99
Cdd:TIGR01271 1218 MDVQGLTAKY-TEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEI----QIDG---VSWNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 KLRAE-----QISMIFQDPM-TSLNPYMRVGEQlmEVLMLHKGLGKAEAFEESVKMLDAVKMPEArkrmrmfpHEFSGGM 173
Cdd:TIGR01271 1289 TWRKAfgvipQKVFIFSGTFrKNLDPYEQWSDE--EIWKVAEEVGLKSVIEQFPDKLDFVLVDGG--------YVLSNGH 1358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 174 RQRVMIAMALLCRPKLLIADEPTTALD-VTVQaqimTLLNELKREF-NTAIIMITH 227
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDpVTLQ----IIRKTLKQSFsNCTVILSEH 1410
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-253 |
8.11e-08 |
|
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: 52.41 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 45 NLRAGETLGIVGESGSGKsqTAFALMglLAangvigGSAKFNGREIlnlpEHELNKL--RAEQISMIFQdpmtslnpyMR 122
Cdd:cd03237 21 SISESEVIGILGPNGIGK--TTFIKM--LA------GVLKPDEGDI----EIELDTVsyKPQYIKADYE---------GT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 123 VGEQLMEVLmlhKGLGKAEAFE-ESVKMLDAVKMPEARKRmrmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 201
Cdd:cd03237 78 VRDLLSSIT---KDFYTHPYFKtEIAKPLQIEQILDREVP------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556427173 202 TVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVmYAGRTMEYGKA 253
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEGEPSVNGVA 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
49-231 |
8.76e-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: 50.83 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 49 GETLGIVGESGSGKSQTAFALMGLLAANGviGGSAKFNGREILNLPEHELNKlraeqismifqdpmtslnpymrvgeqlm 128
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG--GGVIYIDGEDILEEVLDQLLL---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 129 evlmlhkglgkaeafeesvkmldavkmpearKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM 208
Cdd:smart00382 52 -------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180
....*....|....*....|....*...
gi 556427173 209 -----TLLNELKREFNTAIIMITHDLGV 231
Cdd:smart00382 101 lleelRLLLLLKSEKNLTVILTTNDEKD 128
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
168-228 |
9.86e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 9.86e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556427173 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKrEFNTAIIMITHD 228
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLK-TFQGSIIFISHD 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-214 |
1.28e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 51.09 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 17 NLLLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAAN---GVIGGSAKFNGREIlnl 93
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKT----TLLDVLAGRktaGVITGEILINGRPL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 94 pehELNKLR----AEQismifqdpMTSLNPYMRVGEQLMEVLMLhKGLGkaeafeesvkmldavkmPEARKrmrmfphef 169
Cdd:cd03232 74 ---DKNFQRstgyVEQ--------QDVHSPNLTVREALRFSALL-RGLS-----------------VEQRK--------- 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556427173 170 sggmrqRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNEL 214
Cdd:cd03232 116 ------RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
170-253 |
1.70e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFN-TAIIMI------THDLgvvagiCDKVLVM 242
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIyqcsqdAYEL------FDKVIVL 284
|
90
....*....|.
gi 556427173 243 YAGRTMEYGKA 253
Cdd:TIGR00956 285 YEGYQIYFGPA 295
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-254 |
1.74e-07 |
|
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: 52.48 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 46 LRAGETLGIVGESGSGKsqTAFALMglLAanGVI---GGSAKFNGReILNLP---EHELNKLRAEQISMIFQDPMTSlnP 119
Cdd:COG1245 363 IREGEVLGIVGPNGIGK--TTFAKI--LA--GVLkpdEGEVDEDLK-ISYKPqyiSPDYDGTVEEFLRSANTDDFGS--S 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 120 YMRvgEQLMEVLMLHKglgkaeafeesvkMLDavkmpearKRMRmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:COG1245 434 YYK--TEIIKPLGLEK-------------LLD--------KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 200 DVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVmYAGRTMEYGKAR 254
Cdd:COG1245 487 DVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV-FEGEPGVHGHAS 540
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
34-246 |
4.57e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.26 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREILNLpehelnklraeQISMIFQDP 113
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATS---GRIVFDGKDITDW-----------QTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 MTSLNPYMRVGEQLM--EVLMLHKGLGKAEAFEESVKMLDAVkMPEARKRMRMFPHEFSGGMRQRVMIAMALLCRPKLLI 191
Cdd:PRK11614 82 VAIVPEGRRVFSRMTveENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 192 ADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGH 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-231 |
5.26e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.49 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTfktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREIlNLPEHeln 99
Cdd:PRK13539 3 LEGEDLACV----RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP---AAGTIKLDGGDI-DDPDV--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 100 klrAEQISMI-FQDPMtslNPYMRVGEQLmevLMLHKGLGKAEAFEESVkmLDAVKMPEARKRmrmfP-HEFSGGMRQRV 177
Cdd:PRK13539 72 ---AEACHYLgHRNAM---KPALTVAENL---EFWAAFLGGEELDIAAA--LEAVGLAPLAHL----PfGYLSAGQKRRV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITH-DLGV 231
Cdd:PRK13539 137 ALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-255 |
6.61e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAanGVI---GGSAKFNGReilnlPE 95
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKS----TLMKIIA--GIVppdSGTLEIGGN-----PC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 96 HELNKLRAEQ--ISMIFQDPMtsLNPYMRVGEQLMevlmlhKGLGKAEAFEESVKMLdavkmpEARKRMRMFPHEFSGGM 173
Cdd:PRK15439 76 ARLTPAKAHQlgIYLVPQEPL--LFPNLSVKENIL------FGLPKRQASMQKMKQL------LAALGCQLDLDSSAGSL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 174 ----RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:PRK15439 142 evadRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
....*.
gi 556427173 250 YGKARD 255
Cdd:PRK15439 221 SGKTAD 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
49-234 |
7.51e-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: 50.70 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 49 GETLGIVGESGSGKSqtafALMGLLAanGV---IGGSAKF-------------------NGREILNLPEHELNKL--RAE 104
Cdd:TIGR03719 31 GAKIGVLGLNGAGKS----TLLRIMA--GVdkdFNGEARPqpgikvgylpqepqldptkTVRENVEEGVAEIKDAldRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 105 QISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEesVKMlDAVKMPEARKRMRmfphEFSGGMRQRVMIAMALL 184
Cdd:TIGR03719 105 EISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLE--IAM-DALRCPPWDADVT----KLSGGERRRVALCRLLL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556427173 185 CRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 234
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHDryfLDNVAG 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
36-246 |
7.95e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 36 VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlpEHELNKLRAEQ-ISMIFQDpm 114
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS---GSILFQGKEI----DFKSSKEALENgISMVHQE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 115 tsLNPYMRvgEQLMEVLML----HKGLgkaeaFEESVKMLDAVKMPEARKRMRMFPHE----FSGGMRQRVMIAMALLCR 186
Cdd:PRK10982 82 --LNLVLQ--RSVMDNMWLgrypTKGM-----FVDQDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 187 PKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-254 |
9.46e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 9 APQAQQQNNLLLDVKDLRVTFKtpdgdvtavndlNFNL-------RAGETLGIVGESGSGKsqTAFALMglLAanGVI-- 79
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLG------------DFSLeveggeiYEGEVIGIVGPNGIGK--TTFAKL--LA--GVLkp 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 80 -GGSakfngreilnlpehelnklraeqismIFQDPMTSLNP-Y------MRVGEQLMEVlmlhkglgkAEAFEES----- 146
Cdd:PRK13409 392 dEGE--------------------------VDPELKISYKPqYikpdydGTVEDLLRSI---------TDDLGSSyykse 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 147 -VKMLDAVKMPEarKRMRmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMI 225
Cdd:PRK13409 437 iIKPLQLERLLD--KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVV 510
|
250 260
....*....|....*....|....*....
gi 556427173 226 THDLGVVAGICDKVLVmYAGRTMEYGKAR 254
Cdd:PRK13409 511 DHDIYMIDYISDRLMV-FEGEPGKHGHAS 538
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-243 |
9.98e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 46 LRAGETLGIVGESGSGKSQTAFALMGLLAAN-GVIGGSA-------KFNGREILNLpeheLNKLRAEQISmifqdpmTSL 117
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNlGDYDEEPswdevlkRFRGTELQDY----FKKLANGEIK-------VAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 118 NPymrvgeQLMEVL-MLHKG-----LGKAE---AFEESVKMLDAVKMPEarKRMRmfphEFSGGMRQRVMIAMALLCRPK 188
Cdd:COG1245 165 KP------QYVDLIpKVFKGtvrelLEKVDergKLDELAEKLGLENILD--RDIS----ELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMY 243
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-286 |
1.21e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 46 LRAGETLGIVGESGSGKSQTAFALMGLLAAN-----------GVIggsAKFNGREILNLPEhEL--NKLRA-------EQ 105
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdEVL---KRFRGTELQNYFK-KLynGEIKVvhkpqyvDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 106 ISMIFQDpmtslnpymRVGEQLMEVlmlhkglGKAEAFEESVKMLDAVKMPEarKRMRmfphEFSGGMRQRVMIAMALLC 185
Cdd:PRK13409 172 IPKVFKG---------KVRELLKKV-------DERGKLDEVVERLGLENILD--RDIS----ELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYaGRTMEYGkardVFYQPA---- 261
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY-GEPGAYG----VVSKPKgvrv 302
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 556427173 262 -----------------HPYSIGLLNAVPRLDAEGESLLTIP 286
Cdd:PRK13409 303 gineylkgylpeenmriRPEPIEFEERPPRDESERETLVEYP 344
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
54-228 |
2.21e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.60 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 54 IVGESGSGKSQT----AFALMGLLAANGVIG-GSAKFNGReilnlpehelNKLRAeQISMIFQDPMTSLNPYMRVGEQLM 128
Cdd:cd03240 27 IVGQNGAGKTTIiealKYALTGELPPNSKGGaHDPKLIRE----------GEVRA-QVKLAFENANGKKYTITRSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 129 EVLMLHKGlgkaeafeESVKMLdavkmPEARKRMrmfphefSGGMRQ------RVMIAMALLCRPKLLIADEPTTALDV- 201
Cdd:cd03240 96 NVIFCHQG--------ESNWPL-----LDMRGRC-------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEe 155
|
170 180
....*....|....*....|....*..
gi 556427173 202 TVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:cd03240 156 NIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
35-229 |
4.62e-06 |
|
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: 46.94 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 35 DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGREILNLPEHELNKLRAEQISMIFQDP- 113
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT---LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 114 ---------MTSLNPYMRvgeqlmevlMLHKGLGKAEAFEESVKMLDAVKMPEARKRmrmfPHEFSGGMRQRVMIAMALL 184
Cdd:cd03290 90 llnatveenITFGSPFNK---------QRYKAVTDACSLQPDIDLLPFGDQTEIGER----GINLSGGQRQRICVARALY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556427173 185 CRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 229
Cdd:cd03290 157 QNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-253 |
4.94e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 136 GLGKAEAfeesVKMLDAVKMPEA------RKRMRMFPH--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 207
Cdd:cd03222 35 GTGKTTA----VKILAGQLIPNGdndewdGITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 556427173 208 MTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYaGRTMEYGKA 253
Cdd:cd03222 111 ARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGIA 155
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-228 |
5.41e-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: 48.01 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 10 PQAQQQNNLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALmgllaangvIGGSAKFNGRE 89
Cdd:TIGR03719 313 PPGPRLGDKVIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKS-TLFRM---------ITGQEQPDSGT 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 90 IlnlpehELnklrAEQISMIFQDPM-TSLNPYMRVGEQL---MEVLMLhkglGKAE--------AFeesvkmldAVKMPE 157
Cdd:TIGR03719 379 I------EI----GETVKLAYVDQSrDALDPNKTVWEEIsggLDIIKL----GKREipsrayvgRF--------NFKGSD 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556427173 158 ARKRMRmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 228
Cdd:TIGR03719 437 QQKKVG----QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD 499
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
32-231 |
7.85e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 32 PDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFAlmgllaangviGGSAKFNGREILNLPEHELNKLraeqismIFQ 111
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-----------GLYASGKARLISFLPKFSRNKL-------IFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 112 DPMTSLNP----YMRVGeQLMEVLmlhkglgkaeafeesvkmldavkmpearkrmrmfphefSGGMRQRVMIAMALLCRP 187
Cdd:cd03238 66 DQLQFLIDvglgYLTLG-QKLSTL--------------------------------------SGGELQRVKLASELFSEP 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556427173 188 K--LLIADEPTTALDvtvQAQIMTLLNELKR---EFNTaIIMITHDLGV 231
Cdd:cd03238 107 PgtLFILDEPSTGLH---QQDINQLLEVIKGlidLGNT-VILIEHNLDV 151
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-112 |
1.04e-05 |
|
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: 47.10 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 20 LDVKDLRVTFKTPDGDVT-AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgviGGSAKFNGREIlnlPEHEL 98
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE---SGEILLDGQPV---TADNR 401
|
90
....*....|....
gi 556427173 99 NKLRaEQISMIFQD 112
Cdd:COG4615 402 EAYR-QLFSAVFSD 414
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
41-234 |
2.17e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.79 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGvigGSAKFNGREIlnlpehelNKLRAEqismiFQDPM------ 114
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDA---GEVLWQGEPI--------RRQRDE-----YHQDLlylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 115 ----TSLNPYmrvgEQLMEVLMLHKGLGKAEAFEesvkMLDAVKMpeaRKRMRMFPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK13538 83 pgikTELTAL----ENLRFYQRLHGPGDDEALWE----ALAQVGL---AGFEDVPVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556427173 191 IADEPTTALDVTVQAQIMTLLNE-LKRefNTAIIMITH-DLGVVAG 234
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQhAEQ--GGMVILTTHqDLPVASD 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
170-233 |
2.32e-05 |
|
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: 43.89 E-value: 2.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 170 SGGMRQRVMIAMAL-LCRPK---LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVA 233
Cdd:cd03227 79 SGGEKELSALALILaLASLKprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAE 145
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
41-251 |
2.45e-05 |
|
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: 45.23 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgviGGSAKFNGREILnlpehelnklrAEQISMIFqdPMTslnpy 120
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS---EGKIKHSGRISF-----------SSQFSWIM--PGT----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 121 mrVGEQLMEVLML----HKGLGKAEAFEEsvkmlDAVKMPEARKR-MRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:cd03291 114 --IKENIIFGVSYdeyrYKSVVKACQLEE-----DITKFPEKDNTvLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556427173 196 TTALDVTVQAQIMTLLnELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYG 251
Cdd:cd03291 187 FGYLDVFTEKEIFESC-VCKLMANKTRILVTSKMEHLK-KADKILILHEGSSYFYG 240
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
170-232 |
2.56e-05 |
|
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: 46.16 E-value: 2.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556427173 170 SGGMRQRVMIAMALLCR---PKLLIADEPTTAL---DVtvqAQIMTLLNELKREFNTaIIMITHDLGVV 232
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGNT-VVVIEHNLDVI 895
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
170-246 |
4.56e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 4.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLnelkrEFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-251 |
6.91e-05 |
|
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: 44.94 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 28 TFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAngvIGGSAKFNGrEILNLPEHELNKLRAEQIS 107
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK---VEGHVHMKG-SVAYVPQQAWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 108 MIFQDPMTSlNPYMRVGEQ---LMEVLMLHKGlGKAEAFEESVKMldavkmpearkrmrmfphefSGGMRQRVMIAMALL 184
Cdd:TIGR00957 719 ILFGKALNE-KYYQQVLEAcalLPDLEILPSG-DRTEIGEKGVNL--------------------SGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556427173 185 CRPKLLIADEPTTALDVTVQAQI-------MTLLNELKRefntaiIMITHDLGVVAGIcDKVLVMYAGRTMEYG 251
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIfehvigpEGVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
170-234 |
7.40e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 7.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 234
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHDryfLDNVAG 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-251 |
8.54e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 32 PDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLA----ANGVIGGSAKFngreilnLPehelnklraeQIS 107
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPprsdASVVIRGTVAY-------VP----------QVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 108 MIF----QDPMTSLNPYMRVG-EQLMEVLMLHKGLgkaeafeesvKMLDAVKMPEARKRMRmfphEFSGGMRQRVMIAMA 182
Cdd:PLN03130 689 WIFnatvRDNILFGSPFDPERyERAIDVTALQHDL----------DLLPGGDLTEIGERGV----NISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 183 LLCRPKLLIADEPTTALDVTVQAQIMTllNELKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYG 251
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-201 |
1.12e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 22 VKDLRV-TFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGV------------IGGSAKFNGR 88
Cdd:PLN03073 175 IKDIHMeNFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKT-TFLRYMAMHAIDGIpkncqilhveqeVVGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 89 EILNlPEHELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGLGKAEAFEESVKMLDAVKMPEARKR------- 161
Cdd:PLN03073 254 CVLN-TDIERTQLLEEEAQLVAQQ--RELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARaasilag 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556427173 162 -------MRMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 201
Cdd:PLN03073 331 lsftpemQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
170-228 |
1.72e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 1.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556427173 170 SGGMRQRVMIAmALLCRP-KLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 228
Cdd:PRK11147 442 SGGERNRLLLA-RLFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
170-217 |
5.60e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 5.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 556427173 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRE 217
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
170-240 |
7.89e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 7.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556427173 170 SGGMRQRVMIAMALLC---RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAgICDKVL 240
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI-IEHNMHVVK-VADYVL 882
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
159-229 |
9.90e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.41 E-value: 9.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556427173 159 RKRMRMFP-HEFSGGMRQRVMIAMAL---LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 229
Cdd:COG1106 192 KGGNVPLPlSEESDGTKRLLALAGALldaLAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHST 266
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
172-228 |
3.73e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 3.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 556427173 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELkREFNTAIIMITHD 228
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVL-NERNSTMIIISHD 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
174-214 |
4.67e-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: 4.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556427173 174 RQRVMIAMALLCRPKLLI-ADEPTTALDVTVQAQIMTLLNEL 214
Cdd:TIGR00956 907 RKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
|