|
Name |
Accession |
Description |
Interval |
E-value |
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-336 |
0e+00 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 773.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 9 APQAAQQSGLLLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGR 88
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 89 EILNLPERDLNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHE 168
Cdd:PRK09473 82 EILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 249 EYGQARDVFYQPSHPYSIGLLNAVPRLDGEGDSLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLESFAPGRLRA 328
Cdd:PRK09473 242 EYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFGPGRLRA 321
|
....*...
gi 505807353 329 CFKPVGDL 336
Cdd:PRK09473 322 CFKPVEEL 329
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-332 |
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: 551.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGREILNLPERDL 98
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVM 178
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFY 258
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 259 QPSHPYSIGLLNAVPRLDGEGDSLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC-NSAPPLESFAPGRLRACFKP 332
Cdd:COG0444 241 NPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCrEEEPPLREVGPGHRVACHLY 315
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-294 |
3.45e-148 |
|
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: 427.95 E-value: 3.45e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANG-HISGSATFNGREILNLPERD 97
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAaHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRV 177
Cdd:COG4172 86 LRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 505807353 258 YQPSHPYSIGLLNAVPRLDgegdsLLTIPGNPPNLLR 294
Cdd:COG4172 246 AAPQHPYTRKLLAAEPRGD-----PRPVPPDAPPLLE 277
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-251 |
1.84e-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: 358.74 E-value: 1.84e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERdL 98
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT---SGSIIFDGKDLLKLSRR-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEEsVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVM 178
Cdd:cd03257 77 RKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKE-AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-330 |
5.91e-121 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 351.34 E-value: 5.91e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTF-------KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIL 91
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT---SGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 92 NLPERDLNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKM-PEARKRmkmFPHEFS 170
Cdd:COG4608 84 GLSGRELRPLRR-RMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR---YPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 251 GQARDVFYQPSHPYSIGLLNAVPRLDGEGDS---LLTipGNPPNLLRLPKGCPFQPRCPHAMEIC-NSAPPLESFAPGRL 326
Cdd:COG4608 240 APRDELYARPLHPYTQALLSAVPVPDPERRReriVLE--GDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLREVGPGHQ 317
|
....
gi 505807353 327 RACF 330
Cdd:COG4608 318 VACH 321
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-278 |
1.89e-110 |
|
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: 331.10 E-value: 1.89e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 9 APQAAQQSGLLLDVKDLRVTFKT-PDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNG 87
Cdd:COG1123 250 AAPAAAAAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT---SGSILFDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 88 REILNLPERDLNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARkrMKMFPH 167
Cdd:COG1123 327 KDLTKLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDL--ADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
250 260 270
....*....|....*....|....*....|.
gi 505807353 248 MEYGQARDVFYQPSHPYSIGLLNAVPRLDGE 278
Cdd:COG1123 484 VEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-295 |
1.04e-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: 1.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGREILNLPERdl 98
Cdd:COG1123 4 LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 nkLRAEQISMIFQDPMTSLNPyMRVGEQLMEVLMLHkGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVM 178
Cdd:COG1123 80 --LRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENL-GLSRAEARARVLELLEAVGLERRLDR---YPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFY 258
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 505807353 259 QPShpysigLLNAVPRLDGEGDSLLTIPGNPPNLLRL 295
Cdd:COG1123 233 APQ------ALAAVPRLGAARGRAAPAAAAAEPLLEV 263
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-335 |
1.76e-107 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 317.07 E-value: 1.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSA-TFNGREILNLPERD 97
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKlEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRV 177
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 258 YQPSHPYSIGLLNAVPRLDGEGDSLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLESFAPGRLRACFKPVGD 335
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKCHYPLDD 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-276 |
1.26e-99 |
|
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: 303.53 E-value: 1.26e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 9 APQAAQQSGLLLDVKDLRVTFKTPDG-------DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHIsg 81
Cdd:COG4172 265 PRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEI-- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 82 saTFNGREILNLPERDLNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHK-GLSKAAAFEESVRMLDAVKM-PEAR 159
Cdd:COG4172 343 --RFDGQDLDGLSRRALRPLRR-RMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAAR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 160 KRmkmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 239
Cdd:COG4172 420 HR---YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRV 496
|
250 260 270
....*....|....*....|....*....|....*..
gi 505807353 240 LVMYAGRTMEYGQARDVFYQPSHPYSIGLLNAVPRLD 276
Cdd:COG4172 497 MVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-294 |
1.06e-97 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 298.93 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANG--HISGSATFNGREILNLPER 96
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPvvYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 97 DLNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQR 176
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 505807353 257 FYQPSHPYSIGLLNAVPrldgEGDSlLTIPGNPPNLLR 294
Cdd:PRK15134 245 FSAPTHPYTQKLLNSEP----SGDP-VPLPEPASPLLD 277
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
13-320 |
4.64e-92 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 277.74 E-value: 4.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 13 AQQSGLLLDVKDLRVTFKTPDGD---------VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSA 83
Cdd:PRK15079 2 TEGKKVLLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT---DGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 84 TFNGREILNLPERDLNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVL-MLHKGLSKAAAFEESVRMLDAVKM-PEARKR 161
Cdd:PRK15079 79 AWLGKDLLGMKDDEWRAVRSD-IQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLlPNLINR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 162 mkmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 241
Cdd:PRK15079 158 ---YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 242 MYAGRTMEYGQARDVFYQPSHPYSIGLLNAVPRLDG-----------EGDslLTIPGNPPNllrlpkGCPFQPRCPHAME 310
Cdd:PRK15079 235 MYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPdlernktiqllEGE--LPSPINPPS------GCVFRTRCPIAGP 306
|
330
....*....|.
gi 505807353 311 IC-NSAPPLES 320
Cdd:PRK15079 307 ECaKTRPVLEG 317
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-275 |
5.95e-92 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 286.75 E-value: 5.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATF----NGREILNLP 94
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 95 ER---DLNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSG 171
Cdd:PRK10261 92 EQsaaQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|....
gi 505807353 252 QARDVFYQPSHPYSIGLLNAVPRL 275
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQL 275
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-278 |
1.03e-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: 271.29 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangHISGSATFNGREILNLPERDL 98
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER---PWSGEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKlraeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKglsKAAAFEESVRMLDAVKMPEA-RKRmkmFPHEFSGGMRQRV 177
Cdd:COG1124 78 RR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLPPSfLDR---YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250 260
....*....|....*....|.
gi 505807353 258 YQPSHPYSIGLLNAVPRLDGE 278
Cdd:COG1124 228 AGPKHPYTRELLAASLAFERA 248
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-319 |
2.24e-90 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 273.32 E-value: 2.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSA-TFNGREILNLPERD 97
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRfRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVL---------MLHKGLSKAAAfeesVRMLDAVKMPEARKRMKMFPHE 168
Cdd:COG4170 83 RRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpswtfkgkwWQRFKWRKKRA----IELLHRVGIKDHKDIMNSYPHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807353 249 EYGQARDVFYQPSHPYSIGLLNAVPRLDGEGDS---LLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLE 319
Cdd:COG4170 239 ESGPTEQILKSPHHPYTKALLRSMPDFRQPLPHksrLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLR 312
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-330 |
1.30e-88 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 268.76 E-value: 1.30e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 15 QSGLLLDVKDL-------RVTFKtPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNG 87
Cdd:PRK11308 1 SQQPLLQAIDLkkhypvkRGLFK-PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPT---GGELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 88 REILNlPERDLNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKM-PEARKRmkmFP 166
Cdd:PRK11308 77 QDLLK-ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 247 TMEYGQARDVFYQPSHPYSIGLLNAVPRLDGEGDSL-LTIPGNPPNLLRLPKGCPFQPRCPHAMEICNS-APPLESFApG 324
Cdd:PRK11308 233 CVEKGTKEQIFNNPRHPYTQALLSATPRLNPDDRRErIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQeQPQLRDYD-G 311
|
....*.
gi 505807353 325 RLRACF 330
Cdd:PRK11308 312 RLVACF 317
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
38-271 |
1.87e-79 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 241.89 E-value: 1.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHI-SGSATFNGREILNLperdlnKLRAEQISMIFQDPMTS 116
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQtSGEILLDGRPLLPL------SIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LNPYMRVGEQLMEVLMLHKGLSKAAaFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSKQA-RALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGLLNA 271
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-333 |
3.68e-75 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 234.70 E-value: 3.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSA-TFNGREILNLPERD 97
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRmRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVL--MLHKG-------LSKAAAFEesvrMLDAVKMPEARKRMKMFPHE 168
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgWTYKGrwwqrfgWRKRRAIE----LLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 249 EYGQARDVFYQPSHPYSIGLLNAVPRLdgeGDS------LLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNSAPPLESfA 322
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPDF---GSAmphksrLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTG-A 314
|
330
....*....|.
gi 505807353 323 PGRLRACFKPV 333
Cdd:PRK15093 315 KNHLYACHFPL 325
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-269 |
9.56e-67 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 218.42 E-value: 9.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 9 APQAAQQSGLLLDVKDLRVTF-------KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHIsg 81
Cdd:PRK15134 265 PVPLPEPASPLLDVEQLQVAFpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEI-- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 82 saTFNGREILNLPERDLNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLH-KGLSKAAAFEESVRMLDAVKM-PEAR 159
Cdd:PRK15134 343 --WFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLdPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 160 KRmkmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 239
Cdd:PRK15134 420 HR---YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
|
250 260 270
....*....|....*....|....*....|
gi 505807353 240 LVMYAGRTMEYGQARDVFYQPSHPYSIGLL 269
Cdd:PRK15134 497 IVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
19-271 |
1.06e-65 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 208.15 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDG-----DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREilnL 93
Cdd:COG4167 4 LLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPT---SGEILINGHK---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 PERDlNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSkAAAFEESVRM-LDAVKM-PEarkRMKMFPHEFSG 171
Cdd:COG4167 78 EYGD-YKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLT-AEEREERIFAtLRLVGLlPE---HANFYPHMLSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYG 232
|
250 260
....*....|....*....|
gi 505807353 252 QARDVFYQPSHPYSIGLLNA 271
Cdd:COG4167 233 KTAEVFANPQHEVTKRLIES 252
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
6-272 |
1.07e-65 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 207.74 E-value: 1.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 6 MTKAPQAaqqsglLLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATF 85
Cdd:COG4107 1 MTNEEQP------LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPT---SGSVYY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 86 NGRE-----ILNLPERDLNKLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKGLSKAAAFEesvrMLDAVK 154
Cdd:COG4107 72 RDRDggprdLFALSEAERRRLRRTDWGMVYQNPRDGLR--MDVsaggniAERLMAAGERHYGDIRARALE----WLERVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 155 MPEARkrMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAG 234
Cdd:COG4107 146 IPLER--IDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRL 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 505807353 235 ICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGLLNAV 272
Cdd:COG4107 224 LADRTMVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-246 |
8.01e-63 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 199.11 E-value: 8.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL-AANghiSGSATFNGREILNLPERD 97
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdRPT---SGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAEQISMIFQDPmtSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEarkRMKMFPHEFSGGMRQRV 177
Cdd:COG1136 80 LARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGR 246
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-276 |
2.40e-62 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 208.94 E-value: 2.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 7 TKAPQAAQQSGL----LLDVKDLRVTFKTPDG-------DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAA 75
Cdd:PRK10261 297 KQEPPIEQDTVVdgepILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVES 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 76 NGhisGSATFNGREILNLPERDLNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKM 155
Cdd:PRK10261 377 QG---GEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 156 -PEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAG 234
Cdd:PRK10261 453 lPEHAWR---YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVER 529
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 505807353 235 ICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGLLNAVPRLD 276
Cdd:PRK10261 530 ISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVAD 571
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-246 |
3.51e-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: 192.32 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGhiSGSATFNGREILNLPERDLN 99
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPT--SGEVRVDGTDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAEQISMIFQDPmtSLNPYMRVGEQLMeVLMLHKGLSKAAAFEESVRMLDAVKMPEarkRMKMFPHEFSGGMRQRVMI 179
Cdd:cd03255 78 AFRRRHIGFVFQSF--NLLPDLTALENVE-LPLLLAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGR 246
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-251 |
1.43e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.64 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANghiSGSATFNGREIlnlpERDL 98
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIrMLLGLLRPT---SGEVRVLGEDV----ARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHkGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGGMRQRVM 178
Cdd:COG1131 69 AEVRR-RIGYVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRK---VGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
22-261 |
4.20e-53 |
|
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: 174.69 E-value: 4.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGhiSGSATFNGREILNLPERDLNKL 101
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPT--SGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 102 RAeQISMIFQ--DPMTSLNpymrVGEQLMEVLMLHkGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMI 179
Cdd:cd03258 81 RR-RIGMIFQhfNLLSSRT----VFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKADA---YPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQ 259
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 505807353 260 PS 261
Cdd:cd03258 232 PQ 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
35-271 |
4.61e-53 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 175.27 E-value: 4.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 35 DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghisGSATFNGREILNLPERDLNKLRAEQISMIFQDPM 114
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA-----GVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 115 TSLNPYMRVGEQLMEVLmlhKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10418 90 SAFNPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGLLNA 271
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-295 |
5.74e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 177.58 E-value: 5.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLaaNG---HISGSATFNGREILNLPERDL 98
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-T---LIRCI--NLlerPTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAeQISMIFQDP--MTSLN-------PymrvgeqlMEVLmlhkGLSKAAAfEESVR-MLDAVKMPEarkRMKMFPHE 168
Cdd:COG1135 78 RAARR-KIGMIFQHFnlLSSRTvaenvalP--------LEIA----GVPKAEI-RKRVAeLLELVGLSD---KADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 505807353 249 EYGQARDVFYQPSHPYSIGLLNAVPRLDGEGDSLLTIPGNPPN--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 |
1.14e-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: 171.55 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGR-----EILNL 93
Cdd:TIGR02323 3 LLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPD---HGTATYIMRsgaelELYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 PERDLNKLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKGLSKAAAfeesVRMLDAVKMPeaRKRMKMFPH 167
Cdd:TIGR02323 76 SEAERRRLMRTEWGFVHQNPRDGLR--MRVsaganiGERLMAIGARHYGNIRATA----QDWLEEVEID--PTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....*
gi 505807353 248 MEYGQARDVFYQPSHPYSIGLLNAV 272
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-264 |
5.73e-51 |
|
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: 169.39 E-value: 5.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDL 98
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD---SGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAeQISMIFQDP--MTSLNpymrVGEQLMEVLMLHKGLSKAAAfEESVRM-LDAVKMPEARKRMkmfPHEFSGGMRQ 175
Cdd:COG1127 78 YELRR-RIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEI-RELVLEkLELVGLPGAADKM---PSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALD-VTVqAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGqAR 254
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG-TP 226
|
250
....*....|
gi 505807353 255 DVFYQPSHPY 264
Cdd:COG1127 227 EELLASDDPW 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-260 |
7.28e-50 |
|
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: 165.97 E-value: 7.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangHISGSATFNGREILnlpERDLN 99
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK---PTSGEVLVDGKDIT---KKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRaEQISMIFQDP-----MTSlnpymrVGEqlmEVL--MLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGG 172
Cdd:COG1122 72 ELR-RKVGLVFQNPddqlfAPT------VEE---DVAfgPENLGLPREEIRERVEEALELVGLEHLADR---PPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQ 252
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
....*...
gi 505807353 253 ARDVFYQP 260
Cdd:COG1122 218 PREVFSDY 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-265 |
2.19e-49 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 165.87 E-value: 2.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGR-----EILNL 93
Cdd:PRK11701 6 LLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD---AGEVHYRMRdgqlrDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 PERDLNKLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKGLSKAAAfeesVRMLDAVKMPEARkrMKMFPH 167
Cdd:PRK11701 79 SEAERRRLLRTEWGFVHQHPRDGLR--MQVsaggniGERLMAVGARHYGDIRATA----GDWLERVEIDAAR--IDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|....*...
gi 505807353 248 MEYGQARDVFYQPSHPYS 265
Cdd:PRK11701 231 VESGLTDQVLDDPQHPYT 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-253 |
1.55e-48 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 162.60 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANghiSGSATFNGREILNLPERD 97
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLaGLDRPT---SGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAEQISMIFQDPMtsLNPYMRVGEQLMEVLMLhkgLSKAAAFEESVRMLDAVKMPEarkRMKMFPHEFSGGMRQRV 177
Cdd:COG4181 84 RARLRARHVGFVFQSFQ--LLPTLTALENVMLPLEL---AGRRDARARARALLERVGLGH---RLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGQA 253
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRLVEDTAA 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
27-246 |
2.11e-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: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDLnklrAEQI 106
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP---TSGEVLVDGKDLTKLSLKEL----RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQDPMTSL-NPymRVGEqlmEVL--MLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMAL 183
Cdd:cd03225 78 GLVFQNPDDQFfGP--TVEE---EVAfgLENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 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 |
3.70e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.57 E-value: 3.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLP--ER 96
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD---SGRILLDGRDVTGLPpeKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 97 DlnklraeqISMIFQDPmtSLNPYMRVGEQLMEVLMlHKGLSKAAAfEESVR-MLDAVKMPEARKRMkmfPHEFSGGMRQ 175
Cdd:COG3842 78 N--------VGMVFQDY--ALFPHLTVAENVAFGLR-MRGVPKAEI-RARVAeLLELVGLEGLADRY---PHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 256 VFYQPSHPYS---IGLLNAVP-RLDGEGDSLLTIPGNPpnlLRLPKGCPFQP--------RcPHAMEIcnSAPPLESFAP 323
Cdd:COG3842 223 IYERPATRFVadfIGEANLLPgTVLGDEGGGVRTGGRT---LEVPADAGLAAggpvtvaiR-PEDIRL--SPEGPENGLP 296
|
....*
gi 505807353 324 GRLRA 328
Cdd:COG3842 297 GTVED 301
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-257 |
1.19e-46 |
|
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: 158.28 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAAnghISGSATFNGREILNLPERD 97
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKP---SSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 lnklRAEQISMIFQDPMTSLNpyMRVgeqlMEVLML----HKG----LSKA--AAFEESVRMLDAVKMpeARKRMkmfpH 167
Cdd:COG1120 73 ----LARRIAYVPQEPPAPFG--LTV----RELVALgrypHLGlfgrPSAEdrEAVEEALERTGLEHL--ADRPV----D 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250
....*....|
gi 505807353 248 MEYGQARDVF 257
Cdd:COG1120 217 VAQGPPEEVL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
15-242 |
1.24e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 158.71 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 15 QSGLLLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANghiSGSATFNGREIlNL 93
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLrLIAGLEKPT---SGEVLVDGKPV-TG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 PERDlnklraeqISMIFQDPmtSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGM 173
Cdd:COG1116 78 PGPD--------RGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---YPHQLSGGM 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-264 |
3.16e-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: 156.89 E-value: 3.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANghiSGSATFNGREILNLPERDL 98
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKS-TLLRLIvGLLRPD---SGEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAeQISMIFQDP--MTSLNpymrVGEQLMEVLMLHKGLSKAAaFEESVRM-LDAVKMPEARKRMkmfPHEFSGGMRQ 175
Cdd:cd03261 73 YRLRR-RMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEE-IREIVLEkLEAVGLRGAEDLY---PAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 505807353 256 VFyQPSHPY 264
Cdd:cd03261 224 LR-ASDDPL 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-242 |
4.14e-45 |
|
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: 153.40 E-value: 4.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANghiSGSATFNGREIlNLPERDl 98
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIaGLERPT---SGEVLVDGEPV-TGPGPD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 nklraeqISMIFQDPmtSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVM 178
Cdd:cd03293 75 -------RGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-272 |
6.28e-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: 154.58 E-value: 6.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKT-----PDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNL 93
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA---QGTVSFRGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 PERDLNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEarKRMKMFPHEFSGGM 173
Cdd:TIGR02769 79 DRKQRRAFRRD-VQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQA 253
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
250
....*....|....*....
gi 505807353 254 RDVFyQPSHPYSIGLLNAV 272
Cdd:TIGR02769 236 AQLL-SFKHPAGRNLQSAV 253
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-246 |
7.34e-45 |
|
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: 152.89 E-value: 7.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDL 98
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPT---SGEVLFNGQSLSKLSSNER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAEQISMIFQdpMTSLNPYMRVGEQLMeVLMLHKGLSKAAAFEESVRMLDAVKMpeaRKRMKMFPHEFSGGMRQRVM 178
Cdd:TIGR02211 78 AKLRNKKLGFIYQ--FHHLLPDFTALENVA-MPLLIGKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQ 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-262 |
1.62e-44 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 153.41 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDG-----DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREilnL 93
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT---SGELLIDDHP---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 PERDLnKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMpeARKRMKMFPHEFSGGM 173
Cdd:PRK15112 78 HFGDY-SYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL--LPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQA 253
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
....*....
gi 505807353 254 RDVFYQPSH 262
Cdd:PRK15112 235 ADVLASPLH 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-246 |
3.41e-44 |
|
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: 149.47 E-value: 3.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPErdln 99
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD---SGEIKVLGKDIKKEPE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRaEQISMIFQDPmtSLNPYMRVGEQLmevlmlhkglskaaafeesvrmldavkmpearkrmkmfphEFSGGMRQRVMI 179
Cdd:cd03230 70 EVK-RRIGYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-263 |
1.76e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 149.76 E-value: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANghiSGSATFNGREIlNLPERD 97
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLrCINLLEEPD---SGTITVDGEDL-TDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAEqISMIFQdpmtSLN--PYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEarkRMKMFPHEFSGGMRQ 175
Cdd:COG1126 72 INKLRRK-VGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMT-MVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
....*...
gi 505807353 256 VFYQPSHP 263
Cdd:COG1126 223 FFENPQHE 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-257 |
1.97e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.85 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAangHISGSATFNGREIlnlperd 97
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP---PTSGTVRLFGKPP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 lnKLRAEQISMIFQdpMTSLNPY--MRVgeqlMEVLML----HKGL---SKAAAFEESVRMLDAVKMPE-ARKRMkmfpH 167
Cdd:COG1121 71 --RRARRRIGYVPQ--RAEVDWDfpITV----RDVVLMgrygRRGLfrrPSRADREAVDEALERVGLEDlADRPI----G 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMyAGRT 247
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGL 216
|
250
....*....|
gi 505807353 248 MEYGQARDVF 257
Cdd:COG1121 217 VAHGPPEEVL 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-246 |
2.80e-43 |
|
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: 147.33 E-value: 2.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREIlNLPERDLN 99
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP---DSGSILIDGEDL-TDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRaEQISMIFQDPmtSLNPYMRVGEQLMEVLmlhkglskaaafeesvrmldavkmpearkrmkmfphefSGGMRQRVMI 179
Cdd:cd03229 73 PLR-RRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
37-272 |
4.15e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 149.84 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 37 TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGREILNLPERDLNKLRAEqISMIFQDPMTS 116
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQ---GNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPE--ARKRmkmfPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsvLDKR----PPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQ--ARDVFyqpSHPYSIGLLNAV 272
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPvgDKLTF---SSPAGRVLQNAV 254
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
30-253 |
5.12e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.89 E-value: 5.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 30 KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQtafaLMGLLAANGHI-SGSATFNGREILNLPERDLNKLRaEQISM 108
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYGEERPtSGQVLVNGQDLSRLKRREIPYLR-RRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 109 IFQDpmTSLNPYMRVGEQLMEVLMLHkGLSKAAAFEESVRMLDAVKMpeaRKRMKMFPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:COG2884 84 VFQD--FRLLPDRTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQA 253
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-251 |
5.45e-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: 147.67 E-value: 5.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLN 99
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD---SGEILIDGRDVTGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 klraeqISMIFQDPmtSLNPYMRVGEQLmeVLMLHKGLSKAAAFEESVR-MLDAVKMPEARKRmkmFPHEFSGGMRQRVM 178
Cdd:cd03259 74 ------IGMVFQDY--ALFPHLTVAENI--AFGLKLRGVPKAEIRARVReLLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-263 |
5.97e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.49 E-value: 5.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 23 KDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLaaNGHISGSATFNGREILNLPERDLNKLR 102
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLL--ERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 103 aEQISMIFQ--DPMTSLNPYMRVGEQLmEVLMLHKGLSKAAAFEesvrMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIA 180
Cdd:PRK11153 82 -RQIGMIFQhfNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTE----LLELVGLSDKADR---YPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQP 260
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
...
gi 505807353 261 SHP 263
Cdd:PRK11153 233 KHP 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-197 |
9.66e-42 |
|
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: 142.40 E-value: 9.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDLNKlraeQISMIFQDPmtSLN 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP---TEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--QLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 119 PYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEARKR-MKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 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 |
1.68e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 142.57 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 21 DVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANghiSGSATFNGREILNLPERDLN 99
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPS---SGEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAeqismifqdpmtslnpYMrvgEQLMEVL-MLHKglskaaafeesvrmldavkmpeARKRMkmfpHEFSGGMRQRVM 178
Cdd:cd03214 73 RKIA----------------YV---PQALELLgLAHL----------------------ADRPF----NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-251 |
2.31e-41 |
|
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: 143.80 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILnlpeRDLN 99
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT---SGTAYINGYSIR----TDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAEqISMIFQDPMtsLNPYMRVgeqlMEVLMLH---KGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQR 176
Cdd:cd03263 72 AARQS-LGYCPQFDA--LFDELTV----REHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANK---RARTLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-256 |
4.41e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 143.66 E-value: 4.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANghiSGSATFNGREILNLPERD 97
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVEPT---SGEILVDGQDVTALRGRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAeQISMIFQDPmtSLNPYMRVgeqLMEVLM-------LHKGLS-------KAAAFEesvrMLDAVKMPE-ARKRm 162
Cdd:COG3638 75 LRRLRR-RIGMIFQQF--NLVPRLSV---LTNVLAgrlgrtsTWRSLLglfppedRERALE----ALERVGLADkAYQR- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 163 kmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:COG3638 144 ---ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGL 220
|
250
....*....|....
gi 505807353 243 YAGRTMEYGQARDV 256
Cdd:COG3638 221 RDGRVVFDGPPAEL 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-256 |
1.04e-40 |
|
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: 142.58 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANghiSGSATFNGREILNLPERDL 98
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFnLISGFLRPT---SGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKL---RAEQISMIFQDpMTSL-NpyMRVGEQLME---VLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSG 171
Cdd:cd03219 73 ARLgigRTFQIPRLFPE-LTVLeN--VMVAAQARTgsgLLLARARREEREARERAEELLERVGLADLADRP---AGELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
....*
gi 505807353 252 QARDV 256
Cdd:cd03219 226 TPDEV 230
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
27-273 |
1.67e-40 |
|
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: 142.95 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNlpERDLNKLRaEQI 106
Cdd:TIGR04520 6 VSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPT---SGKVTVDGLDTLD--EENLWEIR-KKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQDPMTSLnpymrVGEQL-------MEVLMLhkglskaaAFEESVR----MLDAVKMPEARKRMkmfPHEFSGGMRQ 175
Cdd:TIGR04520 80 GMVFQNPDNQF-----VGATVeddvafgLENLGV--------PREEMRKrvdeALKLVGMEDFRDRE---PHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGQARD 255
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPRE 222
|
250
....*....|....*...
gi 505807353 256 VFYQPSHPYSIGLlnAVP 273
Cdd:TIGR04520 223 IFSQVELLKEIGL--DVP 238
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-256 |
3.13e-40 |
|
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: 141.53 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREilnlPERDL 98
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD---SGSILIDGED----VRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRaEQISMIFQDPMtsLNPYMRVGEQLMEVLMLHkGLSKAAAFEESVRMLDAVKMPEARKRmKMfpHEFSGGMRQRVM 178
Cdd:COG4555 70 REAR-RQIGVLPDERG--LYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDR-RV--GELSTGMKKKVA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-327 |
1.74e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.21 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIL-NLPERDL 98
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD---SGRIVLNGRDLFtNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NklraeqISMIFQDPMtsLNPYMRVGEQL---MEVlmlhKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQ 175
Cdd:COG1118 76 R------VGFVFQHYA--LFPHMTVAENIafgLRV----RPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 256 VFYQPSHPYSIGLLNAVPRLDGE-GDSLLTIPGnppnlLRLPKGCPFQPRC------PHAMEICnSAPPLESFAPGRLR 327
Cdd:COG1118 221 VYDRPATPFVARFLGCVNVLRGRvIGGQLEADG-----LTLPVAEPLPDGPavagvrPHDIEVS-REPEGENTFPATVA 293
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
34-261 |
1.83e-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: 139.29 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPErdlNKlraEQISMIFQDp 113
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT---SGEILLDGKDITNLPP---HK---RPVNTVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mTSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:cd03300 81 -YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRK---PSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPS 261
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-242 |
1.86e-39 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 138.44 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAAnghISGSATFNGREILNLPERdlnk 100
Cdd:cd03235 2 VEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLKP---TSGSIRVFGKPLEKERKR---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 101 lraeqISMIFQdpMTSLNPYM--RVGEQLMEVLMLHKGLSK---AAAFEESVRMLDAVKMPE-ARKRMKmfphEFSGGMR 174
Cdd:cd03235 70 -----IGYVPQ--RRSIDRDFpiSVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLSElADRQIG----ELSGGQQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-287 |
2.16e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 140.63 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREilnLPERDLN 99
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEP---LDPEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KL------RaeqismifqdpmtSLNPYMRVGEQLMEVLMLHkGLSKAAAFEESVRMLDAVKMPEARKRmKMfpHEFSGGM 173
Cdd:COG4152 72 RIgylpeeR-------------GLYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANK-KV--EELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 174 RQRVMIAMALLCRPKLLIADEPTTALD-VTVQAqIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG- 251
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGs 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 505807353 252 --QARDVFyqPSHPYSIgllnavpRLDGEGDSLLTIPG 287
Cdd:COG4152 213 vdEIRRQF--GRNTLRL-------EADGDAGWLRALPG 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-246 |
3.29e-39 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 136.36 E-value: 3.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLNKlraeQI 106
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT---SGEILIDGVDLRDLDLESLRK----NI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQDPmtslnpymrvgeqlmeVLmlhkglskaaaFEESVRmldavkmpearkrmkmfphE--FSGGMRQRVMIAMALL 184
Cdd:cd03228 79 AYVPQDP----------------FL-----------FSGTIR-------------------EniLSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-256 |
3.65e-39 |
|
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: 138.47 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKtpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLN 99
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAeQISMIFQDPmtSLNPYMRVGEQlmeVLM--------------LHKGLSKAAAFEesvrMLDAVKMPE-ARKRMKm 164
Cdd:cd03256 75 QLRR-QIGMIFQQF--NLIERLSVLEN---VLSgrlgrrstwrslfgLFPKEEKQRALA----ALERVGLLDkAYQRAD- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 165 fphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 244
Cdd:cd03256 144 ---QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
250
....*....|..
gi 505807353 245 GRTMEYGQARDV 256
Cdd:cd03256 221 GRIVFDGPPAEL 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-246 |
1.04e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.68 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPerdlNKL 101
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDIAKLP----LEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 102 RAEQISMIFQdpmtslnpymrvgeqlmevlmlhkglskaaafeesvrmldavkmpearkrmkmfpheFSGGMRQRVMIAM 181
Cdd:cd00267 71 LRRRIGYVPQ---------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-246 |
1.73e-37 |
|
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: 133.65 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILnlpeRDLN 99
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT---SGRATVAGHDVV----REPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRaEQISMIFQDPmtSLNPYMrVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKmfpHEFSGGMRQRVMI 179
Cdd:cd03265 70 EVR-RRIGIVFQDL--SVDDEL-TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLV---KTYSGGMRRRLEI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-246 |
6.43e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.86 E-value: 6.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPerdLN 99
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT---SGEIYLDGKPLSAMP---PP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAeQISMIFQDPmtSLnPYMRVGEQLMEVLMLHKglsKAAAFEESVRMLDAVKMPEA--RKRMkmfpHEFSGGMRQRV 177
Cdd:COG4619 71 EWRR-QVAYVPQEP--AL-WGGTVRDNLPFPFQLRE---RKFDRERALELLERLGLPPDilDKPV----ERLSGGERQRL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-246 |
6.50e-37 |
|
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: 131.88 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlNLPERDLN 99
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD---SGTIIIDGLKL-TDDKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAEqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEarkRMKMFPHEFSGGMRQRVMI 179
Cdd:cd03262 73 ELRQK-VGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-256 |
8.22e-37 |
|
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: 131.92 E-value: 8.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQT--AFALMGLLAANGHISGSATFNGREILNLPErD 97
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLlrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDV-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHkGLSKAAAFEESVR-MLDAVKMPEARKRmKMFPHEFSGGMRQ 175
Cdd:cd03260 76 VLELRR-RVGMVFQKP----NPFpGSIYDNVAYGLRLH-GIKLKEELDERVEeALRKAALWDEVKD-RLHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 505807353 256 V 256
Cdd:cd03260 227 I 227
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
40-246 |
1.19e-36 |
|
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: 131.29 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 40 NDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGhiSGSATFNGREILNLPERDLNKLRaEQISMIFQDpmTSLNP 119
Cdd:TIGR02982 22 FDINLEINPGEIVILTGPSGSGKT-TLLTLIGGLRSVQ--EGSLKVLGQELHGASKKQLVQLR-RRIGYIFQA--HNLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 120 YMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMpeaRKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:TIGR02982 96 FLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505807353 200 DVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGR 246
Cdd:TIGR02982 173 DSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGK 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-264 |
1.32e-36 |
|
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: 132.77 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLaaNGHI---SGSATFNGREILNLPERDLNKLRAEQISMIF 110
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCI--NRLIeptSGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 111 QDpmTSLNPYMRVGEQL---MEVlmlhKGLSKAAAFEESVRMLDAVKMpEARKrmKMFPHEFSGGMRQRVMIAMALLCRP 187
Cdd:cd03294 109 QS--FALLPHRTVLENVafgLEV----QGVPRAEREERAAEALELVGL-EGWE--HKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 188 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPY 264
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-251 |
1.64e-36 |
|
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: 130.86 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLN 99
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD---SGEVLFDGKPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAEQismifqdpmtSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPE-ARKRMKmfphEFSGGMRQRVM 178
Cdd:cd03269 74 YLPEER----------GLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
34-240 |
1.11e-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: 128.50 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLaaNGHISGSATFNGREILNLPERDLNKLRAEQISMIFQDp 113
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLL--EKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQN- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mTSLNPYMRVGEQLMEVLMLHKgLSKAAAFEESVRMLDAVKMpeaRKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:TIGR03608 85 -FALIENETVEENLDLGLKYKK-LSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505807353 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 ... |
41-261 |
2.35e-35 |
|
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: 128.61 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLLaanGHISGSATFNGREILNL-PERdlnklraEQISMIFQDpmTSLNP 119
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFI---KPDSGKILLNGKDITNLpPEK-------RDISYVPQN--YALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 120 YMRVGEQLmEVLMLHKGLSKAaafEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:cd03299 85 HMTVYKNI-AYGLKKRKVDKK---EIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 200 DVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPS 261
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
34-261 |
2.35e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.59 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL--AANG--HISGSaTFNGREILNlpERDLNKLRaEQISMI 109
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDSGqlNIAGH-QFDFSQKPS--EKAIRLLR-QKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 110 FQDpmTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:COG4161 88 FQQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGQArDVFYQPS 261
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
34-246 |
7.47e-35 |
|
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: 129.05 E-value: 7.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPErdlnKLRaEQISMIFQDP 113
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPT---SGTARVAGYDVVREPR----KVR-RSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mtslnpymRVGEQL--MEVLMLHK---GLSKAAAFEESVRMLDAVKMPEARKRMKmfpHEFSGGMRQRVMIAMALLCRPK 188
Cdd:TIGR01188 76 --------SVDEDLtgRENLEMMGrlyGLPKDEAEERAEELLELFELGEAADRPV---GTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGR 201
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
26-251 |
9.86e-35 |
|
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: 134.19 E-value: 9.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLperDLNKLRaEQ 105
Cdd:COG2274 478 NVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT---SGRILIDGIDLRQI---DPASLR-RQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDPM----------TSLNPYMRVgEQLMEVLmlhkglsKAAAFEESVRmldavKMPearKRMKMFPHE----FSG 171
Cdd:COG2274 551 IGVVLQDVFlfsgtireniTLGDPDATD-EEIIEAA-------RLAGLHDFIE-----ALP---MGYDTVVGEggsnLSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYG 251
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-256 |
1.01e-34 |
|
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: 127.03 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDL 98
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS---SGSILLEGTDITKLRGKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAeQISMIFQD-----PMTSL-NPYM-RVGEQLMEVLMLhkGLSKAAAFEESVRMLDAVKMPE-ARKRMKmfphEFS 170
Cdd:TIGR02315 75 RKLRR-RIGMIFQHynlieRLTVLeNVLHgRLGYKPTWRSLL--GRFSEEDKERALSALERVGLADkAYQRAD----QLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
....*.
gi 505807353 251 GQARDV 256
Cdd:TIGR02315 228 GAPSEL 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-246 |
1.63e-34 |
|
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: 126.01 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFK--TPDG-DVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAAN-----GHISGSATFNGREI 90
Cdd:COG4778 4 LLEVENLSKTFTlhLQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIYGNylpdsGSILVRHDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 91 LNLPERDLNKLRAEQISMIFQdpmtSLNPYMRVG--EQLMEVLmLHKGLSKAAAFEESVRMLDAVKMPEARKRMkmFPHE 168
Cdd:COG4778 80 AQASPREILALRRRTIGYVSQ----FLRVIPRVSalDVVAEPL-LERGVDREEARARARELLARLNLPERLWDL--PPAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
34-260 |
4.32e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 125.13 E-value: 4.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL--AANG--HISGSAtFNGREILNlpERDLNKLRaEQISMI 109
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRSGtlNIAGNH-FDFSKTPS--DKAIRELR-RNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 110 FQDpmTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK11124 88 FQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGQArDVFYQP 260
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQP 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-251 |
4.55e-34 |
|
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: 131.42 E-value: 4.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 7 TKAPQAAQQSGLLLDVKDLRVTFktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFN 86
Cdd:COG4988 324 AGTAPLPAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY---SGSILIN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 87 GREILNLPERDLNKlraeQISMIFQDPM---TSL--NpyMRVG------EQLMEVLmlhkglsKAAAFEESVRML----D 151
Cdd:COG4988 398 GVDLSDLDPASWRR----QIAWVPQNPYlfaGTIreN--LRLGrpdasdEELEAAL-------EAAGLDEFVAALpdglD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 152 AVKMPEARKrmkmfpheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGV 231
Cdd:COG4988 465 TPLGEGGRG--------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL 534
|
250 260
....*....|....*....|
gi 505807353 232 VAgICDKVLVMYAGRTMEYG 251
Cdd:COG4988 535 LA-QADRILVLDDGRIVEQG 553
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-268 |
5.65e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 5.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLrvTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREilnLPERDL 98
Cdd:PRK13635 5 IIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE---AGTITVGGMV---LSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRaEQISMIFQDPMTSLnpymrVGEQLMEVLML---HKGLSKaaafEESV-RMLDAVKmpeaRKRMKMF----PHEFS 170
Cdd:PRK13635 77 WDVR-RQVGMVFQNPDNQF-----VGATVQDDVAFgleNIGVPR----EEMVeRVDQALR----QVGMEDFlnrePHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
250
....*....|....*...
gi 505807353 251 GQARDVFYQPSHPYSIGL 268
Cdd:PRK13635 222 GTPEEIFKSGHMLQEIGL 239
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
19-263 |
7.51e-34 |
|
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: 127.31 E-value: 7.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGhiSGSATFNGREILNLPERDL 98
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERPT--SGSVIVDGQDLTTLSNSEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRaEQISMIFQ--DPMTSLNPYMRVGEQLmEVlmlhKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQR 176
Cdd:TIGR02314 78 TKAR-RQIGMIFQhfNLLSSRTVFGNVALPL-EL----DNTPKDEIKRKVTELLALVGLGDKHDS---YPSNLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:TIGR02314 149 VAIARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEI 228
|
....*..
gi 505807353 257 FYQPSHP 263
Cdd:TIGR02314 229 FSHPKTP 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-255 |
1.04e-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: 130.27 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 11 QAAQQSGLLLDVKDlrVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREI 90
Cdd:COG4987 325 PAPAPGGPSLELED--VSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ---SGSITLGGVDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 91 LNLPERDLnklrAEQISMIFQDP---MTSL--NpyMRVG------EQLMEVLmlhkglsKAAAFEESVRM----LDAVkM 155
Cdd:COG4987 400 RDLDEDDL----RRRIAVVPQRPhlfDTTLreN--LRLArpdatdEELWAAL-------ERVGLGDWLAAlpdgLDTW-L 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 156 PEARKRmkmfpheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLgVVAGI 235
Cdd:COG4987 466 GEGGRR-------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLER 535
|
250 260
....*....|....*....|
gi 505807353 236 CDKVLVMYAGRTMEYGQARD 255
Cdd:COG4987 536 MDRILVLEDGRIVEQGTHEE 555
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
26-264 |
3.08e-33 |
|
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: 123.18 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFKTPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangHISGSATFNGREILnlpERDLNKLRaEQ 105
Cdd:cd03295 5 NVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE---PTSGEIFIDGEDIR---EQDPVELR-RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEArKRMKMFPHEFSGGMRQRVMIAMALLC 185
Cdd:cd03295 77 IGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPA-EFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPY 264
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
34-275 |
1.33e-32 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 121.45 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDlnklraEQISMIFQDp 113
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPD---SGRIRLNGQDATRVHARD------RKIGFVFQH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mTSLNPYMRVGEQL---MEVLMLHKGLSKAAAFEesvrMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:TIGR00968 81 -YALFKHLTVRDNIafgLEIRKHPKAKIKARVEE----LLELVQLEGLGDR---YPNQLSGGQRQRVALARALAVEPQVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 191 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGLLN 270
Cdd:TIGR00968 153 LLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
....*
gi 505807353 271 AVPRL 275
Cdd:TIGR00968 233 EVNVL 237
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-246 |
2.19e-32 |
|
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: 119.07 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTfktpdgdvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDL 98
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA---SGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRaeqISMIFQDPM-TSLNPYMRVGEQLMevlmlhkglskaaafeesvrmldavkmpearkrmkmFPHEFSGGMRQRV 177
Cdd:cd03215 73 IRAG---IAYVPEDRKrEGLVLDLSVAENIA------------------------------------LSSLLSGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-251 |
2.87e-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: 119.71 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 43 NFNLRA-----GETLGIVGESGSGKSQTAFALMGLLAA-NGHIS--GSATFNGREILNLPERDlnklraEQISMIFQDpm 114
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPdGGTIVlnGTVLFDSRKKINLPPQQ------RKIGLVFQQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 115 TSLNPYMRVGEQLMEVLMLHKGLSKAAAFEEsvrMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRNREDRISVDE---LLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 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 |
3.98e-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: 119.28 E-value: 3.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLL-AANGHISGSATFNGREILNLPERDLNKLRaEQ 105
Cdd:TIGR02673 7 VSKAYP-GGVAALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLyGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDpmTSLNPYMRVGEQL---MEVLmlhkGLSKAAAFEESVRMLDAVKMPEarkRMKMFPHEFSGGMRQRVMIAMA 182
Cdd:TIGR02673 81 IGVVFQD--FRLLPDRTVYENValpLEVR----GKKEREIQRRVGAALRQVGLEH---KADAFPEQLSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807353 183 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-269 |
6.31e-32 |
|
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: 119.37 E-value: 6.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDlnkl 101
Cdd:cd03296 5 VRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD---SGTILFGGEDATDVPVQE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 102 raEQISMIFQDpmTSLNPYMRVGEQL---MEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVM 178
Cdd:cd03296 74 --RNVGFVFQH--YALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFY 258
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 505807353 259 QPSHPYSIGLL 269
Cdd:cd03296 227 HPASPFVYSFL 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-263 |
8.61e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.76 E-value: 8.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 6 MTKAPQAAQQSgllLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqT---AFALMGLLAANGHISGS 82
Cdd:COG1117 1 MTAPASTLEPK---IEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKS-TllrCLNRMNDLIPGARVEGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 83 ATFNGREILNlPERDLNKLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGLSKA---AAFEESVRML---DAVKm 155
Cdd:COG1117 73 ILLDGEDIYD-PDVDVVELRR-RVGMVFQKP----NPFpKSIYDNVAYGLRLHGIKSKSeldEIVEESLRKAalwDEVK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 156 pearKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGI 235
Cdd:COG1117 146 ----DRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARV 219
|
250 260
....*....|....*....|....*...
gi 505807353 236 CDKVLVMYAGRTMEYGQARDVFYQPSHP 263
Cdd:COG1117 220 SDYTAFFYLGELVEFGPTEQIFTNPKDK 247
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
16-260 |
2.11e-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: 120.98 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 16 SGLLLDVK------DLRVTFKTPDGDVTAvndlnfnlragetlgIVGESGSGKSQTAFALMGLL-AANGHIS--GSATFN 86
Cdd:COG4148 1 MMLEVDFRlrrggfTLDVDFTLPGRGVTA---------------LFGPSGSGKTTLLRAIAGLErPDSGRIRlgGEVLQD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 87 GREILNLPerdlnklrAEQ--ISMIFQDPmtSLNPYMRVGEQLMevlmlhKGLSKAAAFEESVRMLDAVKMPEARKRMKM 164
Cdd:COG4148 66 SARGIFLP--------PHRrrIGYVFQEA--RLFPHLSVRGNLL------YGRKRAPRAERRISFDEVVELLGIGHLLDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 165 FPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 244
Cdd:COG4148 130 RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ 209
|
250
....*....|....*.
gi 505807353 245 GRTMEYGQARDVFYQP 260
Cdd:COG4148 210 GRVVASGPLAEVLSRP 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-262 |
3.34e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.09 E-value: 3.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGL--LAANGHISGSATFNGREILNLPERD 97
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKlraeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVR-MLDAVKM-PEARKRMKMFPHEFSGGMRQ 175
Cdd:PRK14247 80 LRR----RVQMVFQIP--NPIPNLSIFENVALGLKLNRLVKSKKELQERVRwALEKAQLwDEVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....*..
gi 505807353 256 VFYQPSH 262
Cdd:PRK14247 232 VFTNPRH 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-262 |
1.93e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.03 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGHISGSATFNGREILNlPER 96
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYS-PRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 97 DLNKLRAEqISMIFQDPmtslNPY-MRVGEQLMEVLMLhKGLSKAAAFEESVR--MLDAVKMPEARKRMKMFPHEFSGGM 173
Cdd:PRK14239 80 DTVDLRKE-IGMVFQQP----NPFpMSIYENVVYGLRL-KGIKDKQVLDEAVEksLKGASIWDEVKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQA 253
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
....*....
gi 505807353 254 RDVFYQPSH 262
Cdd:PRK14239 232 KQMFMNPKH 240
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-264 |
2.38e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.87 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLP--ERD 97
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT---SGEILIGGRDVTDLPpkDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 lnklraeqISMIFQDPmtSLNPYMRVGEQL---MEVlmlhKGLSKAAAfEESVR-MLDAVKMPE--ARKrmkmfPHEFSG 171
Cdd:COG3839 77 --------IAMVFQSY--ALYPHMTVYENIafpLKL----RKVPKAEI-DRRVReAAELLGLEDllDRK-----PKQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD------LGvvagicDKVLVMYAG 245
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDG 210
|
250
....*....|....*....
gi 505807353 246 RTMEYGQARDVFYQPSHPY 264
Cdd:COG3839 211 RIQQVGTPEELYDRPANLF 229
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
249-331 |
2.81e-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: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 249 EYGQARDVFYQPSHPYSIGLLNAVPRLDGEGDSLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNS-APPLESFAPGRLR 327
Cdd:TIGR01727 4 ETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKePPALVEIAEGHRV 83
|
....
gi 505807353 328 ACFK 331
Cdd:TIGR01727 84 ACHL 87
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-251 |
2.83e-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: 114.51 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHIsgsaTFNGREILNLPerdLNKLRaEQ 105
Cdd:cd03244 8 VSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSI----LIDGVDISKIG---LHDLR-SR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDPMT-------SLNPYMRVG-EQLMEVLmlhkglskaaafeESVRMLDAVKMPEARKRMKMfpHE----FSGGM 173
Cdd:cd03244 80 ISIIPQDPVLfsgtirsNLDPFGEYSdEELWQAL-------------ERVGLKEFVESLPGGLDTVV--EEggenLSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE---AFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
34-264 |
3.43e-30 |
|
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: 117.45 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLP--ERDLnklraeqiSMIFQ 111
Cdd:TIGR03265 15 GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT---AGTIYQGGRDITRLPpqKRDY--------GIVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 112 DpmTSLNPYMRVgEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKLLI 191
Cdd:TIGR03265 84 S--YALFPNLTV-ADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 192 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPY 264
Cdd:TIGR03265 158 LDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPF 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
38-275 |
3.49e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.30 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNlPERDLNKLRaEQISMIFQDPmtsl 117
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT---SGKIIIDGVDITD-KKVKLSDIR-KKVGLVFQYP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 118 nPYmrvgeQLMEVLM--------LHKGLSKAAAFEESVRMLDAVKMP-EARKRMKmfPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK13637 93 -EY-----QLFEETIekdiafgpINLGLSEEEIENRVKRAMNIVGLDyEDYKDKS--PFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGL 268
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIGL 244
|
....*..
gi 505807353 269 lnAVPRL 275
Cdd:PRK13637 245 --AVPQV 249
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-268 |
3.87e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.98 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLrvTFK-TPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREilnLPERD 97
Cdd:PRK13650 4 IIEVKNL--TFKyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGQIIIDGDL---LTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRaEQISMIFQDPMTSLnpymrVG---EQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGGMR 174
Cdd:PRK13650 76 VWDIR-HKIGMVFQNPDNQF-----VGatvEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKERE---PARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGQAR 254
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPR 225
|
250
....*....|....
gi 505807353 255 DVFYQPSHPYSIGL 268
Cdd:PRK13650 226 ELFSRGNDLLQLGL 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-246 |
3.91e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.74 E-value: 3.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTfktpdgdvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILN------ 92
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA---DSGEIRLDGKPVRIrsprda 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 93 -------LPErDlnklRAEQ-----------ISMifqdpmTSLNPYMRVGeqlmevlMLHKGLSKAAAfEESVRMLDaVK 154
Cdd:COG1129 325 iragiayVPE-D----RKGEglvldlsirenITL------ASLDRLSRGG-------LLDRRRERALA-EEYIKRLR-IK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 155 MPEARKRMKmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAG 234
Cdd:COG1129 385 TPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLG 459
|
250
....*....|..
gi 505807353 235 ICDKVLVMYAGR 246
Cdd:COG1129 460 LSDRILVMREGR 471
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-256 |
3.93e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.75 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 4 IEMTKAPQAAQQSGLLLDVKDLRVTfktPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSA 83
Cdd:COG3845 242 VLLRVEKAPAEPGEVVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA---SGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 84 TFNGREILNLPERdlnKLRAEQISMIFQDPM-TSLNPYMRVGEQLmeVLMLHKG--------LSKAAAFEESVRMLDA-- 152
Cdd:COG3845 316 RLDGEDITGLSPR---ERRRLGVAYIPEDRLgRGLVPDMSVAENL--ILGRYRRppfsrggfLDRKAIRAFAEELIEEfd 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 153 VKMPEARKRMKMfpheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVV 232
Cdd:COG3845 391 VRTPGPDTPARS----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEI 465
|
250 260
....*....|....*....|....
gi 505807353 233 AGICDKVLVMYAGRTMEYGQARDV 256
Cdd:COG3845 466 LALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
34-251 |
1.06e-29 |
|
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: 112.73 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLNklraeqISMIFQDp 113
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT---SGRIYIGGRDVTDLPPKDRD------IAMVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mTSLNPYMRVGEQLMEVLMLHKglSKAAAFEESVRmlDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:cd03301 81 -YALYPHMTVYDNIAFGLKLRK--VPKDEIDERVR--EVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-251 |
3.60e-29 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 111.15 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNlperdlN 99
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSYQK------N 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAEQISMIFQDPmtSLNPYMRVGEQLmEVLMLHKGLSKAAAFEesvrMLDAVKMPE-ARKRMKmfphEFSGGMRQRVM 178
Cdd:cd03268 68 IEALRRIGALIEAP--GFYPNLTARENL-RLLARLLGIRKKRIDE----VLDVVGLKDsAKKKVK----GFSLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-245 |
4.25e-29 |
|
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: 111.19 E-value: 4.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFKTPDGdVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGReilNLPERDlnklRAEQ 105
Cdd:cd03226 4 NISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES---SGSILLNGK---PIKAKE----RRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDPMTSLnpYMR-VGEQLMEVLM-LHKGLSKAaafEESVRMLDAVKMPEARkrmkmfPHEFSGGMRQRVMIAMAL 183
Cdd:cd03226 73 IGYVMQDVDYQL--FTDsVREELLLGLKeLDAGNEQA---ETVLKDLDLYALKERH------PLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-251 |
7.73e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.42 E-value: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFkTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFAL-MGLLAANghiSGSATFNGReilNLPERDLNKLRaEQ 105
Cdd:COG1132 345 VSF-SYPGDRPVLKDISLTIPPGETVALVGPSGSGKS-TLVNLlLRFYDPT---SGRILIDGV---DIRDLTLESLR-RQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDPM---TSL--NpyMRVG------EQLMEVLmlhkglsKAAAFEESVRML----DAVKMPEARKrmkmfpheFS 170
Cdd:COG1132 416 IGVVPQDTFlfsGTIreN--IRYGrpdatdEEVEEAA-------KAAQAHEFIEALpdgyDTVVGERGVN--------LS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
.
gi 505807353 251 G 251
Cdd:COG1132 556 G 556
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-228 |
1.06e-28 |
|
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: 109.88 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANghiSGSATFNGREILNLPERd 97
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKT-TLLrILAGLLPPS---AGEVLWNGEPIRDARED- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 lnklRAEQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKGLSKAAAFEEsvrMLDAVKMPEARKRmkmFPHEFSGGMRQRV 177
Cdd:COG4133 73 ----YRRRLAYLGHADG--LKPELTVRENLRFWAALYGLRADREAIDE---ALEAVGLAGLADL---PVRQLSAGQKRRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 228
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
34-263 |
1.13e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGHISGSATFNGREILNLPERDLNKLRAEQiSMIFQDp 113
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEA-GMVFQQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEarkRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:PRK09493 86 -FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 194 EPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHP 263
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-264 |
2.83e-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: 112.51 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHIS--GSATFNGREILNLP-ERdlnklRAeqISMIFQDpmTS 116
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVlnGRTLFDSRKGIFLPpEK-----RR--IGYVFQE--AR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARkrmkmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRL------PGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPY 264
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-268 |
2.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.05 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGreiLNLPERDLNKLRaEQI 106
Cdd:PRK13640 11 VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDG---ITLTAKTVWDIR-EKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQDPMTSLnpymrVGEQLMEVLML---HKGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGGMRQRVMIAMAL 183
Cdd:PRK13640 87 GIVFQNPDNQF-----VGATVGDDVAFgleNRAVPRPEMIKIVRDVLADVGMLDYIDSE---PANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGQARDVFYQPSHP 263
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
....*
gi 505807353 264 YSIGL 268
Cdd:PRK13640 238 KEIGL 242
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
19-242 |
3.45e-28 |
|
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: 109.02 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPD-GDV--TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMG-LLAANGHISGSATFNGREILNLP 94
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQqGGVrlPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnYLPDSGRILVRHEGAWVDLAQAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 95 ERDLNKLRAEQISMIFQdpmtslnpYMRVGEQL--MEVLM---LHKGLSKAAAFEESVRMLDAVKMPEarKRMKMFPHEF 169
Cdd:TIGR02324 81 PREVLEVRRKTIGYVSQ--------FLRVIPRVsaLEVVAeplLERGVPREAARARARELLARLNIPE--RLWHLPPATF 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:TIGR02324 151 SGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-251 |
3.69e-28 |
|
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: 108.99 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPerdl 98
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD---AGFATVDGFDVVKEP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 nklRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLH--KGLSKAAAFEESVRMLDavkMPEARKRMKmfpHEFSGGMRQR 176
Cdd:cd03266 74 ---AEARRRLGFVSDSTGLYDRLTARENLEYFAGLYglKGDELTARLEELADRLG---MEELLDRRV---GGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-263 |
3.94e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.06 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGHisGSATFNGREILNLPERD-- 97
Cdd:PRK10619 6 LNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPSE--GSIVVNGQTINLVRDKDgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 --------LNKLRAeQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEaRKRMKmFPHEF 169
Cdd:PRK10619 79 lkvadknqLRLLRT-RLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE-RAQGK-YPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250
....*....|....
gi 505807353 250 YGQARDVFYQPSHP 263
Cdd:PRK10619 233 EGAPEQLFGNPQSP 246
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-247 |
4.25e-28 |
|
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: 107.13 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLN 99
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD---SGEILVDGKEVSFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRaeqISMIFQdpmtslnpymrvgeqlmevlmlhkglskaaafeesvrmldavkmpearkrmkmfpheFSGGMRQRVMI 179
Cdd:cd03216 74 RAG---IAMVYQ---------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-268 |
4.48e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHIsgsaTFNGREILNlpeRDLNKLRaEQ 105
Cdd:PRK13648 13 VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEI----FYNNQAITD---DNFEKLR-KH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDPMTSLnpymrVGEQL-MEVLMlhkGL-SKAAAFEESVRmldavKMPEARKRMKMF------PHEFSGGMRQRV 177
Cdd:PRK13648 85 IGIVFQNPDNQF-----VGSIVkYDVAF---GLeNHAVPYDEMHR-----RVSEALKQVDMLeradyePNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGQARDVF 257
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
250
....*....|.
gi 505807353 258 YQPSHPYSIGL 268
Cdd:PRK13648 231 DHAEELTRIGL 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-260 |
5.68e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.78 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRvtFKTPDGDVtAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlNLPERDL 98
Cdd:PRK13639 1 ILETRDLK--YSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT---SGEVLIKGEPI-KYDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRaEQISMIFQDPMTSLnpYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGGMRQRVM 178
Cdd:PRK13639 74 LEVR-KTVGIVFQNPDDQL--FAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFY 258
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
..
gi 505807353 259 QP 260
Cdd:PRK13639 227 DI 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-263 |
7.22e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.07 E-value: 7.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL--AANGHIS-GSATFNGREILNLPER 96
Cdd:PRK11264 4 IEVKNLVKKFH----GQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRvGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 97 DLNKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQR 176
Cdd:PRK11264 79 LIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS---YPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
....*..
gi 505807353 257 FYQPSHP 263
Cdd:PRK11264 232 FADPQQP 238
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
248-312 |
7.39e-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: 103.25 E-value: 7.39e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 248 MEYGQARDVFYQPSHPYSIGLLNAVPRLDGEGDSLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC 312
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-256 |
9.70e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 9.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGHI---SGSATFNGREIlnlpe 95
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKS-T---LMKILS--GVYqpdSGEILLDGEPV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 RDLNKLRAEQ--ISMIFQDPmtSLNPYMRVGEQL-MEVLMLHKGL-SKAAAFEESVRMLDAVKMPE-ARKRMKmfphEFS 170
Cdd:COG1129 69 RFRSPRDAQAagIAIIHQEL--NLVPNLSVAENIfLGREPRRGGLiDWRAMRRRARELLARLGLDIdPDTPVG----DLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
....*.
gi 505807353 251 GQARDV 256
Cdd:COG1129 222 GPVAEL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-246 |
1.00e-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: 107.49 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 30 KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGH-ISGSATFNGREILNLPERDLNKLRaEQISM 108
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELpTSGTIRVNGQDVSDLRGRAIPYLR-RKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 109 IFQDP--MTSLNPYMRVGEQLMEVLMLHKGLSKaaafeesvRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCR 186
Cdd:cd03292 83 VFQDFrlLPDRNVYENVAFALEVTGVPPREIRK--------RVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 187 PKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-257 |
1.34e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.17 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLrvTFKTPDGdVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREIlNLPERDL 98
Cdd:PRK13636 5 ILKVEEL--NYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP---SSGRILFDGKPI-DYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRaEQISMIFQDP---MTSLNPYMRVGEQLMEVlmlhkGLSKAAAFEESVRMLDAVKMPEARKRMKmfpHEFSGGMRQ 175
Cdd:PRK13636 78 MKLR-ESVGMVFQDPdnqLFSASVYQDVSFGAVNL-----KLPEDEVRKRVDNALKRTGIEHLKDKPT---HCLSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
..
gi 505807353 256 VF 257
Cdd:PRK13636 229 VF 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-251 |
1.38e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.79 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 14 QQSGLLLDVKDL-RVTFKTpdgdVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREiln 92
Cdd:COG4586 16 KEPGLKGALKGLfRREYRE----VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPT---SGEVRVLGYV--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 93 lPERDLNKLrAEQISMIFqdpmtslnpymrvG--EQL------MEVLMLHK---GLSKAAaFEESVRMLdaVKMPE---- 157
Cdd:COG4586 86 -PFKRRKEF-ARRIGVVF-------------GqrSQLwwdlpaIDSFRLLKaiyRIPDAE-YKKRLDEL--VELLDlgel 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 158 ----ARK-----RMKMfphEfsggmrqrvmIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:COG4586 148 ldtpVRQlslgqRMRC---E----------LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
|
250 260
....*....|....*....|...
gi 505807353 229 LGVVAGICDKVLVMYAGRTMEYG 251
Cdd:COG4586 215 MDDIEALCDRVIVIDHGRIIYDG 237
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-257 |
1.78e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.89 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGHI---SGSATFNGREILNLPE 95
Cdd:COG4559 1 MLEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKS-T---LLKLLT--GELtpsSGEVRLNGRPLAAWSP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 RDLNKLRA---EQISMIFqdPMTSLnpymrvgeqlmEVLML--HKGLSKAAAFEESVR-MLDAVKMPEARKRMkmFPhEF 169
Cdd:COG4559 71 WELARRRAvlpQHSSLAF--PFTVE-----------EVVALgrAPHGSSAAQDRQIVReALALVGLAHLAGRS--YQ-TL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAMAlLC--------RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLV 241
Cdd:COG4559 135 SGGEQQRVQLARV-LAqlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILL 212
|
250
....*....|....*.
gi 505807353 242 MYAGRTMEYGQARDVF 257
Cdd:COG4559 213 LHQGRLVAQGTPEEVL 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-246 |
2.40e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFK--TPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGHI---SGSATFNGREILNLP 94
Cdd:COG1101 2 LELKNLSKTFNpgTVN-EKRALDGLNLTIEEGDFVTVIGSNGAGKS-T---LLNAIA--GSLppdSGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 95 ERDlnklRAEQISMIFQDPMTSLNPYMRVGEQLM------EVLMLHKGLSKA--AAFEESVRMLDavkMP-EARKRMKMf 165
Cdd:COG1101 75 EYK----RAKYIGRVFQDPMMGTAPSMTIEENLAlayrrgKRRGLRRGLTKKrrELFRELLATLG---LGlENRLDTKV- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 166 pHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH------DLGvvagicDKV 239
Cdd:COG1101 147 -GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeqalDYG------NRL 219
|
....*..
gi 505807353 240 LVMYAGR 246
Cdd:COG1101 220 IMMHEGR 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-228 |
2.81e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.64 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNlPERDln 99
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVPVTG-PGAD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 klRAeqisMIFQDpmTSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMI 179
Cdd:COG4525 78 --RG----VVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARR---RIWQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
49-249 |
3.97e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.40 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 49 GETLGIVGESGSGKSqtafALMGLLAA-NGHISGSATFNGREILNLPERDLNKLRAEQISMIFQDPMtsLNPYMRVGEQL 127
Cdd:PRK10584 36 GETIALIGESGSGKS----TLLAILAGlDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFM--LIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 128 mEVLMLHKGLSKAAAFEESVRMLDAVKMPearKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 207
Cdd:PRK10584 110 -ELPALLRGESSRQSRNGAKALLEQLGLG---KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505807353 208 MTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGRTME 249
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQLQE 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-246 |
4.81e-27 |
|
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: 105.74 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGeTLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPErdln 99
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS---SGTIRIDGQDVLKQPQ---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAeQISMIFQDPMTSlnPYMRVGEQL--MEVLmlhKGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGGMRQRV 177
Cdd:cd03264 69 KLRR-RIGYLPQEFGVY--PNFTVREFLdyIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKK---IGSLSGGMRRRV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-256 |
5.28e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 111.05 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 1 MSTIEMTKAPQAAQQSGLLLDVKDLRVTFKTPD-GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghi 79
Cdd:TIGR03269 261 MEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT--- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 80 SGSATFN-GREILNLPERD-LNKLRAEQ-ISMIFQDpmTSLNPYMRVGEQLMEVLMLHkgLSKAAAFEESVRMLDAVKMP 156
Cdd:TIGR03269 338 SGEVNVRvGDEWVDMTKPGpDGRGRAKRyIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFD 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 157 E--ARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAG 234
Cdd:TIGR03269 414 EekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLD 493
|
250 260
....*....|....*....|..
gi 505807353 235 ICDKVLVMYAGRTMEYGQARDV 256
Cdd:TIGR03269 494 VCDRAALMRDGKIVKIGDPEEI 515
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-228 |
5.42e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGREILNLPerdln 99
Cdd:COG4136 2 LSLENLTITL----GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTALP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 klrAEQ--ISMIFQDPMtsLNPYMRVGEQLMevLMLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRV 177
Cdd:COG4136 73 ---AEQrrIGILFQDDL--LFPHLSVGENLA--FALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-262 |
5.99e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.46 E-value: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAN--GHISGSATFNGREILNlPERD 97
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeeARVEGEVRLFGRNIYS-PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRaEQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVR--MLDAVKMPEARKRMKMFPHEFSGGMRQ 175
Cdd:PRK14267 80 PIEVR-REVGMVFQYP--NPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwaLKKAALWDEVKDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
....*..
gi 505807353 256 VFYQPSH 262
Cdd:PRK14267 235 VFENPEH 241
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-278 |
9.00e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.25 E-value: 9.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLlaaNGHISGSATFNGREILNLPERDlnklraEQISMIFQDp 113
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL---EHQTSGHIRFHGTDVSRLHARD------RKVGFVFQH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mTSLNPYMRVGEQL---MEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK10851 83 -YALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 191 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGLLN 270
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
....*...
gi 505807353 271 AVPRLDGE 278
Cdd:PRK10851 239 EVNRLQGT 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-268 |
9.17e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.72 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangHISGSATFNGREilnLPERDL 98
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE---EFEGKVKIDGEL---LTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRaEQISMIFQDPMTSLnpymrVGEQLMEVL---MLHKGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGGMRQ 175
Cdd:PRK13642 77 WNLR-RKIGMVFQNPDNQF-----VGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGQARD 255
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE 226
|
250
....*....|...
gi 505807353 256 VFYQPSHPYSIGL 268
Cdd:PRK13642 227 LFATSEDMVEIGL 239
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-251 |
1.35e-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: 105.00 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGdVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLperDLNKLRaEQI 106
Cdd:cd03253 6 VTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS---SGSILIDGQDIREV---TLDSLR-RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQDpmTSL-------N-PYMRVG---EQLMEVlmlhkglSKAAAFEESVrmldaVKMPEARKRM------KMfphef 169
Cdd:cd03253 78 GVVPQD--TVLfndtigyNiRYGRPDatdEEVIEA-------AKAAQIHDKI-----MRFPDGYDTIvgerglKL----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTME 249
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
..
gi 505807353 250 YG 251
Cdd:cd03253 216 RG 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-256 |
1.43e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 104.82 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDLN 99
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP---RSGSIRFDGRDITGLPPHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLraeQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKmpEARKRMKmfpHEFSGGMRQRVMI 179
Cdd:cd03224 74 RA---GIGYVPEGRR--IFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK--ERRKQLA---GTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
41-246 |
1.56e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 104.90 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLlaaNGHISGSATFNGREILNLPERDLNKLRAEQISMIFQdpMTSLNPY 120
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 121 MRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMpeaRKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:PRK11629 102 FTALENVAMPLLI-GKKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505807353 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGR 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-248 |
3.92e-26 |
|
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: 103.95 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 16 SGLLLDVKDLrvtFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGreilNLPE 95
Cdd:cd03267 17 PGLIGSLKSL---FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT---SGEVRVAG----LVPW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 RDLNKLRAeQISMIFQDPmtslnpymrvgEQL------MEVLMLHKGLS--KAAAFEESVRMLdaVKMPEARKRMKMFPH 167
Cdd:cd03267 87 KRRKKFLR-RIGVVFGQK-----------TQLwwdlpvIDSFYLLAAIYdlPPARFKKRLDEL--SELLDLEELLDTPVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
.
gi 505807353 248 M 248
Cdd:cd03267 233 L 233
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-251 |
3.94e-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: 105.56 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTfKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTafalmgLLAANGHI---SGSATFNGREILnlpERDLNKLR 102
Cdd:COG1125 6 NVT-KRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT------LRMINRLIeptSGRILIDGEDIR---DLDPVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 103 aEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEA--RKRmkmFPHEFSGGMRQRVMIA 180
Cdd:COG1125 76 -RRIGYVIQQ--IGLFPHMTVAENIATVPRL-LGWDKERIRARVDELLELVGLDPEeyRDR---YPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD------LGvvagicDKVLVMYAGRTMEYG 251
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDidealkLG------DRIAVMREGRIVQYD 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
42-246 |
5.31e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.30 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 42 LNFNL--RAGETLGIVGESGSGKSqTAFALM-GLLAAnghISGSATFNGREILNLP--ERdlnklraeQISMIFQDpmTS 116
Cdd:COG3840 16 LRFDLtiAAGERVAILGPSGAGKS-TLLNLIaGFLPP---DSGRILWNGQDLTALPpaER--------PVSMLFQE--NN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LNPYMRVGEQLmeVLMLHKGLSKAAAFEESVR-MLDAVKMPEARKRMkmfPHEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:COG3840 82 LFPHLTVAQNI--GLGLRPGLKLTAEQRAQVEqALERVGLAGLLDRL---PGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505807353 196 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-268 |
7.79e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.40 E-value: 7.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGD----VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGREILNlpERDLNKLR 102
Cdd:PRK13633 10 VSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE---GKVYVDGLDTSD--EENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 103 aEQISMIFQDPmtslnpymrvGEQLMevlmlhkglskAAAFEESVRM-------------------LDAVKMPEARKRMk 163
Cdd:PRK13633 85 -NKAGMVFQNP----------DNQIV-----------ATIVEEDVAFgpenlgippeeirervdesLKKVGMYEYRRHA- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 164 mfPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMY 243
Cdd:PRK13633 142 --PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMD 218
|
250 260
....*....|....*....|....*
gi 505807353 244 AGRTMEYGQARDVFYQPSHPYSIGL 268
Cdd:PRK13633 219 SGKVVMEGTPKEIFKEVEMMKKIGL 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
38-268 |
1.03e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.95 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILN-LPERDLNKLRaEQISMIFQDPMts 116
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPT---SGTVTIGERVITAgKKNKKLKPLR-KKVGIVFQFPE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 lnpymrvgEQLMEVLMLHK--------GLSKAAAFEESVRMLDAVKMPEarKRMKMFPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK13634 96 --------HQLFEETVEKDicfgpmnfGVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGL 268
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGL 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-257 |
1.81e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.54 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDL 98
Cdd:PRK13548 2 MLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSP---DSGEVRLNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRA---EQISMIFqdpmtslnPYmRVGEQlmeVLM--LHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGM 173
Cdd:PRK13548 75 ARRRAvlpQHSSLSF--------PF-TVEEV---VAMgrAPHGLSRAEDDALVAAALAQVDLAHLAGR---DYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 174 RQRVMIAMALL------CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
250
....*....|
gi 505807353 248 MEYGQARDVF 257
Cdd:PRK13548 220 VADGTPAEVL 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-277 |
2.04e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.92 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 10 PQAAQQSGL--LLDVKDLRVTFktpDGDvTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGH-ISGSATFN 86
Cdd:PRK11607 8 PQAKTRKALtpLLEIRNLTKSF---DGQ-HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQpTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 87 GREILNLP--ERDLNklraeqisMIFQDpmTSLNPYMRVgEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMkm 164
Cdd:PRK11607 80 GVDLSHVPpyQRPIN--------MMFQS--YALFPHMTV-EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 165 fPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 244
Cdd:PRK11607 147 -PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
250 260 270
....*....|....*....|....*....|...
gi 505807353 245 GRTMEYGQARDVFYQPSHPYSIGLLNAVPRLDG 277
Cdd:PRK11607 226 GKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-233 |
3.04e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 106.35 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA-NGHISGSATFNGREILNLPERD 97
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGClDKPTSGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKLRAEQISMIFQdpMTSLNPYMrVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEarkRMKMFPHEFSGGMRQRV 177
Cdd:PRK10535 80 LAQLRREHFGFIFQ--RYHLLSHL-TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVA 233
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAA 208
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-251 |
3.41e-25 |
|
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: 101.46 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPD-GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAfALmgLLAANGHISGSATFNGREILNLperDLNKLRaEQ 105
Cdd:cd03249 6 VSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVV-SL--LERFYDPTSGEILLDGVDIRDL---NLRWLR-SQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDPM---TSlnpymrVGEQLmevlmlhkGLSKAAAFEESVRmlDAVKMPEARKRMKMFPHEF-----------SG 171
Cdd:cd03249 79 IGLVSQEPVlfdGT------IAENI--------RYGKPDATDEEVE--EAAKKANIHDFIMSLPDGYdtlvgergsqlSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-251 |
3.86e-25 |
|
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: 100.56 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFkTPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPerdLN 99
Cdd:cd03369 7 IEVENLSVRY-APDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA---EEGKIEIDGIDISTIP---LE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRaEQISMIFQDPM-------TSLNPY-MRVGEQLMEVLMLHKGLSKaaafeesvrmldavkmpearkrmkmfpheFSG 171
Cdd:cd03369 79 DLR-SSLTIIPQDPTlfsgtirSNLDPFdEYSDEEIYGALRVSEGGLN-----------------------------LSQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:cd03369 129 GQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE---EFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEY 204
|
.
gi 505807353 251 G 251
Cdd:cd03369 205 D 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-247 |
5.01e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafaLMGLLAanGHI---SGSATFNGREI-LNLP 94
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKS-T---LMKILY--GLYqpdSGEILIDGKPVrIRSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 95 eRDLNKLRaeqISMIFQDPMtsLNPYMRVgeqlMEVLMLhkGLSKAAAFeesvrmldAVKMPEARKR----MKMFP---- 166
Cdd:COG3845 75 -RDAIALG---IGMVHQHFM--LVPNLTV----AENIVL--GLEPTKGG--------RLDRKAARARirelSERYGldvd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 167 -----HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALdvTVQ--AQIMTLLNELKREfNTAIIMITHDLGVVAGICDKV 239
Cdd:COG3845 135 pdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRV 211
|
....*...
gi 505807353 240 LVMYAGRT 247
Cdd:COG3845 212 TVLRRGKV 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-260 |
5.50e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 6 MTKAPQAAQQSGLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANghiSGSAT 84
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIaGFETPD---SGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 85 FNGREILNLPerdlnklrAEQ--ISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgLSKAaafEESVRMLDAVKMPEARKRM 162
Cdd:PRK09452 73 LDGQDITHVP--------AENrhVNTVFQS--YALFPHMTVFENVAFGLRMQK-TPAA---EITPRVMEALRMVQLEEFA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 163 KMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:PRK09452 139 QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
250
....*....|....*...
gi 505807353 243 YAGRTMEYGQARDVFYQP 260
Cdd:PRK09452 219 RDGRIEQDGTPREIYEEP 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-256 |
6.08e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.15 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 17 GLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPER 96
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT---AGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 97 DLNKlraeQISMIFQDpmTSLNPYMRVgEQLMEvLMLHKGLSKAAAFEESVRMldAVKMPEARKRMKMFPH----EFSGG 172
Cdd:PRK09536 74 AASR----RVASVPQD--TSLSFEFDV-RQVVE-MGRTPHRSRFDTWTETDRA--AVERAMERTGVAQFADrpvtSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMItHDLGVVAGICDKVLVMYAGRTMEYGQ 252
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGP 222
|
....
gi 505807353 253 ARDV 256
Cdd:PRK09536 223 PADV 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-257 |
1.29e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.84 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlnlPERDLNKLRaEQI 106
Cdd:PRK13632 13 VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ---SGEIKIDGITI---SKENLKEIR-KKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQDPmtslnpymrvGEQLMevlmlhkGLSKAA--AFEESVRMLDAVKMP----EARKRMKMF------PHEFSGGMR 174
Cdd:PRK13632 86 GIIFQNP----------DNQFI-------GATVEDdiAFGLENKKVPPKKMKdiidDLAKKVGMEdyldkePQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGQAR 254
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
|
...
gi 505807353 255 DVF 257
Cdd:PRK13632 228 EIL 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-267 |
2.80e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.35 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 35 DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLA---ANGHISGSATFNGREILNLperDLNKLRAEqISMIFQ 111
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQI---DAIKLRKE-VGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 112 DPmtSLNPYMRVGEQLMEVLMLHKGLSK---AAAFEESVRMLDAVKmpEARKRMKMFPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK14246 98 QP--NPFPHLSIYDNIAYPLKSHGIKEKreiKKIVEECLRKVGLWK--EVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQP----SHPY 264
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPknelTEKY 251
|
...
gi 505807353 265 SIG 267
Cdd:PRK14246 252 VIG 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-247 |
3.47e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.70 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA---NGHISGSATFNGREILNLPE 95
Cdd:PRK13549 5 LLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKS----TLMKVLSGvypHGTYEGEIIFEGEELQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 RDlnklrAEQ--ISMIFQDPMtsLNPYMRVGEQ--LMEVLMLHKGLSKAAAFEESVRMLDAVKM---PEARKRmkmfphE 168
Cdd:PRK13549 77 RD-----TERagIAIIHQELA--LVKELSVLENifLGNEITPGGIMDYDAMYLRAQKLLAQLKLdinPATPVG------N 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRH 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-246 |
5.90e-24 |
|
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: 102.21 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllAANGHISGSATFNGREIlnlPERDLNKLRAEQISMIFQD-PMTSL 117
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGKFEGNVFINGKPV---DIRNPAQAIRAGIAMVPEDrKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 118 NPYMRVGEQL-MEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFP-HEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:TIGR02633 351 VPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505807353 196 TTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-251 |
6.27e-24 |
|
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: 96.85 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTPDGDVTA--VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAaNGHISGSATFNGReilNLPERD 97
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT-GLGVSGEVLINGR---PLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKlraeQISMIFQDPMtsLNPYMRVGEQLMEVLMLhKGLSkaaafeesvrmldavkmpearkrmkmfphefsGGMRQRV 177
Cdd:cd03213 80 FRK----IIGYVPQDDI--LHPTLTVRETLMFAAKL-RGLS--------------------------------GGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDL-GVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-260 |
1.05e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 17 GLLLDVKDLRVTF--KTPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GHISGSATFNGREILNL 93
Cdd:PRK13631 19 DIILRVKNLYCVFdeKQEN-ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKyGTIQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 PE---------RDLNKLRaEQISMIFQDPmtslnPYMRVGEQLMEVLM---LHKGLSKAAAFEESVRMLdaVKMPEARKR 161
Cdd:PRK13631 98 ELitnpyskkiKNFKELR-RRVSMVFQFP-----EYQLFKDTIEKDIMfgpVALGVKKSEAKKLAKFYL--NKMGLDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 162 MKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLV 241
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIV 248
|
250
....*....|....*....
gi 505807353 242 MYAGRTMEYGQARDVFYQP 260
Cdd:PRK13631 249 MDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-257 |
1.66e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.16 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 18 LLLDVKDLRVTFKTPdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREI-LNLPE- 95
Cdd:PRK13645 7 IILDNVSYTYAKKTP-FEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISE---TGQTIVGDYAIpANLKKi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 RDLNKLRAEqISMIFQDPMTSLnpYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPeaRKRMKMFPHEFSGGMRQ 175
Cdd:PRK13645 83 KEVKRLRKE-IGLVFQFPEYQL--FQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
..
gi 505807353 256 VF 257
Cdd:PRK13645 238 IF 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-264 |
1.85e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLNKLRAEQISMIFQDpmTSL 117
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT---RGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 118 NPYMRVgeqlMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:PRK10070 118 MPHMTV----LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 198 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPY 264
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
39-246 |
2.13e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.39 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllAANGHISGSATFNGREI-LNLPERDLnklrAEQISMIFQD-PMTS 116
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGRWEGEIFIDGKPVkIRNPQQAI----AQGIAMVPEDrKRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LNPYMRVGE--------QLMEVLMLHKGLSKAAAFEESVRMldAVKMPEARKRMKmfphEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK13549 352 IVPVMGVGKnitlaaldRFTGGSRIDDAAELKTILESIQRL--KVKTASPELAIA----RLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-269 |
2.18e-23 |
|
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: 98.33 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 54 IVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPErdlnKLRAeqISMIFQDpmTSLNPYMRVGEQLMEVLML 133
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD---SGSIMLDGEDVTNVPP----HLRH--INMVFQS--YALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 134 hKGLSKAaafEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNE 213
Cdd:TIGR01187 70 -RKVPRA---EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 214 LKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGLL 269
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-246 |
2.21e-23 |
|
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: 96.12 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLNKlraeQI 106
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT---SGSVLLDGTDIRQLDPADLRR----NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQDPMtslnpymrvgeqlmevlmLHKG-----LSKAAAFEESVRMLDAVKMPEARKRMKMFPHEF-----------S 170
Cdd:cd03245 81 GYVPQDVT------------------LFYGtlrdnITLGAPLADDERILRAAELAGVTDFVNKHPNGLdlqigergrglS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-246 |
2.35e-23 |
|
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: 94.59 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLperDLNKLRaEQ 105
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT---SGRVRLDGADISQW---DPNELG-DH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDpmtslnpymrvgEQLmevlmlhkglskaaaFEESVRmlDAVkmpearkrmkmfpheFSGGMRQRVMIAMALLC 185
Cdd:cd03246 78 VGYLPQD------------DEL---------------FSGSIA--ENI---------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLA-SADRILVLEDGR 172
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-251 |
2.47e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.11 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 18 LLLDVKDLrvTFKTPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERD 97
Cdd:PRK13647 3 NIIEVEDL--HFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ---RGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 LNKlraeQISMIFQDP---MTSLNPYMRV--GEQLMevlmlhkGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGG 172
Cdd:PRK13647 77 VRS----KVGLVFQDPddqVFSSTVWDDVafGPVNM-------GLDKDEVERRVEEALKAVRMWDFRDKP---PYHLSYG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:PRK13647 143 QKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
34-229 |
2.56e-23 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 99.02 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTafalmgLL-AANGHI---SGSATFNGREILNLPERDLNKLRAEQISMI 109
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKS-T------LVrCLNRLIeptAGEVLIDGEDITKLSKKELRELRRKKMSMV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 110 FQdpmtS--LNPYMRVGEQL---MEVlmlhKGLSKAAAFEESVRMLDAVKMpEARKrmKMFPHEFSGGMRQRVMIAMALL 184
Cdd:COG4175 111 FQ----HfaLLPHRTVLENVafgLEI----QGVPKAERRERAREALELVGL-AGWE--DSYPDELSGGMQQRVGLARALA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505807353 185 CRPKLLIADEPTTALD----VTVQAQIMTLLNELKRefnTaIIMITHDL 229
Cdd:COG4175 180 TDPDILLMDEAFSALDplirREMQDELLELQAKLKK---T-IVFITHDL 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
39-257 |
3.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREI-LNLPERDLNKLRaEQISMIFQDPMTSL 117
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS---SGTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 118 npymrVGEQLMEVLM---LHKGLSKAAAFEESVRMLDAVKMPEarKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK13641 99 -----FENTVLKDVEfgpKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 195 PTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-259 |
3.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILN-LPERDLNKLRaEQISMIFQDPMTS 116
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT---TGTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LnpYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPeaRKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:PRK13646 98 L--FEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQ 259
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-251 |
4.00e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.04 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALmgLLAANGHISGSATFNGREIlnlpeRDLNK--LRaE 104
Cdd:PRK13657 340 VSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINL--LQRVFDPQSGRILIDGTDI-----RTVTRasLR-R 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 105 QISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVK-MPEARKRMkmfpheFSGGMRQRVMIA 180
Cdd:PRK13657 410 NIAVVFQDAGlfnRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDtVVGERGRQ------LSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-251 |
4.67e-23 |
|
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: 93.92 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDlrVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLperdlN 99
Cdd:cd03247 1 LSINN--VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGVPVSDL-----E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAEQISMIFQDPM---TSLnpYMRVGEQlmevlmlhkglskaaafeesvrmldavkmpearkrmkmfpheFSGGMRQR 176
Cdd:cd03247 71 KALSSLISVLNQRPYlfdTTL--RNNLGRR------------------------------------------FSGGERQR 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYG 251
Cdd:cd03247 107 LALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-256 |
5.89e-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: 95.43 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPerdl 98
Cdd:COG0410 3 MLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR---SGSIRFDGEDITGLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 nklrAEQIS-----------MIFqdpmtslnPYMRVGEQLMEVLMLHKGLSKAAAfeesvrMLDAVkmpearkrMKMFP- 166
Cdd:COG0410 72 ----PHRIArlgigyvpegrRIF--------PSLTVEENLLLGAYARRDRAEVRA------DLERV--------YELFPr 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 167 -HEF--------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICD 237
Cdd:COG0410 126 lKERrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIAD 204
|
250
....*....|....*....
gi 505807353 238 KVLVMYAGRTMEYGQARDV 256
Cdd:COG0410 205 RAYVLERGRIVLEGTAAEL 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-257 |
7.64e-23 |
|
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: 99.05 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDLnklrAEQ 105
Cdd:COG4618 335 NLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP---TAGSVRLDGADLSQWDREEL----GRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDPmtslnpymrvgeQLmevlmlhkglskaaaFEESV-----RM--LDAVKMPEARKRMKMfpHEF--------- 169
Cdd:COG4618 408 IGYLPQDV------------EL---------------FDGTIaeniaRFgdADPEKVVAAAKLAGV--HEMilrlpdgyd 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 ----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAgICDKV 239
Cdd:COG4618 459 trigeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKL 536
|
250
....*....|....*...
gi 505807353 240 LVMYAGRTMEYGQARDVF 257
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVL 554
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
27-242 |
1.06e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.51 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVtAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGREILNLPERDLNKlraeQI 106
Cdd:TIGR02857 327 VSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE---GSIAVNGVPLADADADSWRD----QI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQdpmtslNPYMRVGeQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFP-----HEFSGGMRQRVMIAM 181
Cdd:TIGR02857 399 AWVPQ------HPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVM 242
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-251 |
2.04e-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: 94.09 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFK-TPDGDVtAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLperDLNKLRAe 104
Cdd:cd03252 5 HVRFRyKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE---NGRVLVDGHDLALA---DPAWLRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 105 QISMIFQDPmTSLNPYMRVGEQLMEVLM-LHKglskaaaFEESVRMLDA----VKMPEARKRMKmfpHE----FSGGMRQ 175
Cdd:cd03252 77 QVGVVLQEN-VLFNRSIRDNIALADPGMsMER-------VIEAAKLAGAhdfiSELPEGYDTIV---GEqgagLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-227 |
2.11e-22 |
|
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: 93.49 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 29 FKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGREilnlPERDLNKlraEQISM 108
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQP----RKPDQFQ---KCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 109 IFQDpmTSLNPYMRVGEQL--MEVLMLHKGLSKA--AAFEESVRMLDAVKMPEARKRMKmfphEFSGGMRQRVMIAMALL 184
Cdd:cd03234 86 VRQD--DILLPGLTVRETLtyTAILRLPRKSSDAirKKRVEDVLLRDLALTRIGGNLVK----GISGGERRRVSIAVQLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505807353 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 227
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
41-246 |
2.15e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.43 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGREILNLPERDlnKLRA--------EQISMIFQD 112
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG---GRIMLNGKEINALSTAQ--RLARglvylpedRQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 PMTSLNPYMRVGEQLMevLMLHKGlSKAAAFEESVRMLDaVKMPEARKRMKmfphEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PRK15439 356 APLAWNVCALTHNRRG--FWIKPA-RENAVLERYRRALN-IKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505807353 193 DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-246 |
3.94e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.21 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllaangH-----ISGSATFNGREILNLP 94
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG------HpkyevTSGSILLDGEDILELS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 95 --ERdlnklRAEQISMIFQDPMtslnpymRV-GEQLMEVLMLhkglSKAAAFEESVRMLDAVK-MPEARKRMKMFPH--- 167
Cdd:COG0396 71 pdER-----ARAGIFLAFQYPV-------EIpGVSVSNFLRT----ALNARRGEELSAREFLKlLKEKMKELGLDEDfld 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 -----EFSGGMRQRVMIA-MALLcRPKLLIADEPTTALDVTVqAQIMT-LLNELKREfNTAIIMITH-----DLGVVagi 235
Cdd:COG0396 135 ryvneGFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIDA-LRIVAeGVNKLRSP-DRGILIITHyqrilDYIKP--- 208
|
250
....*....|.
gi 505807353 236 cDKVLVMYAGR 246
Cdd:COG0396 209 -DFVHVLVDGR 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
34-246 |
3.99e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.63 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGL-LAANGHIsgsaTFNGREILNLPERDLNKLRaEQISMIFQD 112
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKI----WFSGHDITRLKNREVPFLR-RQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 PMTSLNpyMRVGEQLMEVLMLhkglskAAAFEESVR-----MLDAVKMPEarkRMKMFPHEFSGGMRQRVMIAMALLCRP 187
Cdd:PRK10908 88 HHLLMD--RTVYDNVAIPLII------AGASGDDIRrrvsaALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 188 KLLIADEPTTALDVTVQAQIMTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
34-261 |
4.37e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.17 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILN--LPERDlnklraeqISMIFQ 111
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT---EGQIFIDGEDVTHrsIQQRD--------ICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 112 DpmTSLNPYMRVGEQLMEVL-MLhkGLSKAaafEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK11432 86 S--YALFPHMSLGENVGYGLkML--GVPKE---ERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 191 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPS 261
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-267 |
4.55e-22 |
|
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: 96.43 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA---NGHISGSATFNGREilnLPE 95
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKS----TLMKILSGvypHGTWDGEIYWSGSP---LKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 RDLNKLRAEQISMIFQDPMtsLNPYMRVGEQ--LMEVLMLHKGLSKAAAF----EESVRMLDAVKMPEARKRMkmfphEF 169
Cdd:TIGR02633 70 SNIRDTERAGIVIIHQELT--LVPELSVAENifLGNEITLPGGRMAYNAMylraKNLLRELQLDADNVTRPVG-----DY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR--- 246
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQhva 221
|
250 260 270
....*....|....*....|....*....|....
gi 505807353 247 -------------TMEYGQARDVFYqPSHPYSIG 267
Cdd:TIGR02633 222 tkdmstmseddiiTMMVGREITSLY-PHEPHEIG 254
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-227 |
7.13e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.41 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTfkTPDGDVTaVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGL-LAANGHISGSAtfnGREILNLPERd 97
Cdd:COG4178 363 LALEDLTLR--TPDGRPL-LEDLSLSLKPGERLLITGPSGSGKS-TLLrAIAGLwPYGSGRIARPA---GARVLFLPQR- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 lnklraeqismifqdpmtslnPYMRVGEqLMEVLmLHKGLSKAAAFEESVRMLDAVKMPEARKRM---KMFPHEFSGGMR 174
Cdd:COG4178 435 ---------------------PYLPLGT-LREAL-LYPATAEAFSDAELREALEAVGLGHLAERLdeeADWDQVLSLGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505807353 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkREFNTAIIMITH 227
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-262 |
8.07e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 92.14 E-value: 8.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 39 VNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAA-NGHISGSATFNGREILNL-PERdlnklraeqiSMIFQDpmTS 116
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLISGlAQPTSGGVILEGKQITEPgPDR----------MVVFQN--YS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LNPYMRVGEQL-MEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:TIGR01184 65 LLPWLTVRENIaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 196 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV-FYQPSH 262
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-251 |
1.47e-21 |
|
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: 91.52 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDlrVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGHI-SGSATFNGREIlnlpeRD- 97
Cdd:cd03251 1 VEFKN--VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVdSGRILIDGHDV-----RDy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 -LNKLRaEQISMIFQDPM---TSLNPYMRVGeqlmevlmlhkglsKAAAFEESVRmlDAVKMPEARKRMKMFPHEF---- 169
Cdd:cd03251 70 tLASLR-RQIGLVSQDVFlfnDTVAENIAYG--------------RPGATREEVE--EAARAANAHEFIMELPEGYdtvi 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 -------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLGVVAGIcDKVLVM 242
Cdd:cd03251 133 gergvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRLSTIENA-DRIVVL 209
|
....*....
gi 505807353 243 YAGRTMEYG 251
Cdd:cd03251 210 EDGKIVERG 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-275 |
2.47e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKtpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDL 98
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT---SGSVLIRGEPITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLraeqISMIFQDPMTSLnpYMRVGEQLMEVLMLHKGLSKAAA---FEESVRMLDavkMPEARKRMkmfPHEFSGGMRQ 175
Cdd:PRK13652 77 RKF----VGLVFQNPDDQI--FSPTVEQDIAFGPINLGLDEETVahrVSSALHMLG---LEELRDRV---PHHLSGGEKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:PRK13652 145 RVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
250 260
....*....|....*....|.
gi 505807353 256 VFYQPSHPYSIGL-LNAVPRL 275
Cdd:PRK13652 225 IFLQPDLLARVHLdLPSLPKL 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-246 |
2.49e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 94.30 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 39 VNDLNFNLRAGETLGIVGESGSGKSQtafaLMGLL-AANGHISGSATFNGREILNL-PERDLnklrAEQISMIFQD---- 112
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTE----LMKVLyGALPRTSGYVTLDGHEVVTRsPQDGL----ANGIVYISEDrkrd 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 ------------PMTSLNPYMRVGEQLmevlmlhKGLSKAAAFEESVRMLDaVKMPEARKRMKMFphefSGGMRQRVMIA 180
Cdd:PRK10762 340 glvlgmsvkenmSLTALRYFSRAGGSL-------KHADEQQAVSDFIRLFN-IKTPSMEQAIGLL----SGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-246 |
7.29e-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: 89.15 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 43 NFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDlnklraEQISMIFQDpmTSLNPYMR 122
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP---ASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 123 VGEQLmeVLMLHKGLSKAAafEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 202
Cdd:TIGR01277 87 VRQNI--GLGLHPGLKLNA--EQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505807353 203 VQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR01277 163 LREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-255 |
8.13e-21 |
|
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: 93.24 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGHI-SGSATFNGREILNLPERDLNKLRA-- 103
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRFYEPdSGQILLDGHDLADYTLASLRRQVAlv 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 104 EQISMIFQDPMTSLNPYMRVGEQLMEvlMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMfphefSGGMRQRVMIAMAL 183
Cdd:TIGR02203 412 SQDVVLFNDTIANNIAYGRTEQADRA--EIERALAAAYAQDFVDKLPLGLDTPIGENGVLL-----SGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGRTMEYGQARD 255
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-259 |
8.52e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 11 QAAQQSGLLLDVKDLRVTfkTPDGDVTAVNdLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHIsgsaTFNGREi 90
Cdd:PRK11174 341 ELASNDPVTIEAEDLEIL--SPDGKTLAGP-LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSL----KINGIE- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 91 lnLPERDLNKLRaEQISMIFQDPM---TSLNPYMRVG------EQLMEVLMLhkglSKAAAFEESVRM-LD-AVKMPEAR 159
Cdd:PRK11174 413 --LRELDPESWR-KHLSWVGQNPQlphGTLRDNVLLGnpdasdEQLQQALEN----AWVSEFLPLLPQgLDtPIGDQAAG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 160 krmkmfpheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKV 239
Cdd:PRK11174 486 ---------LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTHQLEDLAQ-WDQI 553
|
250 260
....*....|....*....|....*.
gi 505807353 240 LVMYAGRTMEYG------QARDVFYQ 259
Cdd:PRK11174 554 WVMQDGQIVQQGdyaelsQAGGLFAT 579
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
34-278 |
8.63e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 8.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLnklrAEQISMIFQDP 113
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ---SGTVFLGDKPISMLSSRQL----ARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 MT------------SLNPYM----RVG---EQLMEVLMLHKGLSKAAafeesVRMLDavkmpearkrmkmfphEFSGGMR 174
Cdd:PRK11231 86 LTpegitvrelvayGRSPWLslwgRLSaedNARVNQAMEQTRINHLA-----DRRLT----------------DLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQAR 254
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
250 260
....*....|....*....|....
gi 505807353 255 DVFYQpshpysiGLLNAVPRLDGE 278
Cdd:PRK11231 224 EVMTP-------GLLRTVFDVEAE 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-246 |
1.61e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 17 GLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAanghisGSATFNGREIL--NLP 94
Cdd:PRK11247 10 GTPLLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLA------GLETPSAGELLagTAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 95 erdLNKLRaEQISMIFQDpmTSLNPYMRVgeqLMEVLMLHKGLSKAAAFEesvrMLDAVKMPEarkRMKMFPHEFSGGMR 174
Cdd:PRK11247 76 ---LAEAR-EDTRLMFQD--ARLLPWKKV---IDNVGLGLKGQWRDAALQ----ALAAVGLAD---RANEWPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
38-229 |
1.63e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.99 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAanGHI---SGSATFNGREIlnlperdlNKLRAEQiSMIFQDpm 114
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKT----TLLNLIA--GFVpyqHGSITLDGKPV--------EGPGAER-GVVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 115 TSLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 505807353 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 229
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-251 |
1.94e-20 |
|
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: 87.58 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTfktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllaangH-----ISGSATFNGREILNLP 94
Cdd:cd03217 1 LEIKDLHVS----VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG------HpkyevTEGEILFKGEDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 95 --ERDLNKlraeqISMIFQDPMT----SLNPYMR-VGEQlmevlmlhkglskaaafeesvrmldavkmpearkrmkmfph 167
Cdd:cd03217 71 peERARLG-----IFLAFQYPPEipgvKNADFLRyVNEG----------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 eFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI-CDKVLVMYAGR 246
Cdd:cd03217 105 -FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGR 182
|
....*
gi 505807353 247 TMEYG 251
Cdd:cd03217 183 IVKSG 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-262 |
1.99e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 37 TAVNDLNFNLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGHISGSATFNGREILNLpeRDLNKLRaEQISMIFQDPm 114
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYRYSGDVLLGGRSIFNY--RDVLEFR-RRVGMLFQRP- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 115 tslNPY-MRVGEQLMEVLMLHKGLSK------AAAFEESVRMLDAVKmpearKRMKMFPHEFSGGMRQRVMIAMALLCRP 187
Cdd:PRK14271 111 ---NPFpMSIMDNVLAGVRAHKLVPRkefrgvAQARLTEVGLWDAVK-----DRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 188 KLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSH 262
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-229 |
2.00e-20 |
|
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: 92.04 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 8 KAPQAAQQSGLLLDVKDLR---VTFKTPDGDVtAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSAT 84
Cdd:TIGR02868 318 AEGSAPAAGAVGLGKPTLElrdLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ---GEVT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 85 FNGREILNLPERDLNKLraeqISMIFQDPM---TSLNPYMRVG------EQLMEVLmlhkglskaaafeESVRMLDAVKM 155
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRR----VSVCAQDAHlfdTTVRENLRLArpdatdEELWAAL-------------ERVGLADWLRA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 156 PEARKRMKMFPH--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDL 229
Cdd:TIGR02868 457 LPDGLDTVLGEGgaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
37-257 |
3.80e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 87.60 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 37 TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPerdLNKlRAE-------QISMI 109
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGKILLDGQDITKLP---MHK-RARlgigylpQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 110 FQDpmtslnpyMRVGEQLMEVLMLHKgLSKAAAFEESVRMLDAVKMPEARKRMKMFpheFSGGMRQRVMIAMALLCRPKL 189
Cdd:cd03218 87 FRK--------LTVEENILAVLEIRG-LSKKEREEKLEELLEEFHITHLRKSKASS---LSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 190 LIADEPTTALDVTVQAQIMTLLNELKrefNTAI-IMIT-HDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILK---DRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-240 |
4.29e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.86 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGR-EILNLPERd 97
Cdd:PRK09544 4 LVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNGKlRIGYVPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 lnklraeqismIFQDPMTSLNpymrvgeqLMEVLMLHKGLSKAaafeesvRMLDAVKMPEARKRMKMFPHEFSGGMRQRV 177
Cdd:PRK09544 76 -----------LYLDTTLPLT--------VNRFLRLRPGTKKE-------DILPALKRVQAGHLIDAPMQKLSGGETQRV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 240
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-257 |
4.43e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.40 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 13 AQQSGLLLDvkDLRVTFKTPDgdvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHISgsatfngreIL 91
Cdd:PRK15056 2 MQQAGIVVN--DVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVrLASGKIS---------IL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 92 NLPERdlNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVkmpeARKRMKMFPH---- 167
Cdd:PRK15056 68 GQPTR--QALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAAL----ARVDMVEFRHrqig 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICDKVlVMYAGRT 247
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYT-VMVKGTV 219
|
250
....*....|
gi 505807353 248 MEYGQARDVF 257
Cdd:PRK15056 220 LASGPTETTF 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-256 |
4.44e-20 |
|
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: 90.87 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDLNKlraeQ 105
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP---TSGSVRLDGADLKQWDRETFGK----H 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISmifqdpmtslnpYMRVGEQLMEvlmlhkGLSKA--AAFEESV---RMLDAVKMPEARKRMKMFPHEF----------- 169
Cdd:TIGR01842 394 IG------------YLPQDVELFP------GTVAEniARFGENAdpeKIIEAAKLAGVHELILRLPDGYdtvigpggatl 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGIcDKVLVMYAGRTME 249
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGCV-DKILVLQDGRIAR 533
|
....*..
gi 505807353 250 YGQARDV 256
Cdd:TIGR01842 534 FGERDEV 540
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-227 |
6.17e-20 |
|
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: 85.28 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFKTPDGDVTaVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHISGSAtfnGREILNLPERdlnklrae 104
Cdd:cd03223 5 NLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWpWGSGRIGMPE---GEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 105 qismifqdpmtslnPYMRVGeQLMEVLMlhkglskaaafeesvrmldavkmpearkrmkmFP--HEFSGGMRQRVMIAMA 182
Cdd:cd03223 73 --------------PYLPLG-TLREQLI--------------------------------YPwdDVLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505807353 183 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrefnTAIIMITH 227
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-251 |
7.56e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.35 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGREILNLPERDL 98
Cdd:PRK11300 5 LLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG---GTILLRGQHIEGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKL---RAEQISMIFQDpMTSLNPYMRVGEQLMEVLMLHkGLSKAAAFEESVR--------MLDAVKMPEARKRMKmfpH 167
Cdd:PRK11300 78 ARMgvvRTFQHVRLFRE-MTVIENLLVAQHQQLKTGLFS-GLLKTPAFRRAESealdraatWLERVGLLEHANRQA---G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
....
gi 505807353 248 MEYG 251
Cdd:PRK11300 233 LANG 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
30-256 |
1.19e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 30 KTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANghiSGSATFNGReilnlperdlnklraeqISM 108
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIaGILEPT---SGRVEVNGR-----------------VSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 109 IFqDPMTSLNPYMRVGEQLMEVLMLHkGLSKA---AAFEESVR---MLDAVKMPearkrMKMFphefSGGMRQRVMIAMA 182
Cdd:COG1134 92 LL-ELGAGFHPELTGRENIYLNGRLL-GLSRKeidEKFDEIVEfaeLGDFIDQP-----VKTY----SSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807353 183 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-246 |
1.25e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.17 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 43 NFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANghiSGSATFNGREILNLP--ERdlnklraeQISMIFQDpmTSLNP 119
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIaGFLTPA---SGSLTLNGQDHTTTPpsRR--------PVSMLFQE--NNLFS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 120 YMRVGEQLmeVLMLHKGLSKAAAFEESVR-MLDAVKMPEARKRmkmFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 198
Cdd:PRK10771 85 HLTVAQNI--GLGLNPGLKLNAAQREKLHaIARQMGIEDLLAR---LPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505807353 199 LDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
33-251 |
2.31e-19 |
|
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: 85.35 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 33 DGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLaanGHISGSATFNGREILNLPErdlNKLRaEQISMIFQD 112
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFY---DPQKGQILIDGIDIRDISR---KSLR-SMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 PM---TSLNPYMRVGEQL--MEVLMLhkgLSKAAAFEESVRML----DAVKMPEArkrmkmfpHEFSGGMRQRVMIAMAL 183
Cdd:cd03254 86 TFlfsGTIMENIRLGRPNatDEEVIE---AAKEAGAHDFIMKLpngyDTVLGENG--------GNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 184 LCRPKLLIADEPTTALDV----TVQAQIMTLLNelkrefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:cd03254 155 LRDPKILILDEATSNIDTetekLIQEALEKLMK------GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-257 |
2.80e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 29 FKTPDGDVTAVNDLNFNLRAgeTLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGrEILNLPERDLNKLRaEQISM 108
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQ---KGAVLWQG-KPLDYSKRGLLALR-QQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 109 IFQDPMTSLNpYMRVGEQLMEVLmlhKGLSKAAAfEESVRMLDAVKMPEARKrmkmFPHE----FSGGMRQRVMIAMALL 184
Cdd:PRK13638 82 VFQDPEQQIF-YTDIDSDIAFSL---RNLGVPEA-EITRRVDEALTLVDAQH----FRHQpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
42-257 |
3.32e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 42 LNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAAnghiSGSATFNGREILNLPERDLNKLRAeqisMIFQDPMTSLNpy 120
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLPG----QGEILLNGRPLSDWSAAELARHRA----YLSQQQSPPFA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 121 MRVGEQLMevLMLHKGLSKAAAFEESVRMLDAVKMpeARKRMKMFpHEFSGGMRQRVMIAMALL-------CRPKLLIAD 193
Cdd:COG4138 84 MPVFQYLA--LHQPAGASSEAVEQLLAQLAEALGL--EDKLSRPL-TQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807353 194 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGIT-VVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-251 |
3.54e-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: 84.51 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 23 KDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGReilnlperdlnklr 102
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD---SGTVTVRGR-------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 103 aeqISMIFqDPMTSLNPYMRVGEQLMEVLMLHkGLSKA--AAFEESVRML----DAVKMPearkrMKmfphEFSGGMRQR 176
Cdd:cd03220 85 ---VSSLL-GLGGGFNPELTGRENIYLNGRLL-GLSRKeiDEKIDEIIEFselgDFIDLP-----VK----TYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-260 |
3.69e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.85 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 18 LLLDVK------DLRVTFKTPDGDVTAvndlnfnlragetlgIVGESGSGKSQTAFALMGLLAANghiSGSATFNGReIL 91
Cdd:PRK11144 2 LELNFKqqlgdlCLTVNLTLPAQGITA---------------IFGRSGAGKTSLINAISGLTRPQ---KGRIVLNGR-VL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 92 NLPERDLNkLRAEQ--ISMIFQDpmTSLNPYMRV-GEqlmevlmLHKGLSK--AAAFEESVRMLDAVKMpearkrMKMFP 166
Cdd:PRK11144 63 FDAEKGIC-LPPEKrrIGYVFQD--ARLFPHYKVrGN-------LRYGMAKsmVAQFDKIVALLGIEPL------LDRYP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
250
....*....|....
gi 505807353 247 TMEYGQARDVFYQP 260
Cdd:PRK11144 207 VKAFGPLEEVWASS 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-257 |
4.14e-19 |
|
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: 85.14 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGHISGSATFN------GREiln 92
Cdd:COG1119 3 LLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLITGDLPPTYGNDVRlfgerrGGE--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 93 lperDLNKLRAeQI---SMIFQDpmtslnpYMRVGEQLMEVLM--------LHKGLSkAAAFEESVRMLDAVKMpeARKR 161
Cdd:COG1119 72 ----DVWELRK-RIglvSPALQL-------RFPRDETVLDVVLsgffdsigLYREPT-DEQRERARELLELLGL--AHLA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 162 MKMFpHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG-VVAGIcDKVL 240
Cdd:COG1119 137 DRPF-GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVL 214
|
250
....*....|....*..
gi 505807353 241 VMYAGRTMEYGQARDVF 257
Cdd:COG1119 215 LLKDGRVVAAGPKEEVL 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-256 |
5.07e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.98 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghiSGSATFNGREILNLPERDLNKLRA---EQISMIFqdpmtsln 118
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG----SGSIQFAGQPLEAWSAAELARHRAylsQQQTPPF-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 119 pymrvgeqLMEV---LMLHKGLSKAAAFEESV--RMLDAVKMPEARKRMKmfpHEFSGGMRQRVMIAMALL-----CRP- 187
Cdd:PRK03695 83 --------AMPVfqyLTLHQPDKTRTEAVASAlnEVAEALGLDDKLGRSV---NQLSGGEWQRVRLAAVVLqvwpdINPa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 188 -KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK03695 152 gQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
38-257 |
8.18e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.80 E-value: 8.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPE-RDLNKLRaEQISMIFQDPMTs 116
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT---QGSVRVDDTLITSTSKnKDIKQIR-KKVGLVFQFPES- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 lnpymrvgeQLMEVLMLhkglsKAAAFEES---VRMLDAVKMpeARKRMKMF----------PHEFSGGMRQRVMIAMAL 183
Cdd:PRK13649 97 ---------QLFEETVL-----KDVAFGPQnfgVSQEEAEAL--AREKLALVgiseslfeknPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807353 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-246 |
1.14e-18 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 82.93 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDlnklraEQISMIFQDpmTSLNPY 120
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQ---SGRVLINGVDVTAAPPAD------RPVSMLFQE--NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 121 MRVGEQLmeVLMLHKGLSKAAAFEESVRMLdAVKMPEARKrMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:cd03298 85 LTVEQNV--GLGLSPGLKLTAEDRQAIEVA-LARVGLAGL-EKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505807353 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
44-242 |
1.48e-18 |
|
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: 82.98 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 44 FNLRAGETLGIVGESGSGKSQTAFALMGLLA---ANGHISGSATFNG-REILNLPERDlnklraeqiSMIFQDPMTslnp 119
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpakGTVKVAGASPGKGwRHIGYVPQRH---------EFAWDFPIS---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 120 ymrVGEQLMEVLMLHKGL---SKAAAFEESVRMLDAVKMPEARKRMKmfpHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:TIGR03771 68 ---VAHTVMSGRTGHIGWlrrPCVADFAAVRDALRRVGLTELADRPV---GELSGGQRQRVLVARALATRPSVLLLDEPF 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505807353 197 TALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:TIGR03771 142 TGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL 186
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
27-251 |
1.59e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.23 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGreiLNLPERDLNKLRaEQI 106
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID---EGEILLDG---HDLRDYTLASLR-NQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMI------FQDPMTSLNPYMRvgeqlmevlmlhKGLSKAAAFEESVRMLDAVKMPEarkrmKMfPHEF----------- 169
Cdd:PRK11176 420 ALVsqnvhlFNDTIANNIAYAR------------TEQYSREQIEEAARMAYAMDFIN-----KM-DNGLdtvigengvll 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTME 249
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
..
gi 505807353 250 YG 251
Cdd:PRK11176 559 RG 560
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-256 |
1.95e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 3 TIEMTKAPQAAQQSGLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GHISg 81
Cdd:PRK13536 25 GISEAKASIPGSMSTVAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDaGKIT- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 82 satfngreILNLPERDLNKLRAEQISMIFQdpMTSLNPYMRVGEQLmevlmlhkgLSKAAAFEESVRMLDAVkMPE---- 157
Cdd:PRK13536 100 --------VLGVPVPARARLARARIGVVPQ--FDNLDLEFTVRENL---------LVFGRYFGMSTREIEAV-IPSllef 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 158 ARKRMKMFPH--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGI 235
Cdd:PRK13536 160 ARLESKADARvsDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERL 238
|
250 260
....*....|....*....|.
gi 505807353 236 CDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK13536 239 CDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-256 |
1.96e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlnlPERdlN 99
Cdd:PRK13537 8 IDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD---AGSISLCGEPV---PSR--A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAEQISMIFQdpMTSLNPYMRVGEQLMeVLMLHKGLSKAAAFEESVRMLDAVKMpEARKRMKMfpHEFSGGMRQRVMI 179
Cdd:PRK13537 76 RHARQRVGVVPQ--FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKL-ENKADAKV--GELSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
34-233 |
4.32e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.74 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGHISGSAtfnGREILNLPERdlnklraeqISMIFQD 112
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRAG---GARVAYVPQR---------SEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 PMTSlnpymrvgEQLMEV-LMLHKGLSK---AAAFEESVRMLDAVKMPEARKRMKmfpHEFSGGMRQRVMIAMALLCRPK 188
Cdd:NF040873 71 PLTV--------RDLVAMgRWARRGLWRrltRDDRAAVDDALERVGLADLAGRQL---GELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVA 233
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-256 |
4.96e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPerdLN 99
Cdd:COG1137 4 LEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGRIFLDGEDITHLP---MH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KlRA-------EQISMIFQDpMTslnpymrVGEQLMEVLMLHKgLSKAAAFEESVRMLDAVKMPEARKRMKMfphEFSGG 172
Cdd:COG1137 74 K-RArlgigylPQEASIFRK-LT-------VEDNILAVLELRK-LSKKEREERLEELLEEFGITHLRKSKAY---SLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 173 MRQRVMIAMALLCRPKLLIADEPTTALD-VTVqAQIMTLLNELKrEFNTAIImIT-HD----LgvvaGICDKVLVMYAGR 246
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVL-ITdHNvretL----GICDRAYIISEGK 213
|
250
....*....|
gi 505807353 247 TMEYGQARDV 256
Cdd:COG1137 214 VLAEGTPEEI 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-255 |
5.60e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 35 DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllaANGHISGSATFNGREILnlPERDLNKLRaEQISMIFQD-- 112
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDKRAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITESrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 -----PMTSLNPYMRVGEQLmevlmlhkglsKAAAFEESVRMLDAVK----MPEARKRMKMFPH-------EFSGGMRQR 176
Cdd:PRK09700 349 dngffPNFSIAQNMAISRSL-----------KDGGYKGAMGLFHEVDeqrtAENQRELLALKCHsvnqnitELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD 255
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-251 |
6.26e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 84.49 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 5 EMTKAPQAAQqsgllLDVKDLRVTFK----TPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiS 80
Cdd:COG5265 341 EVADAPDAPP-----LVVGGGEVRFEnvsfGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVT---S 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 81 GSATFNGREIlnlpeRDLNK--LRAeQISMIFQDpmTSL-------N-PYMRVG---EQLMEVlmlhkglSKAAAFEESV 147
Cdd:COG5265 413 GRILIDGQDI-----RDVTQasLRA-AIGIVPQD--TVLfndtiayNiAYGRPDaseEEVEAA-------ARAAQIHDFI 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 148 RMLdavkmPEARKRM------KMfphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTA 221
Cdd:COG5265 478 ESL-----PDGYDTRvgerglKL-----SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRT 545
|
250 260 270
....*....|....*....|....*....|
gi 505807353 222 IIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:COG5265 546 TLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-261 |
6.28e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 6.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 26 RVTFKTPDGdVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGreilnLPERDLNKLRA-- 103
Cdd:PRK13644 6 NVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ---KGKVLVSG-----IDTGDFSKLQGir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 104 EQISMIFQDPMTSLnpymrVGEQLMEVLML---HKGLSKAAAFEESVRMLDAVKMPEARKRMkmfPHEFSGGMRQRVMIA 180
Cdd:PRK13644 77 KLVGIVFQNPETQF-----VGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRHRS---PKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAgICDKVLVMYAGRTMEYGQARDVFYQP 260
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV 226
|
.
gi 505807353 261 S 261
Cdd:PRK13644 227 S 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
49-277 |
1.30e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 83.78 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 49 GETLGIVGESGSGKSQTAFALMGLLAANGhisgsatFNGREILNlpERDLNKLRAEQISMIFQDPMtsLNPYMRVGEQLM 128
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNN-------FTGTILAN--NRKPTKQILKRTGFVTQDDI--LYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 129 --EVLMLHKGLSKaaafEESVRMLDAV--KMPEARKRMKMFPHEF----SGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:PLN03211 163 fcSLLRLPKSLTK----QEKILVAESVisELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARD-------VFYQPSHP-----YSIGL 268
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDamayfesVGFSPSFPmnpadFLLDL 318
|
....*....
gi 505807353 269 LNAVPRLDG 277
Cdd:PLN03211 319 ANGVCQTDG 327
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-252 |
2.09e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 11 QAAQQSGLLLDVKDlrVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLA----ANghiSGSATFN 86
Cdd:PRK11160 330 STAAADQVSLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTrawdPQ---QGEILLN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 87 GREILNLPERDLnklRAeQISMIFQDP---MTSLNPYMRVG------EQLMEVLMlHKGLSKAAAFEESvrmLDAVKMPE 157
Cdd:PRK11160 401 GQPIADYSEAAL---RQ-AISVVSQRVhlfSATLRDNLLLAapnasdEALIEVLQ-QVGLEKLLEDDKG---LNAWLGEG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 158 ARkrmkmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGIcD 237
Cdd:PRK11160 473 GR--------QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-D 541
|
250
....*....|....*
gi 505807353 238 KVLVMYAGRTMEYGQ 252
Cdd:PRK11160 542 RICVMDNGQIIEQGT 556
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
53-260 |
2.16e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 53 GIVGESGSGKSQTAFAL--MGLLAANGHISGSATFNGREILnlpER--DLNKLRaEQISMIFQDPmtSLNPyMRVGEQL- 127
Cdd:PRK14258 37 AIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNQNIY---ERrvNLNRLR-RQVSMVHPKP--NLFP-MSVYDNVa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 128 --MEVLMLHKGLSKAAAFEESVRmlDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 205
Cdd:PRK14258 110 ygVKIVGWRPKLEIDDIVESALK--DADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASM 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 206 QIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA-----GRTMEYGQARDVFYQP 260
Cdd:PRK14258 188 KVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-249 |
2.97e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLA---ANGHISGSATFNGREilnLPE 95
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKS----TLMKVLSgvyPHGSYEGEILFDGEV---CRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 RDLNKLRAEQISMIFQDpmTSLNPYMRVGEQLM---EVLmlHKGL-SKAAAFEESVRMLDAVKMPEArkrmkmfPHEFSG 171
Cdd:NF040905 70 KDIRDSEALGIVIIHQE--LALIPYLSIAENIFlgnERA--KRGViDWNETNRRARELLAKVGLDES-------PDTLVT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 ----GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRT 247
Cdd:NF040905 139 digvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGRT 217
|
..
gi 505807353 248 ME 249
Cdd:NF040905 218 IE 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-253 |
3.36e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.69 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAanGH-----ISGSATFNGREILNL 93
Cdd:CHL00131 7 ILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKS----TLSKVIA--GHpaykiLEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 -PErdlnkLRAEQ-ISMIFQDPMTSlnpymrVGEQLMEVLML-------HKGLSKAAA---FEESVRMLDAVKMPEArkr 161
Cdd:CHL00131 77 ePE-----ERAHLgIFLAFQYPIEI------PGVSNADFLRLaynskrkFQGLPELDPlefLEIINEKLKLVGMDPS--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 162 mkmFPHE-----FSGGMRQRVMI-AMALLcRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI 235
Cdd:CHL00131 143 ---FLSRnvnegFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYI 217
|
250
....*....|....*....
gi 505807353 236 C-DKVLVMYAGRTMEYGQA 253
Cdd:CHL00131 218 KpDYVHVMQNGKIIKTGDA 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-251 |
3.86e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.46 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPD-GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGREILNLPERDLNKlraeQ 105
Cdd:TIGR00958 484 VSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG---GQVLLDGVPLVQYDHHYLHR----Q 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 ISMIFQDPmtslnpymrvgeqlmeVLM---LHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEF-----------SG 171
Cdd:TIGR00958 557 VALVGQEP----------------VLFsgsVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYdtevgekgsqlSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAqimtLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
46-263 |
5.04e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 46 LRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGREIlnlperDLNKLRAeqIS-MIFQDPMtsLNPYMRVG 124
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPI------DAKEMRA--ISaYVQQDDL--FIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 125 EQLM--EVLMLHKGLSKA---AAFEESVRMLDAVKMPEAR----KRMKmfphEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:TIGR00955 118 EHLMfqAHLRMPRRVTKKekrERVDEVLQALGLRKCANTRigvpGRVK----GLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 196 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG---QARDVFYQPSHP 263
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGspdQAVPFFSDLGHP 264
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
34-256 |
6.01e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.97 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMG-LLAANghiSGSATFNGREILNLPERDLnklrAEQISMIFQD 112
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLPPD---SGEVLVDGLDVATTPSREL----AKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 PmtSLNPYMRVGEqlmevlmL--------HKG-LSKAaafeesvrmlDAVKMPEARKRMKM------FPHEFSGGMRQRV 177
Cdd:COG4604 84 N--HINSRLTVRE-------LvafgrfpySKGrLTAE----------DREIIDEAIAYLDLedladrYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-246 |
7.74e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.93 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLlaaNGHISGSATFNGREILNlpeRDLNKLRAEQISMIFQDP-MTS 116
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGI---REKSAGTITLHGKKINN---HNANEAINHGFALVTEERrSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LNPYMRVGeqlmevlmLHKGLSKAAAFEESVRMLDAVKMPEARK------RMKMFPHE-----FSGGMRQRVMIAMALLC 185
Cdd:PRK10982 337 IYAYLDIG--------FNSLISNIRNYKNKVGLLDNSRMKSDTQwvidsmRVKTPGHRtqigsLSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
38-259 |
1.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.62 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAN------GHISGSATFNGREILnlPERdlnklraEQISMIFQ 111
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTegkvtvGDIVVSSTSKQKEIK--PVR-------KKVGVVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 112 DPMTslnpymrvgeQLMEVLMLHK--------GLSKAAAFEESVRMLDAVKMpeARKRMKMFPHEFSGGMRQRVMIAMAL 183
Cdd:PRK13643 92 FPES----------QLFEETVLKDvafgpqnfGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQ 259
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-256 |
1.64e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.59 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTF--KTPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLN 99
Cdd:PRK13651 5 VKNIVKIFnkKLPT-ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPD---TGTIEWIFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAE--------------------QISMIFQdpmtsLNPYMRVGEQLMEVLM---LHKGLSKAAAFEESVRMLDAVKMP 156
Cdd:PRK13651 81 EKVLEklviqktrfkkikkikeirrRVGVVFQ-----FAEYQLFEQTIEKDIIfgpVSMGVSKEEAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 157 EARkrMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGIC 236
Cdd:PRK13651 156 ESY--LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLEWT 232
|
250 260
....*....|....*....|
gi 505807353 237 DKVLVMYAGRTMEYGQARDV 256
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDI 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-262 |
2.15e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 10 PQAAQQSGLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQT--AFALMGLLAANGHISGSATFNG 87
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrCFNRLNDLIPGFRVEGKVTFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 88 REiLNLPERDLNKLRaEQISMIFQDPmtslNPYmrvgeqlmevlmlHKGLSKAAAF---------------EESVRmlDA 152
Cdd:PRK14243 77 KN-LYAPDVDPVEVR-RRIGMVFQKP----NPF-------------PKSIYDNIAYgaringykgdmdelvERSLR--QA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 153 VKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVV 232
Cdd:PRK14243 136 ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQA 213
|
250 260 270
....*....|....*....|....*....|....*....
gi 505807353 233 AGICDKVLVMYA---------GRTMEYGQARDVFYQPSH 262
Cdd:PRK14243 214 ARVSDMTAFFNVeltegggryGYLVEFDRTEKIFNSPQQ 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-256 |
3.21e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLA-ANGHISGSATFNGREILNLPERDLNKLraeQISMIFQD 112
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSgIHEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 pmtslnpyMRVGEQL--MEVLMLHKGLSKAAAfeeSVRMLDAVKMPEARKRM------KMFPHEFSGGM----RQRVMIA 180
Cdd:PRK09700 89 --------LSVIDELtvLENLYIGRHLTKKVC---GVNIIDWREMRVRAAMMllrvglKVDLDEKVANLsishKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-256 |
8.56e-16 |
|
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: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFAL----------------MGLLAANGHIsGSA 83
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhVALCEKCGYV-ERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 84 TFNGR------EILNLPERDL----NKLRA---EQISMIFQDPMtSLNPYMRVGEQLMEVLMlHKGLSKAAAFEESVRML 150
Cdd:TIGR03269 76 SKVGEpcpvcgGTLEPEEVDFwnlsDKLRRrirKRIAIMLQRTF-ALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 151 DAVKMPEarkRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG 230
Cdd:TIGR03269 154 EMVQLSH---RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 505807353 231 VVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-256 |
9.29e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.96 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 13 AQQSGLLLDVKDLRVTfktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGllaanGHI---SGSATFNGRE 89
Cdd:PRK11831 1 EQSVANLVDMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKT-TLLRLIG-----GQIapdHGEILFDGEN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 90 ILNLPERDLNKLRaEQISMIFQDP--MTSLNPYMRVGEQLMEvlmlHKGLSkAAAFEESVRM-LDAVKMPEARKRMkmfP 166
Cdd:PRK11831 71 IPAMSRSRLYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQLP-APLLHSTVMMkLEAVGLRGAAKLM---P 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKK 221
|
250
....*....|
gi 505807353 247 TMEYGQARDV 256
Cdd:PRK11831 222 IVAHGSAQAL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-251 |
9.63e-16 |
|
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: 74.61 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGDVTA--VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNG---REILNLPERDLNKL 101
Cdd:cd03233 9 ISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGipyKEFAEKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 102 RAEQISMifqdpmtslnPYMRVgEQLMEVLMLHKGlskaaafEESVRmldavkmpearkrmkmfphEFSGGMRQRVMIAM 181
Cdd:cd03233 89 SEEDVHF----------PTLTV-RETLDFALRCKG-------NEFVR-------------------GISGGERKRVSIAE 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVA-GICDKVLVMYAGRTMEYG 251
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQIYYG 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-250 |
1.48e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 10 PQAAQQSGLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAF-ALMGLLAANghiSGSATFnGR 88
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS-TLLkLLAGELEPD---SGTVKL-GE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 89 EIlnlperdlnklraeQISMIFQDpMTSLNPYMRVGEQLMEVlmlHKGLSkaaafEESVR-MLdavkmpearKRMkMFPH 167
Cdd:COG0488 377 TV--------------KIGYFDQH-QEELDPDKTVLDELRDG---APGGT-----EQEVRgYL---------GRF-LFSG 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 E--------FSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHDLGVVAGICDK 238
Cdd:COG0488 424 DdafkpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-----LEEALDDFPGTVLLVSHDRYFLDRVATR 498
|
250
....*....|..
gi 505807353 239 VLVMYAGRTMEY 250
Cdd:COG0488 499 ILEFEDGGVREY 510
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
37-257 |
1.52e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.93 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 37 TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPerdLNKLRAEQISMIFQDPmtS 116
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD---AGNIIIDDEDISLLP---LHARARRGIGYLPQEA--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 LNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKmfpHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 197 TALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVF 257
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-260 |
1.57e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.42 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRvtfKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGHI-SGSATFNGREILNL-P-ER 96
Cdd:PRK11650 4 LKLQAVR---KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMVAGLERItSGEIWIGGRVVNELePaDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 97 DlnklraeqISMIFQDpmTSLNPYMRVgEQLMEVLMLHKGLSKAaafEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQR 176
Cdd:PRK11650 77 D--------IAMVFQN--YALYPHMSV-RENMAYGLKIRGMPKA---EIEERVAEAARILELEPLLDRKPRELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQiMTL-LNELKREFNTAIIMITHD------LGvvagicDKVLVMYAGRTME 249
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGGVAEQ 215
|
250
....*....|.
gi 505807353 250 YGQARDVFYQP 260
Cdd:PRK11650 216 IGTPVEVYEKP 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-246 |
1.79e-15 |
|
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: 74.43 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFKTPD-GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGREIlnlPERDlNK 100
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG---GQVLLDGKPI---SQYE-HK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 101 LRAEQISMIFQDPMT---SLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMfphefSGGMRQRV 177
Cdd:cd03248 85 YLHSKVSLVGQEPVLfarSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL-----SGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGR 246
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-228 |
1.86e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALM-GLLAANghiSGSATFNGREIL-----NLPE 95
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS-TLLKILaGELEPD---SGEVSIPKGLRIgylpqEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 --------------RDLNKLRAE--QISMIFQDPMTSLNPYMRVGEQlMEVLMLHKGLSKAAafeesvRMLDAVKMPEAR 159
Cdd:COG0488 73 dddltvldtvldgdAELRALEAEleELEAKLAEPDEDLERLAELQEE-FEALGGWEAEARAE------EILSGLGFPEED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 160 KRMKMfpHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtVQAqIMTLLNELKReFNTAIIMITHD 228
Cdd:COG0488 146 LDRPV--SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLKN-YPGTVLVVSHD 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
39-246 |
3.37e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.98 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGllAANGH-ISGSATFNGREIlnlperDLNKLR---AEQISMIFQDPM 114
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGRnISGTVFKDGKEV------DVSTVSdaiDAGLAYVTEDRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 115 TS-LNpymrvgeqLME------VLMLHKGLSKAAAFEESVRMLDAVkmpEARKRMKMFPH-------EFSGGMRQRVMIA 180
Cdd:NF040905 348 GYgLN--------LIDdikrniTLANLGKVSRRGVIDENEEIKVAE---EYRKKMNIKTPsvfqkvgNLSGGNQQKVVLS 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGR 481
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
34-269 |
4.77e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.07 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGHISGSATFNGREILN-LPERDLNklraeqISMIFQD 112
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGDLFIGEKRMNdVPPAERG------VGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 pmTSLNPYMRVGEQLMEVLMLhKGLSKAAA---FEESVRMLDAVKMPEARkrmkmfPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK11000 84 --YALYPHLSVAENMSFGLKL-AGAKKEEInqrVNQVAEVLQLAHLLDRK------PKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFYQPSHPYSIGLL 269
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-242 |
2.90e-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: 69.01 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafalmgllaanghisgsaTFngreiLNLperdln 99
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKS--------------------TL-----LKL------ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 klraeqismifqdpmtslnpymrvgeqLMEVLMLHKGlskaaafeeSVRMLDAVKMPearkrmkMFPHeFSGGMRQRVMI 179
Cdd:cd03221 46 ---------------------------IAGELEPDEG---------IVTWGSTVKIG-------YFEQ-LSGGEKMRLAL 81
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807353 180 AMALLCRPKLLIADEPTTALDV-TVQAqimtLLNELKrEFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03221 82 AKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALK-EYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-258 |
2.92e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.83 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 4 IEMTKAPQAAQQSGLLlDVKDLRVTFKtPDGDVTaVNDLNFNLRAGETLGIVGESGSGKSQTAfalMGLLAANGHISGSA 83
Cdd:TIGR00957 1270 IQETAPPSGWPPRGRV-EFRNYCLRYR-EDLDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEI 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 84 TFNGreiLNLPERDLNKLRAeQISMIFQDPM-------TSLNPYMRVGEQ----LMEVLMLHKGLSKAAAfeesvrMLDA 152
Cdd:TIGR00957 1344 IIDG---LNIAKIGLHDLRF-KITIIPQDPVlfsgslrMNLDPFSQYSDEevwwALELAHLKTFVSALPD------KLDH 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 153 vKMPEARKRMkmfphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTllnelkrEFNTAIIM-ITH 227
Cdd:TIGR00957 1414 -ECAEGGENL-------SVGQRQLVCLARALLRKTKILVLDEATAAVDLEtdnlIQSTIRT-------QFEDCTVLtIAH 1478
|
250 260 270
....*....|....*....|....*....|....*..
gi 505807353 228 DLGVVAGICdKVLVMYAGRTMEYG------QARDVFY 258
Cdd:TIGR00957 1479 RLNTIMDYT-RVIVLDKGEVAEFGapsnllQQRGIFY 1514
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
42-251 |
4.52e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.23 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLNKLraeqISMIFQDPMT------ 115
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE---RGRILIDGCDISKFGLMDLRKV----LGIIPQAPVLfsgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 116 -SLNPYMRVGE-QLMEVLmlhkglsKAAAFEESVRM----LDAvKMPEARKrmkmfphEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PLN03130 1331 fNLDPFNEHNDaDLWESL-------ERAHLKDVIRRnslgLDA-EVSEAGE-------NFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 190 LIADEPTTALDVTVQAQIMTLLNElkrEFNT-AIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIRE---EFKScTMLIIAHRLNTIID-CDRILVLDAGRVVEFD 1454
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
38-245 |
4.81e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.20 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGREILNLPE--RDLNKLRAeQISMIFQdpmt 115
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRlaRDIRKSRA-NTGYIFQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 116 SLNPYMRVgeQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEA-----RKRMKMFPHE----FSGGMRQRVMIAMALLCR 186
Cdd:PRK09984 94 QFNLVNRL--SVLENVLI-GALGSTPFWRTCFSWFTREQKQRAlqaltRVGMVHFAHQrvstLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 187 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-249 |
1.13e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.36 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 14 QQSGLLLDVKDlrVTFKTpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNL 93
Cdd:PRK10247 2 QENSPLLQLQN--VGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT---SGTLLFEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 -PERdlnklRAEQISMIFQDPMTslnpymrVGEQLMEVLMLHKGLSKAAAFEES-VRMLDAVKMPEA--RKRMkmfpHEF 169
Cdd:PRK10247 75 kPEI-----YRQQVSYCAQTPTL-------FGDTVYDNLIFPWQIRNQQPDPAIfLDDLERFALPDTilTKNI----AEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVM--YAGRT 247
Cdd:PRK10247 139 SGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLqpHAGEM 217
|
..
gi 505807353 248 ME 249
Cdd:PRK10247 218 QE 219
|
|
| 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 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREIlnlpERDLNKLRAEQISMIFQDP 113
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHI----QHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 MTSLNpyMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:PRK10253 91 TTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-246 |
4.85e-13 |
|
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: 70.43 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFKtPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlnlpERDLNKL 101
Cdd:TIGR01257 931 VKNLVKIFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT---SGTVLVGGKDI----ETNLDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 102 RaEQISMIFQDPMtsLNPYMRVGEQLMEVLMLhKGLSKAAAFEESVRMLDAVKMPEARKRMKmfpHEFSGGMRQRVMIAM 181
Cdd:TIGR01257 1002 R-QSLGMCPQHNI--LFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEEA---QDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-256 |
8.76e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 68.76 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLrvTFKTPDGDV-TAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANG---HISGSATFNGreilnlperd 97
Cdd:PRK13545 24 LKDL--FFRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKgtvDIKGSAALIA---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 lnklraeqISMIFQDPMTslnpymrvGEQLMEVLMLHKGLSKAAAFEESVRMLDavkMPEARKRMKMFPHEFSGGMRQRV 177
Cdd:PRK13545 92 --------ISSGLNGQLT--------GIENIELKGLMMGLTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK13545 153 GFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-246 |
9.01e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlnlperdlnklraeqismifqDP 113
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPV---------------------DA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mTSLNPYMRVG---------EQL--MEVLMLHKGL------SKAAAFEESVR--MLDAVkmpearkrMKMFPHEFSGGMR 174
Cdd:NF033858 333 -GDIATRRRVGymsqafslyGELtvRQNLELHARLfhlpaaEIAARVAEMLErfDLADV--------ADALPDSLPLGIR 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:NF033858 404 QRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMN-EAERCDRISLMHAGR 474
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-246 |
9.40e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 66.34 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTPDGDVTAV-NDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAangHISGSATFNGRE--------I 90
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPGSIayvsqepwI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 91 LNLPERDlnklraeqiSMIFQDPMtslNPymrvgEQLMEVLmlhkglsKAAAFEEsvrmlDavkmpearkrMKMFPH--- 167
Cdd:cd03250 78 QNGTIRE---------NILFGKPF---DE-----ERYEKVI-------KACALEP-----D----------LEILPDgdl 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 168 ----E----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT--LLNELKRefNTAIIMITHDLGVVAgICD 237
Cdd:cd03250 119 teigEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLP-HAD 195
|
....*....
gi 505807353 238 KVLVMYAGR 246
Cdd:cd03250 196 QIVVLDNGR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-232 |
9.49e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLL--AANGHISGSATFNGREIlNLperd 97
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLydPTEGDIIINDSHNLKDI-NL---- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 98 lnKLRAEQISMIFQDPMT--------------SLNPYMRVGEQLME-VLMLHKGLSK--------AAAFEESVRMLDAVK 154
Cdd:PTZ00265 456 --KWWRSKIGVVSQDPLLfsnsiknnikyslySLKDLEALSNYYNEdGNDSQENKNKrnscrakcAGDLNDMSNTTDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 155 MPEARKRM-------------KMFPHEF-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 202
Cdd:PTZ00265 534 LIEMRKNYqtikdsevvdvskKVLIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270
....*....|....*....|....*....|
gi 505807353 203 VQAQIMTLLNELKREFNTAIIMITHDLGVV 232
Cdd:PTZ00265 614 SEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
9-274 |
1.02e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 9 APQAAQQSGLLLDVKDLRVTfktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGR 88
Cdd:PTZ00243 1300 APHPVQAGSLVFEGVQMRYR----EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCG---GEIRVNGR 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 89 EILNLPERDLNKlraeQISMIFQDPM-------TSLNPYMRvgeqlmevlmlhkglskaAAFEESVRMLDAVKMPE---- 157
Cdd:PTZ00243 1373 EIGAYGLRELRR----QFSMIPQDPVlfdgtvrQNVDPFLE------------------ASSAEVWAALELVGLRErvas 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 158 ----ARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLI-ADEPTT----ALDVTVQAQIMTLLNelkrefNTAIIMITHD 228
Cdd:PTZ00243 1431 esegIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHR 1504
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 505807353 229 LGVVAGiCDKVLVMYAGRTMEYGQARDVFYQPSHPYSiGLLNAVPR 274
Cdd:PTZ00243 1505 LHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNRQSIFH-SMVEALGR 1548
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-260 |
1.17e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 28 TFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGHIS-GSATFNGreiLNLPERDLNKLRAE-- 104
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSeGDIRFHD---IPLTKLQLDSWRSRla 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 105 ---QISMIFQDPMTSlNpymrvgeqlmevLMLHKGLSKAAAFEESVRML----DAVKMP-----EARKRMKMFphefSGG 172
Cdd:PRK10789 393 vvsQTPFLFSDTVAN-N------------IALGRPDATQQEIEHVARLAsvhdDILRLPqgydtEVGERGVML----SGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGQ 252
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
....*...
gi 505807353 253 ARDVFYQP 260
Cdd:PRK10789 533 HDQLAQQS 540
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
42-250 |
1.40e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLNKLraeqISMIFQDPMT------ 115
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE---KGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVLfsgtvr 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 116 -SLNPYMRVGEqlmevlmlhKGLSKAAafeESVRMLDAVKMPEARKRMKMFP--HEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PLN03232 1328 fNIDPFSEHND---------ADLWEAL---ERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 193 DEPTTALDVTVQAQIMTLLNElkrEFNT-AIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE---EFKScTMLVIAHRLNTIID-CDKILVLSSGQVLEY 1450
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-256 |
1.74e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 27 VTFKTPDGdvTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANGhiSGSATFNGREILNLPerdlNKLRAEQI 106
Cdd:PRK10575 17 VSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRHQPPS--EGEILLDAQPLESWS----SKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 107 SMIFQ-----DPMTsLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDavkmpearkrMKMFPHEF----SGGMRQRV 177
Cdd:PRK10575 88 AYLPQqlpaaEGMT-VRELVAIGRYPWHGALGRFGAADREKVEEAISLVG----------LKPLAHRLvdslSGGERQRA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-246 |
1.79e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 36 VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDlnKLRAeQISMIFQDpmT 115
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD---AGSILIDGQEMRFASTTA--ALAA-GVAIIYQE--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 116 SLNPYMRVGEQLMEVLMLHKG--LSKAAAFEESVRMLDAVKM---PEARKRmkmfphEFSGGMRQRVMIAMALLcRPKLL 190
Cdd:PRK11288 89 HLVPEMTVAENLYLGQLPHKGgiVNRRLLNYEAREQLEHLGVdidPDTPLK------YLSIGQRQMVEIAKALA-RNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 191 IA-DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11288 162 IAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
39-262 |
3.19e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 39 VNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL----AANG-HISGSATFNGREILNLPERDLNKLRA-----EQISM 108
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGaRVTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 109 IFQ-DPMTSLNPYMrvgeqlmevlmlHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAMAL---- 183
Cdd:PRK13547 97 AFSaREIVLLGRYP------------HARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 184 -----LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDVFy 258
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL- 243
|
....
gi 505807353 259 QPSH 262
Cdd:PRK13547 244 TPAH 247
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-245 |
6.92e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 36 VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREilnlpeRDLNKLRAEQ---ISMIFQD 112
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD---AGSILYLGKE------VTFNGPKSSQeagIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 pmtsLN--PYMRVGEQLM---EVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKmfpHEFSGGMRQRVMIAMALLCRP 187
Cdd:PRK10762 88 ----LNliPQLTIAENIFlgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLV---GELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 188 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-242 |
7.75e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 37 TAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAanghisgsatfngREILNLPERDLNKLRAEQISmifqdpmts 116
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLLA-------------GALKGTPVAGCVDVPDNQFG--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 lnpymrvgeqlmEVLMLHKGLSKAAAFEESVRMLDAVKMPEA---RKRmkmfPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:COG2401 98 ------------REASLIDAIGRKGDFKDAVELLNAVGLSDAvlwLRR----FKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505807353 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 |
1.28e-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: 65.54 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 31 TPDGDVTaVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAAnghisgsaTFNGReiLNLPERdlNKlraeqismIF 110
Cdd:TIGR00954 461 TPNGDVL-IESLSFEVPSGNNLLICGPNGCGKS-SLFRILGELWP--------VYGGR--LTKPAK--GK--------LF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 111 QDPMtslNPYMRVG---EQL---MEVL-MLHKGLSKAaafeESVRMLDAVKMPEARKR------MKMFPHEFSGGMRQRV 177
Cdd:TIGR00954 519 YVPQ---RPYMTLGtlrDQIiypDSSEdMKRRGLSDK----DLEQILDNVQLTHILEReggwsaVQDWMDVLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITH 227
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-241 |
1.67e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTPDgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALM----------------------------- 70
Cdd:PTZ00265 1166 IEIMDVNFRYISRP-NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 71 ------GLLAAN--------GHISGSATF-NGREIL----NLPERDLNKLRaEQISMIFQDPM---TSLNPYMRVGEQ-- 126
Cdd:PTZ00265 1245 deeqnvGMKNVNefsltkegGSGEDSTVFkNSGKILldgvDICDYNLKDLR-NLFSIVSQEPMlfnMSIYENIKFGKEda 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 127 -LMEVlmlhKGLSKAAAFEESVRMLDAvkmpEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 205
Cdd:PTZ00265 1324 tREDV----KRACKFAAIDEFIESLPN----KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
250 260 270
....*....|....*....|....*....|....*.
gi 505807353 206 QIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLV 241
Cdd:PTZ00265 1396 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-251 |
6.13e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.73 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANgHISGSATFNGREILNLPERDl 98
Cdd:PRK09580 1 MLSIKDLHVSVE----DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE-VTGGTVEFKGKDLLELSPED- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 nklRA-EQISMIFQDPM------------TSLNPYMRVGEQlmEVLmlhKGLSKAAAFEESVRMLdavKMPEARkRMKMF 165
Cdd:PRK09580 75 ---RAgEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPL---DRFDFQDLMEEKIALL---KMPEDL-LTRSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 166 PHEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGI-CDKVLVMY 243
Cdd:PRK09580 143 NVGFSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVLY 220
|
....*...
gi 505807353 244 AGRTMEYG 251
Cdd:PRK09580 221 QGRIVKSG 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-246 |
2.39e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 43 NFNLRAGETLGIVGESGSGKSQtafaLMGLL-AANGHISGSATFNGREILNLPERDlnKLRAeQISMIFQD-------PM 114
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSE----LMKLLyGATRRTAGQVYLDGKPIDIRSPRD--AIRA-GIMLCPEDrkaegiiPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 115 TS----LNPYMRvGEQLMEVLMLHKGLSKAAAfEESVRMLdAVKMPEARKRMkMFpheFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK11288 346 HSvadnINISAR-RHHLRAGCLINNRWEAENA-DRFIRSL-NIKTPSREQLI-MN---LSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 191 IADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-259 |
4.04e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPERDLN 99
Cdd:PRK10790 341 IDIDNVSFAYRD---DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT---EGEIRLDGRPLSSLSHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KlraeQISMIFQDPMTslnpymrVGEQLMEVLMLHKGLSKAAAFE--ESVRMLDAVK-MPEA-RKRMKMFPHEFSGGMRQ 175
Cdd:PRK10790 415 Q----GVAMVQQDPVV-------LADTFLANVTLGRDISEEQVWQalETVQLAELARsLPDGlYTPLGEQGNNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG---- 251
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGthqq 560
|
250
....*....|
gi 505807353 252 --QARDVFYQ 259
Cdd:PRK10790 561 llAAQGRYWQ 570
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
34-249 |
5.21e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFAlmgllaanGHISGSATfnGREILNLPERDLNKlRAEQISMIFQDP 113
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP--------AHV*GPDA--GRRPWRF*TWCANR-RALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 MTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMfphEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807353 194 EPTTALDVTVQAQIMTLLNELKREFNTAII---------MITHDLGVV-------AGICDKVLVMYAGRTME 249
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLttqymeeaeQLAHELTVIdrgrviaDGKVDELKTKVGGRTLQ 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-245 |
8.01e-10 |
|
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: 60.41 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 38 AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIL-NLPERDLNKLRAEQISMIfQDPMTS 116
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVT---SGDATVAGKSILtNISDVHQNMGYCPQFDAI-DDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 117 lnpymrvgeqlMEVLMLHKGLSKAAAfEESVRMLD-AVKMPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:TIGR01257 2030 -----------REHLYLYARLRGVPA-EEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505807353 196 TTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
42-232 |
1.60e-09 |
|
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: 56.98 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHISgsatFNGREILNLPErdlnkLRAEQISMIFQDPmtSLNPY 120
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrPDSGEVR----WNGTPLAEQRD-----EPHENILYLGHLP--GLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 121 MRVGEQLMEVLMLHKGLSKAA--AFEEsVRMLDAVKMPearkrmkmfPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 198
Cdd:TIGR01189 88 LSALENLHFWAAIHGGAQRTIedALAA-VGLTGFEDLP---------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 505807353 199 LDVTVQAQIMTLLNE-LKRefNTAIIMITH-DLGVV 232
Cdd:TIGR01189 158 LDKAGVALLAGLLRAhLAR--GGIVLLTTHqDLGLV 191
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-261 |
3.15e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.61 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 47 RAGETLGIVGESGSGKSQTAFALMGLLAAN-GHISGSAT-------FNGREILNLperdLNKLRAEQISMIFQDPMTSLN 118
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNlGKFDDPPDwdeildeFRGSELQNY----FTKLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 119 PYMRVGEqlmeVLMLHKGLSKAAAFEESVRMLdavkmpEARKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 198
Cdd:cd03236 100 PKAVKGK----VGELLKKKDERGKLDELVDQL------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807353 199 LDVTVQAQIMTLLNELKREFNtAIIMITHDLGVVAGICDKVLVMYaGRTMEYGqardVFYQPS 261
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY-GEPGAYG----VVTLPK 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-262 |
4.35e-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: 56.40 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLrvTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISgsatFNGREILNLPerdLN 99
Cdd:cd03289 3 MTVKDL--TAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQ----IDGVSWNSVP---LQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 100 KLRAE-----QISMIFQDPM-TSLNPYMRVGEqlmevlmlhkglskaaafEESVRMLDAVKMpeaRKRMKMFPHE----- 168
Cdd:cd03289 74 KWRKAfgvipQKVFIFSGTFrKNLDPYGKWSD------------------EEIWKVAEEVGL---KSVIEQFPGQldfvl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 169 ------FSGGMRQRVMIAMALLCRPKLLIADEPTTALD-VTVQaqimTLLNELKREFNT-AIIMITHDLGVVAGiCDKVL 240
Cdd:cd03289 133 vdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ----VIRKTLKQAFADcTVILSEHRIEAMLE-CQRFL 207
|
250 260
....*....|....*....|..
gi 505807353 241 VMYAGRTMEYGQARDVFYQPSH 262
Cdd:cd03289 208 VIEENKVRQYDSIQKLLNEKSH 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-228 |
4.47e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAANGHISgsatfNGREILnlpERDLNKLRAEQ-------- 105
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILNGEVLLD-----DGRIIY---EQDLIVARLQQdpprnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 106 -----ISMIFQDPMTSLNPYMRVGEQLMEVLMlHKGLSKAAAFEESVRMLDAVKMpEAR-----KRMKMFPH----EFSG 171
Cdd:PRK11147 82 tvydfVAEGIEEQAEYLKRYHDISHLVETDPS-EKNLNELAKLQEQLDHHNLWQL-ENRinevlAQLGLDPDaalsSLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKrEFNTAIIMITHD 228
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLK-TFQGSIIFISHD 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
34-246 |
8.37e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLPErdlNKLRAEQISMIFQdp 113
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT---SGRIVFDGKDITDWQT---AKIMREAVAIVPE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 mtslnpymrvGEQLMEVLMLHKGLSKAAAFEESVRMLDAVK-----MPEARKRMKMFPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK11614 88 ----------GRRVFSRMTVEENLAMGGFFAERDQFQERIKwvyelFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGH 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
49-250 |
8.68e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 49 GETLGIVGESGSGKSQTAFALMGLLAANGhisGSATFNGREILNLPERDLNKLRAEQISMIFQDPmtslnpymRVGEQLM 128
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADG---GSYTFPGNWQLAWVNQETPALPQPALEYVIDGD--------REYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 129 EVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKMFPH--------------EFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10636 96 AQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHglgfsneqlerpvsDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 195 PTTALDvtVQAQIMtlLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:PRK10636 176 PTNHLD--LDAVIW--LEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
42-266 |
1.52e-08 |
|
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: 54.91 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPerdLNKLRAeQISMIFQDPMT------ 115
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI---FDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILfsgsir 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 116 -SLNPYMRVGEQlmevlmlhkglskaaafeesvRMLDAVKMPEARKRMKMFP-----------HEFSGGMRQRVMIAMAL 183
Cdd:cd03288 113 fNLDPECKCTDD---------------------RLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 184 LCRPKLLIADEPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGQARDVFYQ 259
Cdd:cd03288 172 VRKSSILIMDEATASIDMAteniLQKVVMTAFAD------RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
....*..
gi 505807353 260 PSHPYSI 266
Cdd:cd03288 245 EDGVFAS 251
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-262 |
1.57e-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: 56.07 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 16 SGLLLDVKDLRVTFkTPDGDvTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISgsatFNGreiLNLPE 95
Cdd:TIGR01271 1214 SGGQMDVQGLTAKY-TEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQ----IDG---VSWNS 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 96 RDLNKLRAE-----QISMIFQDPM-TSLNPYMRVGEqlmevlmlhkglskaaafEESVRMLDAVKMpeaRKRMKMFPHE- 168
Cdd:TIGR01271 1285 VTLQTWRKAfgvipQKVFIFSGTFrKNLDPYEQWSD------------------EEIWKVAEEVGL---KSVIEQFPDKl 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 169 ----------FSGGMRQRVMIAMALLCRPKLLIADEPTTALD-VTVQaqimTLLNELKREF-NTAIIMITHDLGVVAGiC 236
Cdd:TIGR01271 1344 dfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ----IIRKTLKQSFsNCTVILSEHRVEALLE-C 1418
|
250 260
....*....|....*....|....*.
gi 505807353 237 DKVLVMYAGRTMEYGQARDVFYQPSH 262
Cdd:TIGR01271 1419 QQFLVIEGSSVKQYDSIQKLLNETSL 1444
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-256 |
1.70e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRVTFKTpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGreilnlperdlnkl 101
Cdd:PRK13546 24 MKDALIPKHK-NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPT---VGKVDRNG-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 102 raeQISMIFQDpmTSLNPYMrVGEQLMEVLMLHKGLSKAaafEESVRMLDAVKMPEARKRMKMFPHEFSGGMRQRVMIAM 181
Cdd:PRK13546 86 ---EVSVIAIS--AGLSGQL-TGIENIEFKMLCMGFKRK---EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGQARDV 256
Cdd:PRK13546 157 NITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-214 |
1.72e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.79 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 17 GLLLDVKDLRVTFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqtafALMGLLAAN---GHISGSATFNGReilnl 93
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKT----TLLDVLAGRktaGVITGEILINGR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 94 pERDLNKLR----AEQismifqdpMTSLNPYMRVGEQLMEVLMLhKGLSkaaafeesvrmldavkmPEARKrmkmfphef 169
Cdd:cd03232 72 -PLDKNFQRstgyVEQ--------QDVHSPNLTVREALRFSALL-RGLS-----------------VEQRK--------- 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505807353 170 sggmrqRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNEL 214
Cdd:cd03232 116 ------RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-217 |
6.14e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 43 NFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDLNKLraeqISMIFQDPMTSLnpyMR 122
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPL---LSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNTDM---LS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 123 VGEQ-----LMEVLMLHkgLSKAAAFEESVRMLDAVKMPEARkrmkmFPHeFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:PRK10938 93 PGEDdtgrtTAEIIQDE--VKDPARCEQLAQQFGITALLDRR-----FKY-LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|
gi 505807353 198 ALDVTVQAQIMTLLNELKRE 217
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQS 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
49-231 |
6.50e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 49 GETLGIVGESGSGKSQTAFALMGLLAANGHisgsatfngreilnlperdlnklraeqiSMIFQDpmtslnpymrvGEQLM 128
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGG----------------------------GVIYID-----------GEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 129 EVLMLHKGLskaaafeesvrmldavkmpearKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM 208
Cdd:smart00382 43 EEVLDQLLL----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180
....*....|....*....|....*...
gi 505807353 209 -----TLLNELKREFNTAIIMITHDLGV 231
Cdd:smart00382 101 lleelRLLLLLKSEKNLTVILTTNDEKD 128
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
35-229 |
9.93e-08 |
|
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: 51.95 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 35 DVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAAnghISGSATFNGREILNLPERDLNKLRAEQISMIFQDP- 113
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT---LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 114 ---------MTSLNPYMRvgeqlmevlMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKmfphEFSGGMRQRVMIAMALL 184
Cdd:cd03290 90 llnatveenITFGSPFNK---------QRYKAVTDACSLQPDIDLLPFGDQTEIGERGI----NLSGGQRQRICVARALY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505807353 185 CRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 229
Cdd:cd03290 157 QNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
49-234 |
1.18e-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: 53.02 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 49 GETLGIVGESGSGKSqTAFALM-------------------GLLAANGHISGSATFngREILNLPERDLNKL--RAEQIS 107
Cdd:TIGR03719 31 GAKIGVLGLNGAGKS-TLLRIMagvdkdfngearpqpgikvGYLPQEPQLDPTKTV--RENVEEGVAEIKDAldRFNEIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 108 MIFQDPMTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEesvRMLDAVKMPEARKRMKmfphEFSGGMRQRVMIAMALLCRP 187
Cdd:TIGR03719 108 AKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLE---IAMDALRCPPWDADVT----KLSGGERRRVALCRLLLSKP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505807353 188 KLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 234
Cdd:TIGR03719 181 DMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHDryfLDNVAG 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-232 |
1.22e-07 |
|
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: 51.34 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 42 LNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHISgsatfngreilnLPERDLNKLRAE-QISMIFQDPMTSLNP 119
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVL------------LNGGPLDFQRDSiARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 120 YMRVGEQLMevlMLHKGLSKAAAFEESVRM-LDAVKMPEArkrmkmfpHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 198
Cdd:cd03231 87 TLSVLENLR---FWHADHSDEQVEEALARVgLNGFEDRPV--------AQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|....*
gi 505807353 199 LDVTVQAQIMTLLNElKREFNTAIIMITH-DLGVV 232
Cdd:cd03231 156 LDKAGVARFAEAMAG-HCARGGMVVLTTHqDLGLS 189
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-228 |
1.64e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 34 GDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGHISGSatfNGREILNLPERDLNKLRAEQISMifqD 112
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPvSGEIGLA---KGIKLGYFAQHQLEFLRADESPL---Q 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 113 PMTSLNPymRVGEQLMEVLMLHKGLSKaaafeesvrmlDAVKMPEARkrmkmfpheFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PRK10636 397 HLARLAP--QELEQKLRDYLGGFGFQG-----------DKVTEETRR---------FSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190
....*....|....*....|....*....|....*..
gi 505807353 193 DEPTTALDVTV-QAqimtlLNELKREFNTAIIMITHD 228
Cdd:PRK10636 455 DEPTNHLDLDMrQA-----LTEALIDFEGALVVVSHD 486
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-265 |
2.02e-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: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 46 LRAGETLGIVGESGSGKSQTAFALMGLLAAN-GHISGSAT-------FNGREILNLperdLNKLRAEQISmifqdpmTSL 117
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNlGDYDEEPSwdevlkrFRGTELQDY----FKKLANGEIK-------VAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 118 NPymrvgeQLMEVL-MLHKG-----LSKA---AAFEESVRMLDAVKMPEARKRmkmfphEFSGGMRQRVMIAMALLCRPK 188
Cdd:COG1245 165 KP------QYVDLIpKVFKGtvrelLEKVderGKLDELAEKLGLENILDRDIS------ELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYaGRTMEYGqardVFyqpSHPYS 265
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY-GEPGVYG----VV---SKPKS 300
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-228 |
2.45e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 17 GLLLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFA-LMGLLAANghiSGSATF---------- 85
Cdd:TIGR03719 320 DKVIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKS-TLFRmITGQEQPD---SGTIEIgetvklayvd 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 86 NGREILnlperDLNKLRAEQISmifqdpmtSLNPYMRVGEQLMEvlmlhkglSKA--AAFeesvrmldAVKMPEARKRMK 163
Cdd:TIGR03719 392 QSRDAL-----DPNKTVWEEIS--------GGLDIIKLGKREIP--------SRAyvGRF--------NFKGSDQQKKVG 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 164 mfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 228
Cdd:TIGR03719 443 ----QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD 499
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-241 |
2.48e-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: 52.09 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 46 LRAGETLGIVGESGSGKsqTAFA--LMGLLAANghiSGSATFNGReILNLP---ERDLNKLRAEQISMIFQDPMTSlnPY 120
Cdd:COG1245 363 IREGEVLGIVGPNGIGK--TTFAkiLAGVLKPD---EGEVDEDLK-ISYKPqyiSPDYDGTVEEFLRSANTDDFGS--SY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 121 MRvgEQLMEVLMLHkglskaaafeesvRMLDavkmpearKRMKmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:COG1245 435 YK--TEIIKPLGLE-------------KLLD--------KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505807353 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 241
Cdd:COG1245 488 VEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-265 |
3.23e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 46 LRAGETLGIVGESGSGKSQTAFALMGLLAAN-GHISGSAT-------FNGREILNLPERdL--NKLRA-------EQISM 108
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlGDYEEEPSwdevlkrFRGTELQNYFKK-LynGEIKVvhkpqyvDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 109 IFQDpmtslnpymRVGEQLMEVlmlhkglSKAAAFEESVRMLDAVKMPEarKRMKmfphEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK13409 175 VFKG---------KVRELLKKV-------DERGKLDEVVERLGLENILD--RDIS----ELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 189 LLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYaGRTMEYGqardVFyqpSHPYS 265
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY-GEPGAYG----VV---SKPKG 299
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
36-246 |
4.15e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 36 VTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlnlpERDLNKLRAEQ-ISMIFQDpm 114
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEI----DFKSSKEALENgISMVHQE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 115 tsLNPYMRVgeQLMEVLMLHKgLSKAAAFEESVRMLDAVKMPEARKRMKMFPHE----FSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK10982 82 --LNLVLQR--SVMDNMWLGR-YPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 191 IADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-253 |
4.36e-07 |
|
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: 50.10 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 45 NLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSatfngreilnlpERDLNKLRAEQISMIFQdpmtslnpyMRVG 124
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------------ELDTVSYKPQYIKADYE---------GTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 125 EQLMEVLmlhKGLSKAAAFEESVrmLDAVKMpeaRKRMKMFPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ 204
Cdd:cd03237 80 DLLSSIT---KDFYTHPYFKTEI--AKPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505807353 205 AQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVmYAGRTMEYGQA 253
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEGEPSVNGVA 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-241 |
4.45e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 7 TKAPQAAQQSGLLLDVKDLRVTFKtpdgdvtavndlNFNL-------RAGETLGIVGESGSGKSQTAFALMGLLAANghi 79
Cdd:PRK13409 328 ERPPRDESERETLVEYPDLTKKLG------------DFSLeveggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPD--- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 80 SGSatfngreilnlperdlnklraeqismIFQDPMTSLNP-YMRVgEQLMEVLMLhkgLSKAAA-------FEESVRMLD 151
Cdd:PRK13409 393 EGE--------------------------VDPELKISYKPqYIKP-DYDGTVEDL---LRSITDdlgssyyKSEIIKPLQ 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 152 AVKMPEarKRMKmfphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGV 231
Cdd:PRK13409 443 LERLLD--KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYM 516
|
250
....*....|
gi 505807353 232 VAGICDKVLV 241
Cdd:PRK13409 517 IDYISDRLMV 526
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
170-253 |
4.58e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFN-TAIIMI------THDLgvvagiCDKVLVM 242
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIyqcsqdAYEL------FDKVIVL 284
|
90
....*....|.
gi 505807353 243 YAGRTMEYGQA 253
Cdd:TIGR00956 285 YEGYQIYFGPA 295
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-231 |
9.76e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.72 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTfktpDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHISgsatFNGREIlnlperDL 98
Cdd:PRK13539 3 LEGEDLACV----RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLpPAAGTIK----LDGGDI------DD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRaEQISMI-FQDPMtslNPYMRVGEQLmevlmlhkglskaaAFEESVRMLDAVKMPEARKRMKMFP------HEFSG 171
Cdd:PRK13539 69 PDVA-EACHYLgHRNAM---KPALTVAENL--------------EFWAAFLGGEELDIAAALEAVGLAPlahlpfGYLSA 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807353 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITH-DLGV 231
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-227 |
3.00e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.25 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFKtpdgDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlnlpERDL 98
Cdd:PRK13540 1 MLDVIELDFDYH----DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE---KGEILFERQSI----KKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NklrAEQISMIFQDPMTSLNPYMRVGEQLMevLMLHKGlSKAAAFEESVRMLDAVKMPEarkrmkmFP-HEFSGGMRQRV 177
Cdd:PRK13540 70 C---TYQKQLCFVGHRSGINPYLTLRENCL--YDIHFS-PGAVGITELCRLFSLEHLID-------YPcGLLSSGQKRQV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505807353 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITH 227
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
41-251 |
3.40e-06 |
|
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: 47.93 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMG-LLAANGHI--SGSATFngreilnlperdlnklrAEQISMIFqdPMTsl 117
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKIkhSGRISF-----------------SSQFSWIM--PGT-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 118 npymrVGEQLMEVLML----HKGLSKAAAFEEsvrmlDAVKMPEARKR-MKMFPHEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:cd03291 114 -----IKENIIFGVSYdeyrYKSVVKACQLEE-----DITKFPEKDNTvLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 193 DEPTTALDVTVQAQIMTLLnELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYG 251
Cdd:cd03291 184 DSPFGYLDVFTEKEIFESC-VCKLMANKTRILVTSKMEHLK-KADKILILHEGSSYFYG 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
41-234 |
3.61e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.11 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 41 DLNFNLRAGETLGIVGESGSGKSQTAFALMGLL-AANGHISgsatFNGREIlnlperdlNKLRAEqismiFQDPM----- 114
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLArPDAGEVL----WQGEPI--------RRQRDE-----YHQDLlylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 115 -----TSLNPYmrvgEQLMEVLMLHKGLSKAAAFEesvrMLDAVKMpeaRKRMKMFPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK13538 82 qpgikTELTAL----ENLRFYQRLHGPGDDEALWE----ALAQVGL---AGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505807353 190 LIADEPTTALDVTVQAQIMTLLNE-LKRefNTAIIMITH-DLGVVAG 234
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQ--GGMVILTTHqDLPVASD 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
54-228 |
3.99e-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: 46.83 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 54 IVGESGSGKSQT----AFALMGLLAAN---GHISGSATFNGREILnlperdlnklraeQISMIFQDPMTSLNPYMRVGEQ 126
Cdd:cd03240 27 IVGQNGAGKTTIiealKYALTGELPPNskgGAHDPKLIREGEVRA-------------QVKLAFENANGKKYTITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 127 LMEVLMLHKGLSKAAAFEEsvrmldavkmpeaRKRMkmfphefSGGMRQ------RVMIAMALLCRPKLLIADEPTTALD 200
Cdd:cd03240 94 LENVIFCHQGESNWPLLDM-------------RGRC-------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180
....*....|....*....|....*....
gi 505807353 201 V-TVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:cd03240 154 EeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-112 |
4.88e-06 |
|
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: 47.87 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 20 LDVKDLRVTFKTPDGDVT-AVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREIlnlPERDL 98
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE---SGEILLDGQPV---TADNR 401
|
90
....*....|....
gi 505807353 99 NKLRaEQISMIFQD 112
Cdd:COG4615 402 EAYR-QLFSAVFSD 414
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-251 |
5.91e-06 |
|
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: 48.02 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 28 TFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMG---LLAANGHISGSATFngreilnLPERDLNKLRAE 104
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAemdKVEGHVHMKGSVAY-------VPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 105 QISMIFQDPMTSlnPYMRvgeQLMEvlmlhkglskAAAFEESVRMLDAVKMPE-ARKRMKMfphefSGGMRQRVMIAMAL 183
Cdd:TIGR00957 716 RENILFGKALNE--KYYQ---QVLE----------ACALLPDLEILPSGDRTEiGEKGVNL-----SGGQKQRVSLARAV 775
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 184 LCRPKLLIADEPTTALDVTVQAQI-------MTLLNELKRefntaiIMITHDLGVVAGIcDKVLVMYAGRTMEYG 251
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIfehvigpEGVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-245 |
6.46e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 19 LLDVKDLRVTFktpdGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANghiSGSATFNGREILNLperdl 98
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGNPCARL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 99 NKLRAEQ--ISMIFQDPMtsLNPYMRVGEQLMevlmlhKGLSKAAAFEEsvRMLDAVKMPEARKRMKMFPHEFSGGMRQR 176
Cdd:PRK15439 79 TPAKAHQlgIYLVPQEPL--LFPNLSVKENIL------FGLPKRQASMQ--KMKQLLAALGCQLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807353 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
147-253 |
1.54e-05 |
|
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: 44.87 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 147 VRMLDAVKMPEA------RKRMKMFPH--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREF 218
Cdd:cd03222 42 VKILAGQLIPNGdndewdGITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
90 100 110
....*....|....*....|....*....|....*
gi 505807353 219 NTAIIMITHDLGVVAGICDKVLVMYaGRTMEYGQA 253
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGIA 155
|
|
| 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 505807353 170 SGGMRQRVMIAMALLCR---PKLLIADEPTTAL---DVtvqAQIMTLLNELKREFNTaIIMITHDLGVV 232
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGNT-VVVIEHNLDVI 895
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
170-233 |
2.81e-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: 2.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 170 SGGMRQRVMIAMAL-LCRPK---LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVA 233
Cdd:cd03227 79 SGGEKELSALALILaLASLKprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAE 145
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
32-231 |
3.20e-05 |
|
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: 43.85 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 32 PDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGHISGSATFNGREILNLperdlNKLRAeqismifq 111
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKLIFI-----DQLQF-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 112 dpMTSLN-PYMRVGeQLMEVLmlhkglskaaafeesvrmldavkmpearkrmkmfphefSGGMRQRVMIAMALLCRPK-- 188
Cdd:cd03238 71 --LIDVGlGYLTLG-QKLSTL--------------------------------------SGGELQRVKLASELFSEPPgt 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505807353 189 LLIADEPTTALDvtvQAQIMTLLNELKR---EFNTaIIMITHDLGV 231
Cdd:cd03238 110 LFILDEPSTGLH---QQDINQLLEVIKGlidLGNT-VILIEHNLDV 151
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
170-246 |
5.25e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 5.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLnelkrEFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-251 |
6.29e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 32 PDGDVTAVNDLNFNLRAGETLGIVGESGSGKSQTAFALMGLLAANGhiSGSATFNGReILNLPerdlnklraeQISMIF- 110
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS--DASVVIRGT-VAYVP----------QVSWIFn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 111 ---QDPMTSLNPYMRVG-EQLMEVLMLHKGLSkaaafeesvrMLDAVKMPEARKRMKmfphEFSGGMRQRVMIAMALLCR 186
Cdd:PLN03130 693 atvRDNILFGSPFDPERyERAIDVTALQHDLD----------LLPGGDLTEIGERGV----NISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807353 187 PKLLIADEPTTALDVTVQAQIMTllNELKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYG 251
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
170-234 |
6.32e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 6.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 234
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHDryfLDNVAG 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
170-228 |
1.36e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 1.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 170 SGGMRQRVMIAmALLCRP-KLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 228
Cdd:PRK11147 442 SGGERNRLLLA-RLFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-201 |
1.43e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 22 VKDLRV-TFKTPDGDVTAVNDLNFNLRAGETLGIVGESGSGKSqTAFALMGLLAANG--------HIS----GSATFNGR 88
Cdd:PLN03073 175 IKDIHMeNFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKT-TFLRYMAMHAIDGipkncqilHVEqevvGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807353 89 EILNLP-ERdlNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGLSKAAAFEESVRMLDAVKMPEARKRMKM--- 164
Cdd:PLN03073 254 CVLNTDiER--TQLLEEEAQLVAQQ--RELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASila 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505807353 165 ---FPHE--------FSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 201
Cdd:PLN03073 330 glsFTPEmqvkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
170-217 |
6.27e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 6.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 505807353 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRE 217
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
159-229 |
6.46e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 41.18 E-value: 6.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807353 159 RKRMKMFP-HEFSGGMRQRVMIAMAL---LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 229
Cdd:COG1106 192 KGGNVPLPlSEESDGTKRLLALAGALldaLAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHST 266
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
170-240 |
8.91e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 8.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807353 170 SGGMRQRVMIAMALLC---RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAgICDKVL 240
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI-IEHNMHVVK-VADYVL 882
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
172-228 |
3.63e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 3.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 505807353 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 505807353 174 RQRVMIAMALLCRPKLLI-ADEPTTALDVTVQAQIMTLLNEL 214
Cdd:TIGR00956 907 RKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| |
