|
Name |
Accession |
Description |
Interval |
E-value |
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
7-336 |
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 495069250 7 SAPQQTAASQAtLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFN 86
Cdd:PRK09473 1 TVPLAQQQADA-LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 87 GREILNLPERELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYP 166
Cdd:PRK09473 80 GREILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 247 TMEYGKAREVFYDPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSTTPPLEEFAPGRL 326
Cdd:PRK09473 240 TMEYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFGPGRL 319
|
330
....*....|
gi 495069250 327 RACFKPVEEL 336
Cdd:PRK09473 320 RACFKPVEEL 329
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-335 |
0e+00 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 560.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPEREL 98
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVM 178
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFY 258
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 259 DPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSTT-PPLEEFAPGRLRACFKPVEE 335
Cdd:COG0444 241 NPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEePPLREVGPGHRVACHLYEEE 318
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-294 |
1.82e-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: 428.72 E-value: 1.82e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 15 SQATLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG-RIGGSATFNGREILNL 93
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAaHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 PERELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGM 173
Cdd:COG4172 82 SERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKA 253
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 495069250 254 REVFYDPAHPYSIGLLNAVPRLDAegeslLTIPGNPPNLLR 294
Cdd:COG4172 242 AELFAAPQHPYTRKLLAAEPRGDP-----RPVPPDAPPLLE 277
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-251 |
3.14e-126 |
|
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: 360.67 E-value: 3.14e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEREL 98
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS---GSIIFDGKDLLKLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 nRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEEsVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVM 178
Cdd:cd03257 78 -KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKE-AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
13-330 |
4.40e-126 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 364.05 E-value: 4.40e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 13 AASQATLLDVKDLRVTF-------ATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATF 85
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTS---GEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 86 NGREILNLPERELNRLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKM-PEARKRmrm 164
Cdd:COG4608 78 DGQDITGLSGRELRPLRR-RMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 165 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 244
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 245 GRTMEYGKAREVFYDPAHPYSIGLLNAVPRLDAEGES---LLTipGNPPNLLRLPKGCPFQPRCPHAMEICSTT-PPLEE 320
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAVPVPDPERRReriVLE--GDVPSPLNPPSGCRFHTRCPYAQDRCATEePPLRE 311
|
330
....*....|
gi 495069250 321 FAPGRLRACF 330
Cdd:COG4608 312 VGPGHQVACH 321
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-278 |
5.94e-113 |
|
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: 337.26 E-value: 5.94e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 8 APQQTAASQATLLDVKDLRVTFAT-PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFN 86
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS---GSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 87 GREILNLPERELNRLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARkrMRMYP 166
Cdd:COG1123 326 GKDLTKLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDL--ADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250 260 270
....*....|....*....|....*....|..
gi 495069250 247 TMEYGKAREVFYDPAHPYSIGLLNAVPRLDAE 278
Cdd:COG1123 483 IVEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-295 |
4.59e-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: 329.94 E-value: 4.59e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLRVTFatPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPER 96
Cdd:COG1123 2 TPLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 elnrLRAEQISMIFQDPMTSLNPyMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQR 176
Cdd:COG1123 80 ----LRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLG-LSRAEARARVLELLEAVGLERRLDR---YPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 495069250 257 FYDPAhpysigLLNAVPRLDAEGESLLTIPGNPPNLLRL 295
Cdd:COG1123 231 LAAPQ------ALAAVPRLGAARGRAAPAAAAAEPLLEV 263
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-335 |
1.92e-109 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 321.69 E-value: 1.92e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSA-TFNGREILNLPERE 97
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKlEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRV 177
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVF 257
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 258 YDPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSTTPPLEEFAPGRLRACFKPVEE 335
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKCHYPLDD 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-276 |
1.06e-102 |
|
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: 311.62 E-value: 1.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 8 APQQTAASQATLLDVKDLRVTFATPDG-------DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIg 80
Cdd:COG4172 264 DPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEI- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 81 gsaTFNGREILNLPERELNRLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHK-SMSKAEAFEESVRMLDAVKM-PEA 158
Cdd:COG4172 343 ---RFDGQDLDGLSRRALRPLRR-RMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 159 RKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDK 238
Cdd:COG4172 419 RHR---YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHR 495
|
250 260 270
....*....|....*....|....*....|....*...
gi 495069250 239 VLVMYAGRTMEYGKAREVFYDPAHPYSIGLLNAVPRLD 276
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-331 |
1.17e-97 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 292.00 E-value: 1.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 12 TAASQATLLDVKDLRVTFATPDGD---------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGS 82
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD---GE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 83 ATFNGREILNLPERELNRLRAEqISMIFQDPMTSLNPYMRVGEQLMEVL-MLHKSMSKAEAFEESVRMLDAVKM-PEARK 160
Cdd:PRK15079 78 VAWLGKDLLGMKDDEWRAVRSD-IQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLlPNLIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 161 RmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 240
Cdd:PRK15079 157 R---YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 241 VMYAGRTMEYGKAREVFYDPAHPYSIGLLNAVPRLDAEGESLLTI---PGNPPNLLRLPKGCPFQPRCPHAMEICSTTPP 317
Cdd:PRK15079 234 VMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIqllEGELPSPINPPSGCVFRTRCPIAGPECAKTRP 313
|
330
....*....|....
gi 495069250 318 LEEFAPGRLRACFK 331
Cdd:PRK15079 314 VLEGSFRHAVSCLK 327
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-294 |
2.33e-96 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 295.46 E-value: 2.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI--GGSATFNGREILNLPE 95
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQ 175
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARE 255
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 495069250 256 VFYDPAHPYSIGLLNAVPRLDAegeslLTIPGNPPNLLR 294
Cdd:PRK15134 244 LFSAPTHPYTQKLLNSEPSGDP-----VPLPEPASPLLD 277
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-277 |
4.42e-93 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 289.45 E-value: 4.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 9 PQQTAASQATLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATF--- 85
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 86 -NGREILNLPER---ELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKR 161
Cdd:PRK10261 82 rRSRQVIELSEQsaaQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 162 MRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 241
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 495069250 242 MYAGRTMEYGKAREVFYDPAHPYSIGLLNAVPRLDA 277
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLGA 277
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-337 |
2.52e-92 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 278.33 E-value: 2.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggSA---TFNGREILNLPE 95
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHV--TAdrfRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVL---------MLHKSMSKAEAfeesVRMLDAVKMPEARKRMRMYP 166
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpswtfkgkwWQRFKWRKKRA----IELLHRVGIKDHKDIMNSYP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 247 TMEYGKAREVFYDPAHPYSIGLLNAVP--RLDAEGESLL-TIPGNPPNLLRLPKGCPFQPRCPHAMEICSTTPPLEEFAp 323
Cdd:COG4170 237 TVESGPTEQILKSPHHPYTKALLRSMPdfRQPLPHKSRLnTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRKIK- 315
|
330
....*....|....*.
gi 495069250 324 GRLRACFKP--VEELK 337
Cdd:COG4170 316 GHEFACHFPlnMEEKK 331
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-335 |
4.66e-92 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 277.62 E-value: 4.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 15 SQATLLDVKDLRVTFA------TPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGR 88
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTG---GELYYQGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 89 EILNlPERELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKM-PEARKRmrmYPH 167
Cdd:PRK11308 78 DLLK-ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 248 MEYGKAREVFYDPAHPYSIGLLNAVPRLDAEGESL-LTIPGNPPNLLRLPKGCPFQPRCPHAMEICST-TPPLEEFApGR 325
Cdd:PRK11308 234 VEKGTKEQIFNNPRHPYTQALLSATPRLNPDDRRErIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQeQPQLRDYD-GR 312
|
330
....*....|
gi 495069250 326 LRACFkPVEE 335
Cdd:PRK11308 313 LVACF-AVEQ 321
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-278 |
1.45e-90 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 270.91 E-value: 1.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEREL 98
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS---GEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRlraeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKsmsKAEAFEESVRMLDAVKMPEA-RKRmrmYPHEFSGGMRQRV 177
Cdd:COG1124 78 RR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLPPSfLDR---YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVF 257
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250 260
....*....|....*....|.
gi 495069250 258 YDPAHPYSIGLLNAVPRLDAE 278
Cdd:COG1124 228 AGPKHPYTRELLAASLAFERA 248
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
38-271 |
6.58e-81 |
|
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: 245.74 E-value: 6.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI-GGSATFNGREILNLperelnRLRAEQISMIFQDPMTS 116
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQtSGEILLDGRPLLPL------SIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LNPYMRVGEQLMEVLMLHKSMSKaEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGLLNA 271
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-333 |
8.47e-76 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 236.24 E-value: 8.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSA-TFNGREILNLPERE 97
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRmRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVL---------MLHKSMSKAEAFEesvrMLDAVKMPEARKRMRMYPHE 168
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgrwWQRFGWRKRRAIE----LLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 249 EYGKAREVFYDPAHPYSIGLLNAVP---RLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSTTPPLEEfAPGR 325
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPdfgSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTG-AKNH 317
|
....*...
gi 495069250 326 LRACFKPV 333
Cdd:PRK15093 318 LYACHFPL 325
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
19-272 |
3.75e-68 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 214.29 E-value: 3.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRI---GGSATFNGRE-----I 90
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLY--FDLaptSGSVYYRDRDggprdL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 91 LNLPERELNRLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKSMSKAEAFEesvrMLDAVKMPEARkrMRM 164
Cdd:COG4107 82 FALSEAERRRLRRTDWGMVYQNPRDGLR--MDVsaggniAERLMAAGERHYGDIRARALE----WLERVEIPLER--IDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 165 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 244
Cdd:COG4107 154 LPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKN 233
|
250 260
....*....|....*....|....*...
gi 495069250 245 GRTMEYGKAREVFYDPAHPYSIGLLNAV 272
Cdd:COG4107 234 GRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-269 |
6.20e-68 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 221.50 E-value: 6.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 9 PQQTAASQATLLDVKDLRVTFATPDG-------DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIgg 81
Cdd:PRK15134 265 PVPLPEPASPLLDVEQLQVAFPIRKGilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEI-- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 82 saTFNGREILNLPERELNRLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLH-KSMSKAEAFEESVRMLDAVKM-PEAR 159
Cdd:PRK15134 343 --WFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLdPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 160 KRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 239
Cdd:PRK15134 420 HR---YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
|
250 260 270
....*....|....*....|....*....|
gi 495069250 240 LVMYAGRTMEYGKAREVFYDPAHPYSIGLL 269
Cdd:PRK15134 497 IVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
18-271 |
7.09e-68 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 213.55 E-value: 7.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFATPDG-----DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIln 92
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTS---GEILINGHKL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 93 lpERELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKM-PEarkRMRMYPHEFSG 171
Cdd:COG4167 78 --EYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPE---HANFYPHMLSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYG 232
|
250 260
....*....|....*....|
gi 495069250 252 KAREVFYDPAHPYSIGLLNA 271
Cdd:COG4167 233 KTAEVFANPQHEVTKRLIES 252
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-246 |
1.25e-63 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 201.43 E-value: 1.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIggsaTFNGREILNLP 94
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPTSGEV----LIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 95 ERELNRLRAEQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEarkRMRMYPHEFSGGMR 174
Cdd:COG1136 77 ERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGD---RLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495069250 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGR 246
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-276 |
3.66e-63 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 211.25 E-value: 3.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 5 ELSAPQQTAASQATLLDVKDLRVTFATPDG-------DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG 77
Cdd:PRK10261 299 EPPIEQDTVVDGEPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 78 rigGSATFNGREILNLPERELNRLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKM-P 156
Cdd:PRK10261 379 ---GEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 157 EARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGIC 236
Cdd:PRK10261 455 EHAWR---YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERIS 531
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 495069250 237 DKVLVMYAGRTMEYGKAREVFYDPAHPYSIGLLNAVPRLD 276
Cdd:PRK10261 532 HRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVAD 571
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-246 |
6.43e-60 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 191.55 E-value: 6.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPERELN 99
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPTS--GEVRVDGTDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAEQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKSmSKAEAFEESVRMLDAVKMPEarkRMRMYPHEFSGGMRQRVMI 179
Cdd:cd03255 78 AFRRRHIGFVFQSF--NLLPDLTALENVELPLLLAGV-PKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGR 246
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-295 |
1.89e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.43 E-value: 1.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTafaLMGLLAA-----NGRIggsaTFNGREILNLPER 96
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-T---LIRCINLlerptSGSV----LVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ELNRLRAeQISMIFQDP--MTSLNpymrVGEQLMEVLMLHKsMSKAEAfEESVR-MLDAVKMPEARKRmrmYPHEFSGGM 173
Cdd:COG1135 76 ELRAARR-KIGMIFQHFnlLSSRT----VAENVALPLEIAG-VPKAEI-RKRVAeLLELVGLSDKADA---YPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKA 253
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 495069250 254 REVFYDPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPN--LLRL 295
Cdd:COG1135 226 LDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGGgrLVRL 269
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
22-260 |
1.90e-54 |
|
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: 178.16 E-value: 1.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPERELNRL 101
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPTS--GSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 102 RAeQISMIFQ--DPMTSLNpymrVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMI 179
Cdd:cd03258 81 RR-RIGMIFQhfNLLSSRT----VFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKADA---YPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYD 259
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
.
gi 495069250 260 P 260
Cdd:cd03258 232 P 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-256 |
2.15e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.25 E-value: 2.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREIlnlpEREL 98
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIrMLLGLLRPTS---GEVRVLGEDV----ARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRAeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 178
Cdd:COG1131 69 AEVRR-RIGYVPQEP--ALYPDLTVRENLRFFARLYG-LPRKEARERIDELLELFGLTDAADR---KVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
15-257 |
4.78e-53 |
|
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: 174.40 E-value: 4.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 15 SQATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREILNL 93
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDsGEI----LVDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 PERELNRLRAeQISMIFQDP--MTSLNpymrVGEQLMEVLMLHKSMSKAEAfEESVRM-LDAVKMPEARKRMrmyPHEFS 170
Cdd:COG1127 73 SEKELYELRR-RIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEI-RELVLEkLELVGLPGAADKM---PSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 171 GGMRQRVMIAMALLCRPKLLIADEPTTALD-VTVqAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
....*...
gi 495069250 250 YGKAREVF 257
Cdd:COG1127 223 EGTPEELL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
13-249 |
9.35e-53 |
|
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: 173.77 E-value: 9.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 13 AASQATLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREIL 91
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLLAGLDRPtSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 92 NLPERELNRLRAEQISMIFQDPMtsLNPYMRVGEQLMEVLMLhksMSKAEAFEESVRMLDAVKMPEarkRMRMYPHEFSG 171
Cdd:COG4181 78 ALDEDARARLRARHVGFVFQSFQ--LLPTLTALENVMLPLEL---AGRRDARARARALLERVGLGH---RLDHYPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTME 249
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRLVE 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
35-271 |
1.33e-52 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 174.12 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 35 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrigGSATFNGREILNLPERELNRLRAEQISMIFQDPM 114
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA-----GVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 115 TSLNPYMRVGEQLMEVLmlhKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10418 90 SAFNPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGLLNA 271
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
19-272 |
2.70e-52 |
|
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: 173.09 E-value: 2.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGR-----EILNL 93
Cdd:TIGR02323 3 LLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDH---GTATYIMRsgaelELYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 PERELNRLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKSMSKAEAfeesVRMLDAVKMPeaRKRMRMYPH 167
Cdd:TIGR02323 76 SEAERRRLMRTEWGFVHQNPRDGLR--MRVsaganiGERLMAIGARHYGNIRATA----QDWLEEVEID--PTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....*
gi 495069250 248 MEYGKAREVFYDPAHPYSIGLLNAV 272
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
14-265 |
6.40e-51 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 169.72 E-value: 6.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 14 ASQATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGR----- 88
Cdd:PRK11701 1 MMDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA---GEVHYRMRdgqlr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 89 EILNLPERELNRLRAEQISMIFQDPMTSLNpyMRV------GEQLMEVLMLHKSMSKAEAfeesVRMLDAVKMPEARkrM 162
Cdd:PRK11701 74 DLYALSEAERRRLLRTEWGFVHQHPRDGLR--MQVsaggniGERLMAVGARHYGDIRATA----GDWLERVEIDAAR--I 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 163 RMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250 260
....*....|....*....|...
gi 495069250 243 YAGRTMEYGKAREVFYDPAHPYS 265
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDPQHPYT 248
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-260 |
3.36e-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: 166.74 E-value: 3.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELN 99
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS---GEVLVDGKDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RlraeQISMIFQDP-----MTSlnpymrVGEqlmEVL--MLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGG 172
Cdd:COG1122 75 R----KVGLVFQNPddqlfAPT------VEE---DVAfgPENLGLPREEIRERVEEALELVGLEHLADR---PPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
....*...
gi 495069250 253 AREVFYDP 260
Cdd:COG1122 218 PREVFSDY 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-272 |
9.79e-49 |
|
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: 164.21 E-value: 9.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFAT-----PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILN 92
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQ---GTVSFRGQDLYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 93 LPERELNRLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEarKRMRMYPHEFSGG 172
Cdd:TIGR02769 78 LDRKQRRAFRRD-VQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
|
250 260
....*....|....*....|
gi 495069250 253 AREVFyDPAHPYSIGLLNAV 272
Cdd:TIGR02769 235 VAQLL-SFKHPAGRNLQSAV 253
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-257 |
2.37e-48 |
|
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: 162.91 E-value: 2.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAAngrIGGSATFNGREILNLPERE 97
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKP---SSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 lnrlRAEQISMIFQDPMTSLNpyMRVgeqlMEVLML----HKSM---SKAEAFEESVRMLDAVKMpeARKRMRMYpHEFS 170
Cdd:COG1120 73 ----LARRIAYVPQEPPAPFG--LTV----RELVALgrypHLGLfgrPSAEDREAVEEALERTGL--EHLADRPV-DELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
....*..
gi 495069250 251 GKAREVF 257
Cdd:COG1120 220 GPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
22-246 |
2.85e-48 |
|
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: 161.10 E-value: 2.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFatPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLaanGRIGGSATFNGREILNLPERELNRl 101
Cdd:cd03225 2 LKNLSFSY--PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDLTKLSLKELRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 102 raeQISMIFQDPMTSL-NPymRVGEqlmEVL--MLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 178
Cdd:cd03225 76 ---KVGLVFQNPDDQFfGP--TVEE---EVAfgLENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
16-303 |
9.95e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 164.12 E-value: 9.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 16 QATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREILNLP 94
Cdd:COG3842 2 AMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDsGRI----LLDGRDVTGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 95 --ERelnrlraeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKsMSKAEAfEESVR-MLDAVKMPEARKRmrmYPHEFSG 171
Cdd:COG3842 74 peKR--------NVGMVFQDY--ALFPHLTVAENVAFGLRMRG-VPKAEI-RARVAeLLELVGLEGLADR---YPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVG 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 252 KAREVFYDPAHPYS---IGLLNAVP-RLDAEGESLLTIPGNPpnlLRLPKGCPFQP 303
Cdd:COG3842 219 TPEEIYERPATRFVadfIGEANLLPgTVLGDEGGGVRTGGRT---LEVPADAGLAA 271
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-264 |
1.67e-47 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 159.97 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANGrigGSATFNGREILNLPEREL 98
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKS-TLLRLIvGLLRPDS---GEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRAeQISMIFQDP--MTSLNpymrVGEQLMEVLMLHKSMSKAEaFEESVRM-LDAVKMPEARKRMrmyPHEFSGGMRQ 175
Cdd:cd03261 73 YRLRR-RMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEE-IREIVLEkLEAVGLRGAEDLY---PAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARE 255
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 495069250 256 VFyDPAHPY 264
Cdd:cd03261 224 LR-ASDDPL 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-242 |
1.86e-47 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 160.64 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 14 ASQATLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREILN 92
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLrLIAGLEKPTS---GEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 93 LPERelnrlraeqISMIFQDPmtSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGG 172
Cdd:COG1116 78 PGPD---------RGVVFQEP--ALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDA---YPHQLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-246 |
4.32e-46 |
|
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: 155.97 E-value: 4.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEREL 98
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTS---GEVLFNGQSLSKLSSNER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMpeaRKRMRMYPHEFSGGMRQRVM 178
Cdd:TIGR02211 78 AKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLIGK-KSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQ 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-242 |
7.49e-46 |
|
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: 155.32 E-value: 7.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANGrigGSATFNGREIlnlpeREL 98
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIaGLERPTS---GEVLVDGEPV-----TGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRlraeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 178
Cdd:cd03293 72 GP----DRGYVFQQD--ALLPWLTVLDNVALGLELQG-VPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-262 |
2.12e-45 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 155.72 E-value: 2.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFATPDG-----DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIln 92
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS---GELLIDDHPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 93 lpERELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMpeARKRMRMYPHEFSGG 172
Cdd:PRK15112 78 --HFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL--LPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|
gi 495069250 253 AREVFYDPAH 262
Cdd:PRK15112 234 TADVLASPLH 243
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-263 |
6.97e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 153.23 E-value: 6.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREIlNLPERE 97
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLrCINLLEEPDS---GTITVDGEDL-TDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNRLRAEqISMIFQdpmtSLN--PYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEarkRMRMYPHEFSGGMRQ 175
Cdd:COG1126 72 INKLRRK-VGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARE 255
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMT-MVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
....*...
gi 495069250 256 VFYDPAHP 263
Cdd:COG1126 223 FFENPQHE 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-263 |
1.94e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 155.34 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 23 KDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLaaNGRIGGSATFNGREILNLPERELNRLR 102
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLL--ERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 103 aEQISMIFQ--DPMTSLNPYMRVGEQLmEVLMLHKSMSKAEAFEesvrMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIA 180
Cdd:PRK11153 82 -RQIGMIFQhfNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTE----LLELVGLSDKADR---YPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDP 260
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
...
gi 495069250 261 AHP 263
Cdd:PRK11153 233 KHP 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-251 |
2.41e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 151.13 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELN 99
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDS---GEILIDGRDVTGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 rlraeqISMIFQDPmtSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMI 179
Cdd:cd03259 74 ------IGMVFQDY--ALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-246 |
6.34e-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: 148.70 E-value: 6.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELN 99
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS---GEIKVLGKDIKKEPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RlraeqISMIFQDPmtSLNPYMRVGEQLmevlmlhksmskaeafeesvrmldavkmpearkrmrmyphEFSGGMRQRVMI 179
Cdd:cd03230 74 R-----IGYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-261 |
7.22e-44 |
|
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: 150.67 E-value: 7.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREILNLPEREL 98
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFnLISGFLRPTS---GSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRL---RAEQISMIFQDpMTSL-NpyMRVGEQLME---VLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSG 171
Cdd:cd03219 73 ARLgigRTFQIPRLFPE-LTVLeN--VMVAAQARTgsgLLLARARREEREARERAEELLERVGLADLADRP---AGELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
250
....*....|
gi 495069250 252 KAREVFYDPA 261
Cdd:cd03219 226 TPDEVRNNPR 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
37-249 |
1.66e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 150.61 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 37 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRLRAEqISMIFQDPMTS 116
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQ---GNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPE--ARKRmrmyPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsvLDKR----PPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-257 |
2.51e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 2.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAangRIGGSATFNGREilnlPE 95
Cdd:COG1121 4 MPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP---PTSGTVRLFGKP----PR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRL----RAEQISMIFqdPMTslnpymrvgeqLMEVLM--------LHKSMSKAEAfEESVRMLDAVKMPE-ARKRM 162
Cdd:COG1121 72 RARRRIgyvpQRAEVDWDF--PIT-----------VRDVVLmgrygrrgLFRRPSRADR-EAVDEALERVGLEDlADRPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 163 RmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:COG1121 138 G----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL 212
|
250
....*....|....*
gi 495069250 243 yAGRTMEYGKAREVF 257
Cdd:COG1121 213 -NRGLVAHGPPEEVL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-251 |
2.69e-43 |
|
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: 147.20 E-value: 2.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 21 DVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREILNLPERELN 99
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPSS---GEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAeqismifqdpmtslnpYMrvgEQLMEVL-MLHKsmskaeafeesvrmldavkmpeARKRMrmypHEFSGGMRQRVM 178
Cdd:cd03214 73 RKIA----------------YV---PQALELLgLAHL----------------------ADRPF----NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-246 |
7.10e-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: 146.18 E-value: 7.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREIlNLPERELN 99
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE---PDSGSILIDGEDL-TDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRaEQISMIFQDPmtSLNPYMRVGEQLMEVLmlhksmskaeafeesvrmldavkmpearkrmrmyphefSGGMRQRVMI 179
Cdd:cd03229 73 PLR-RRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
33-246 |
2.67e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 146.35 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 33 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQtafaLMGLLAANGRI-GGSATFNGREILNLPERELNRLRaEQISMIFQ 111
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYGEERPtSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 112 DpmTSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLI 191
Cdd:COG2884 87 D--FRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 192 ADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
18-256 |
4.55e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 146.36 E-value: 4.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFAtpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREILNLPER 96
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVEPTS---GEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ELNRLRAeQISMIFQDPmtSLNPYMRVgeqLMEVLM-------LHKSMS-------KAEAFEesvrMLDAVKMPE-ARKR 161
Cdd:COG3638 74 ALRRLRR-RIGMIFQQF--NLVPRLSV---LTNVLAgrlgrtsTWRSLLglfppedRERALE----ALERVGLADkAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 162 mrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 241
Cdd:COG3638 144 ----ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
250
....*....|....*
gi 495069250 242 MYAGRTMEYGKAREV 256
Cdd:COG3638 220 LRDGRVVFDGPPAEL 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-197 |
2.25e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 141.25 E-value: 2.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPERELNRlraeQISMIFQDPmtSLN 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP---TEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--QLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 119 PYMRVGEQLMEVLMLhKSMSKAEAFEESVRMLDAVKMPEARKR-MRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:pfam00005 72 PRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-327 |
9.47e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.67 E-value: 9.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREIL-NLPERE 97
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDsGRI----VLNGRDLFtNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNrlraeqISMIFQDPMtsLNPYMRVGEQL---MEVLMLhksmSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMR 174
Cdd:COG1118 75 RR------VGFVFQHYA--LFPHMTVAENIafgLRVRPP----SKAEIRARVEELLELVQLEGLADR---YPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAR 254
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPD 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 255 EVFYDPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPnlLRLPKGCPFQP-----RcPHAMEIcSTTPPLEEFAPGRLR 327
Cdd:COG1118 220 EVYDRPATPFVARFLGCVNVLRGRVIGGQLEADGLT--LPVAEPLPDGPavagvR-PHDIEV-SREPEGENTFPATVA 293
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-251 |
3.20e-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: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREilnlPEREL 98
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS---GSILIDGED----VRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRaEQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 178
Cdd:COG4555 70 REAR-RQIGVLPDERG--LYDRLTVRENIRYFAELYG-LFDEELKKRIEELIELLGLEEFLDR---RVGELSTGMKKKVA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
27-273 |
3.47e-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: 142.18 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREILNlpERELNRLRaEQ 105
Cdd:TIGR04520 6 VSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTsGKV----TVDGLDTLD--EENLWEIR-KK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 106 ISMIFQDPMTSLnpymrVGEQL-------MEVLML-HKSMSK--AEAfeesvrmLDAVKMPEARKRMrmyPHEFSGGMRQ 175
Cdd:TIGR04520 79 VGMVFQNPDNQF-----VGATVeddvafgLENLGVpREEMRKrvDEA-------LKLVGMEDFRDRE---PHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKARE 255
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPRE 222
|
250
....*....|....*...
gi 495069250 256 VFYDPAHPYSIGLlnAVP 273
Cdd:TIGR04520 223 IFSQVELLKEIGL--DVP 238
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-242 |
3.90e-40 |
|
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: 140.36 E-value: 3.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLL-AANGRI---GGSATFNGREILNLPER 96
Cdd:cd03235 2 VEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLkPTSGSIrvfGKPLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 -ELNR---LRAEQISMifqdpmTSLNPYMRvgeqlmevlmLHKSMSKAEaFEESVRMLDAVKMPE-ARKRMRmyphEFSG 171
Cdd:cd03235 77 rSIDRdfpISVRDVVL------MGLYGHKG----------LFRRLSKAD-KAKVDEALERVGLSElADRQIG----ELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-246 |
1.07e-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: 137.51 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREILNLPERELNRlraeQ 105
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTsGEI----LIDGVDLRDLDLESLRK----N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 106 ISMIFQDPmtslnpymrvgeqlmeVLmlhksmskaeaFEESVRmldavkmpearkrmrmyphE--FSGGMRQRVMIAMAL 183
Cdd:cd03228 78 IAYVPQDP----------------FL-----------FSGTIR-------------------EniLSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-246 |
2.34e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.22 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRl 101
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS---GEILIDGKDIAKLPLEELRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 102 raeQISMIFQdpmtslnpymrvgeqlmevlmlhksmskaeafeesvrmldavkmpearkrmrmypheFSGGMRQRVMIAM 181
Cdd:cd00267 74 ---RIGYVPQ---------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-251 |
3.48e-39 |
|
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: 138.02 E-value: 3.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILnlpeRELN 99
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS---GTAYINGYSIR----TDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAEqISMIFQDPMtsLNPYMRVgeqlMEVLMLH---KSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQR 176
Cdd:cd03263 72 AARQS-LGYCPQFDA--LFDELTV----REHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-256 |
3.54e-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: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFAtpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELN 99
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS---GSVLIDGTDINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAeQISMIFQDPmtSLNPYMRVGEQlmeVLM-----------LHKSMSKAE---AFEesvrMLDAVKMPE-ARKRMRm 164
Cdd:cd03256 75 QLRR-QIGMIFQQF--NLIERLSVLEN---VLSgrlgrrstwrsLFGLFPKEEkqrALA----ALERVGLLDkAYQRAD- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 165 yphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 244
Cdd:cd03256 144 ---QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
250
....*....|..
gi 495069250 245 GRTMEYGKAREV 256
Cdd:cd03256 221 GRIVFDGPPAEL 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
34-261 |
1.54e-38 |
|
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: 136.60 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERElnrlraEQISMIFQDp 113
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS---GEILLDGKDITNLPPHK------RPVNTVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 mTSLNPYMRVGEQLMEVLMLhKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:cd03300 81 -YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPA 261
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-264 |
2.70e-38 |
|
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: 137.00 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGRI---GGSATFNGREILNLPERELNRLRAEQISMIF 110
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCI--NRLIeptSGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 111 QDpmTSLNPYMRVGEQL---MEVlmlhKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRP 187
Cdd:cd03294 109 QS--FALLPHRTVLENVafgLEV----QGVPRAEREERAAEALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 188 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPY 264
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-256 |
4.16e-38 |
|
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: 135.39 E-value: 4.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQT--AFALMGLLAANGRIGGSATFNGREILNLPERE 97
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLlrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNrLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmRMYPHEFSGGMRQR 176
Cdd:cd03260 77 LE-LRR-RVGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-256 |
7.39e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.78 E-value: 7.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREI----LN--- 92
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS---GEVLWDGEPLdpedRRrig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 93 -LPE-RelnrlraeqismifqdpmtSLNPYMRVGEQLMEVLMLHkSMSKAEAFEESVRMLDAVKMPEARKRMRmypHEFS 170
Cdd:COG4152 75 yLPEeR-------------------GLYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANKKV---EELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 171 GGMRQRVMIAMALLCRPKLLIADEPTTALD-VTVQAqIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
....*..
gi 495069250 250 YGKAREV 256
Cdd:COG4152 210 SGSVDEI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-246 |
4.30e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.25 E-value: 4.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELN 99
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS---GEIYLDGKPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RlraeQISMIFQDPmtSLnPYMRVGEQLMEVLMLHKsmsKAEAFEESVRMLDAVKMPEARKRMRMypHEFSGGMRQRVMI 179
Cdd:COG4619 74 R----QVAYVPQEP--AL-WGGTVRDNLPFPFQLRE---RKFDRERALELLERLGLPPDILDKPV--ERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
41-260 |
4.89e-37 |
|
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: 132.84 E-value: 4.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 41 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLaanGRIGGSATFNGREILNLPERElnrlraEQISMIFQDpmTSLNPY 120
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFI---KPDSGKILLNGKDITNLPPEK------RDISYVPQN--YALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 121 MRVGEQLmEVLMLHKSMSKAEAFEesvRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:cd03299 86 MTVYKNI-AYGLKKRKVDKKEIER---KVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDP 260
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-246 |
5.60e-37 |
|
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: 132.56 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFA--TPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAN-----GRIGGSATFNGRE 89
Cdd:COG4778 3 TLLEVENLSKTFTlhLQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIYGNylpdsGSILVRHDGGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 90 ILNLPERELNRLRAEQISMIFQdpmtSLNPYMRVG--EQLMEVLmLHKSMSKAEAFEESVRMLDAVKMPEarKRMRMYPH 167
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQ----FLRVIPRVSalDVVAEPL-LERGVDREEARARARELLARLNLPE--RLWDLPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
40-246 |
5.97e-37 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 132.06 E-value: 5.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 40 NDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPERELNRLRaEQISMIFQDpmTSLNP 119
Cdd:TIGR02982 22 FDINLEINPGEIVILTGPSGSGKT-TLLTLIGGLRSVQE--GSLKVLGQELHGASKKQLVQLR-RRIGYIFQA--HNLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 120 YMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:TIGR02982 96 FLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495069250 200 DVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGR 246
Cdd:TIGR02982 173 DSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGK 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-246 |
6.78e-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: 6.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIlNLPERELN 99
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS---GTIIIDGLKL-TDDKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAEqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEarkRMRMYPHEFSGGMRQRVMI 179
Cdd:cd03262 73 ELRQK-VGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-255 |
1.70e-36 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 130.95 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILnlpeRELN 99
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS---GRATVAGHDVV----REPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRaEQISMIFQDPmtSLNPYMrVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYpheFSGGMRQRVMI 179
Cdd:cd03265 70 EVR-RRIGIVFQDL--SVDDEL-TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARE 255
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
34-240 |
3.62e-36 |
|
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: 129.66 E-value: 3.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPERELNRLRAEQISMIFQDp 113
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFDS--GQVYLNGQETPPLNSKKASKFRREKLGYLFQN- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 mTSLNPYMRVGEQLmEVLMLHKSMSKAEAFEESVRMLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:TIGR03608 85 -FALIENETVEENL-DLGLKYKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495069250 194 EPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLgVVAGICDKVL 240
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
26-264 |
5.23e-36 |
|
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: 130.50 E-value: 5.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFATPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGREILNLPERELNRlrae 104
Cdd:cd03295 5 NVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEI----FIDGEDIREQDPVELRR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 QISMIFQDpmTSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRMRmYPHEFSGGMRQRVMIAMALL 184
Cdd:cd03295 76 KIGYVIQQ--IGLFPHMTVEENIALVPKLLK-WPKEKIRERADELLALVGLDPAEFADR-YPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPY 264
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-251 |
9.37e-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: 128.55 E-value: 9.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELN 99
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS---GEVLFDGKPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAEQismifqdpmtSLNPYMRVGEQLMEVLMLhKSMSKAEAFEESVRMLDAVKMPE-ARKRMRmyphEFSGGMRQRVM 178
Cdd:cd03269 74 YLPEER----------GLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-256 |
1.29e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 129.34 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFAtpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEREL 98
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSS---GSILLEGTDITKLRGKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRAeQISMIFQD-----PMTSL-NPYM-RVGEQ--LMEVLMLHKSMSKAEAFEesvrMLDAVKMPE-ARKRMRmyphE 168
Cdd:TIGR02315 75 RKLRR-RIGMIFQHynlieRLTVLeNVLHgRLGYKptWRSLLGRFSEEDKERALS----ALERVGLADkAYQRAD----Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
....*...
gi 495069250 249 EYGKAREV 256
Cdd:TIGR02315 226 FDGAPSEL 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-251 |
1.73e-34 |
|
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: 125.49 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 43 NFSLRA-----GETLGIVGESGSGKSQTAFALMGLLAA-NGRI--GGSATFNGREILNLPERElnrlraEQISMIFQDpm 114
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPdGGTIvlNGTVLFDSRKKINLPPQQ------RKIGLVFQQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 115 TSLNPYMRVGEQLMEVLMLHKSMSKAEAFEEsvrMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRNREDRISVDE---LLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
26-256 |
4.72e-34 |
|
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: 132.27 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRIggsaTFNGREILNLPERELNRlrae 104
Cdd:COG2274 478 NVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPtSGRI----LIDGIDLRQIDPASLRR---- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 QISMIFQDPM----------TSLNPYMRVgEQLMEVLMLhksmskAEAFEESVRM---LDAVKMPEARKrmrmypheFSG 171
Cdd:COG2274 550 QIGVVLQDVFlfsgtireniTLGDPDATD-EEIIEAARL------AGLHDFIEALpmgYDTVVGEGGSN--------LSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYG 251
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
....*
gi 495069250 252 KAREV 256
Cdd:COG2274 692 THEEL 696
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-255 |
8.08e-34 |
|
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: 130.66 E-value: 8.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 9 PQQTAASQATLLDVKDlrVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGR 88
Cdd:COG4987 323 AEPAPAPGGPSLELED--VSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS---GSITLGGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 89 EILNLPERELnrlrAEQISMIFQDP---MTSL--NpyMRVG------EQLMEVLmlhksmskaeafeESVRMLDAVKMPE 157
Cdd:COG4987 398 DLRDLDEDDL----RRRIAVVPQRPhlfDTTLreN--LRLArpdatdEELWAAL-------------ERVGLGDWLAALP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 158 ARKRMRMYPH--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLgVVAGI 235
Cdd:COG4987 459 DGLDTWLGEGgrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLER 535
|
250 260
....*....|....*....|
gi 495069250 236 CDKVLVMYAGRTMEYGKARE 255
Cdd:COG4987 536 MDRILVLEDGRIVEQGTHEE 555
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
34-255 |
9.49e-34 |
|
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: 125.97 E-value: 9.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILnlpeRELNRLRaEQISMIFQDP 113
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTS---GTARVAGYDVV----REPRKVR-RSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 mtslnpymRVGEQL--MEVLMLHKS---MSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:TIGR01188 76 --------SVDEDLtgRENLEMMGRlygLPKDEAEERAEELLELFELGEAADR---PVGTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 189 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARE 255
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-255 |
1.01e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 130.26 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 10 QQTAASQATLLDVKDLRVTFatpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGRE 89
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS---GSILINGVD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 90 ILNLPERELNRlraeQISMIFQDP----MTslnpymrvgeqLMEVLMLhksmSKAEAFEEsvRMLDAVKMPEARKRMRMY 165
Cdd:COG4988 401 LSDLDPASWRR----QIAWVPQNPylfaGT-----------IRENLRL----GRPDASDE--ELEAALEAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 166 PHEF-----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAg 234
Cdd:COG4988 460 PDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA- 536
|
250 260
....*....|....*....|.
gi 495069250 235 ICDKVLVMYAGRTMEYGKARE 255
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEE 557
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
34-275 |
3.82e-33 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 122.60 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREILNLPerelnrLRAEQISMIFQD 112
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDsGRI----RLNGQDATRVH------ARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pmTSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:TIGR00968 81 --YALFKHLTVRDNIAFGLEIRK-HPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVALARALAVEPQVLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 193 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGLLNAV 272
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
...
gi 495069250 273 PRL 275
Cdd:TIGR00968 235 NVL 237
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
19-263 |
3.88e-33 |
|
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: 125.38 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPEREL 98
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERPTS--GSVIVDGQDLTTLSNSEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRaEQISMIFQ--DPMTSLNPYMRVGEQLmEVlmlhKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQR 176
Cdd:TIGR02314 78 TKAR-RQIGMIFQhfNLLSSRTVFGNVALPL-EL----DNTPKDEIKRKVTELLALVGLGDKHDS---YPSNLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:TIGR02314 149 VAIARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEI 228
|
....*..
gi 495069250 257 FYDPAHP 263
Cdd:TIGR02314 229 FSHPKTP 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-264 |
4.45e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREILNLPEREL 98
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTsGEI----LIGGRDVTDLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NrlraeqISMIFQDPMtsLNPYMRVGEQLMEVLMLHKsMSKAEAfEESVR-MLDAVKMPEARKRmrmYPHEFSGGMRQRV 177
Cdd:COG3839 76 N------IAMVFQSYA--LYPHMTVYENIAFPLKLRK-VPKAEI-DRRVReAAELLGLEDLLDR---KPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD------LGvvagicDKVLVMYAGRTMEYG 251
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVG 216
|
250
....*....|...
gi 495069250 252 KAREVFYDPAHPY 264
Cdd:COG3839 217 TPEELYDRPANLF 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-257 |
5.11e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 16 QATLLDVKDLrvTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREilnLPE 95
Cdd:PRK13635 2 KEEIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA---GTITVGGMV---LSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRLRaEQISMIFQDPMTSLnpymrVGEQLMEVLmlhksmskaeAF---------EESVRMLDavkmpEARKRMRMY- 165
Cdd:PRK13635 74 ETVWDVR-RQVGMVFQNPDNQF-----VGATVQDDV----------AFglenigvprEEMVERVD-----QALRQVGMEd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 166 -----PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVL 240
Cdd:PRK13635 133 flnrePHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVI 211
|
250
....*....|....*..
gi 495069250 241 VMYAGRTMEYGKAREVF 257
Cdd:PRK13635 212 VMNKGEILEEGTPEEIF 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-269 |
5.51e-33 |
|
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: 122.45 E-value: 5.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERElnrl 101
Cdd:cd03296 5 VRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDS---GTILFGGEDATDVPVQE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 102 raEQISMIFQDpmTSLNPYMRVGEQL---MEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 178
Cdd:cd03296 74 --RNVGFVFQH--YALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFY 258
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 495069250 259 DPAHPYSIGLL 269
Cdd:cd03296 227 HPASPFVYSFL 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-262 |
6.19e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 122.71 E-value: 6.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL--LAANGRIGGSATFNGREILNLPERE 97
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNRlraeQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKSM-SKAEAFEESVRMLDAVKM-PEARKRMRMYPHEFSGGMRQ 175
Cdd:PRK14247 80 LRR----RVQMVFQIP--NPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwDEVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARE 255
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....*..
gi 495069250 256 VFYDPAH 262
Cdd:PRK14247 232 VFTNPRH 238
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-246 |
7.23e-33 |
|
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: 120.23 E-value: 7.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLRVTfatpdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPER 96
Cdd:cd03215 2 EPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAS---GEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ELNRLRaeqISMIFQDPM-TSLNPYMRVGEQLMEVLMLhksmskaeafeesvrmldavkmpearkrmrmyphefSGGMRQ 175
Cdd:cd03215 71 DAIRAG---IAYVPEDRKrEGLVLDLSVAENIALSSLL------------------------------------SGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-246 |
1.00e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 4 IELSAPQQTAASQATLLDVKDLRVTfatpdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSA 83
Cdd:COG1129 241 LEDLFPKRAAAPGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA---DSGEI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 84 TFNGREILN-------------LPErelNRLR---------AEQISMifqdpmTSLNPYMRVGeqlmevlMLHKSMSKAE 141
Cdd:COG1129 310 RLDGKPVRIrsprdairagiayVPE---DRKGeglvldlsiRENITL------ASLDRLSRGG-------LLDRRRERAL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 142 AfEESVRMLDaVKMPEARKRMRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTA 221
Cdd:COG1129 374 A-EEYIKRLR-IKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKA 446
|
250 260
....*....|....*....|....*
gi 495069250 222 IIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:COG1129 447 VIVISSELPELLGLSDRILVMREGR 471
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-296 |
1.27e-32 |
|
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: 124.06 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 24 DLRVTFATPDGDVTAvndlnfslragetlgIVGESGSGKSQTAFALMGLL-AANGRI--GGSATFNGREILNLPerelnr 100
Cdd:COG4148 15 TLDVDFTLPGRGVTA---------------LFGPSGSGKTTLLRAIAGLErPDSGRIrlGGEVLQDSARGIFLP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 101 lrAEQ--ISMIFQDPmtSLNPYMRVGEQLMEvlmlhkSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVM 178
Cdd:COG4148 74 --PHRrrIGYVFQEA--RLFPHLSVRGNLLY------GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFY 258
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495069250 259 DPAHPYSIGLLNAVPRLDAE--------GESLLTIPGNPpnlLRLP 296
Cdd:COG4148 224 RPDLLPLAGGEEAGSVLEATvaahdpdyGLTRLALGGGR---LWVP 266
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
34-260 |
2.92e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 120.50 E-value: 2.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANG--RIGGSaTFNGREILNlpERELNRLRaEQISMI 109
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDSGqlNIAGH-QFDFSQKPS--EKAIRLLR-QKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 110 FQDpmTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:COG4161 88 FQQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGKArEVFYDP 260
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQP 231
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
34-264 |
2.93e-32 |
|
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: 123.22 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERelnrlrAEQISMIFQDp 113
Cdd:TIGR03265 15 GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTA---GTIYQGGRDITRLPPQ------KRDYGIVFQS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 mTSLNPYMRVgEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:TIGR03265 85 -YALFPNLTV-ADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPY 264
Cdd:TIGR03265 160 EPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPF 230
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
27-246 |
3.13e-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: 119.66 E-value: 3.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLL-AANGRIGGSATFNGREILNLPERELNRLRaEQ 105
Cdd:TIGR02673 7 VSKAYP-GGVAALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLyGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 106 ISMIFQDpmTSLNPYMRVGEQLmeVLMLHKSMSKAEAFEESV-RMLDAVKMPEarkRMRMYPHEFSGGMRQRVMIAMALL 184
Cdd:TIGR02673 81 IGVVFQD--FRLLPDRTVYENV--ALPLEVRGKKEREIQRRVgAALRQVGLEH---KADAFPEQLSGGEQQRVAIARAIV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495069250 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR02673 154 NSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
249-331 |
1.82e-31 |
|
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: 113.61 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 249 EYGKAREVFYDPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICST-TPPLEEFAPGRLR 327
Cdd:TIGR01727 4 ETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKePPALVEIAEGHRV 83
|
....
gi 495069250 328 ACFK 331
Cdd:TIGR01727 84 ACHL 87
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
22-287 |
2.38e-31 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 120.87 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrIGGSATFNGREILNLPERELNrl 101
Cdd:TIGR03258 8 IDHLRVAY----GANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAG-LTGRIAIADRDLTHAPPHKRG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 102 raeqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAM 181
Cdd:TIGR03258 81 ----LALLFQN--YALFPHLKVEDNVAFGLRAQK-MPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREF-NTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDP 260
Cdd:TIGR03258 151 AIAIEPDVLLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAP 230
|
250 260
....*....|....*....|....*..
gi 495069250 261 AHPYSIGLLNAVPRLDAEGESLLTIPG 287
Cdd:TIGR03258 231 ADGFAAEFLGAANILPAIALGITEAPG 257
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-263 |
2.60e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.22 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 11 QTAASQATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqT---AFALMGLLAANGRIGGSATFNG 87
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKS-TllrCLNRMNDLIPGARVEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 88 REILNlPERELNRLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKSMSKA---EAFEESVRML---DAVKmpearK 160
Cdd:COG1117 78 EDIYD-PDVDVVELRR-RVGMVFQKP----NPFpKSIYDNVAYGLRLHGIKSKSeldEIVEESLRKAalwDEVK-----D 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 161 RMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVL 240
Cdd:COG1117 147 RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTA 224
|
250 260
....*....|....*....|...
gi 495069250 241 VMYAGRTMEYGKAREVFYDPAHP 263
Cdd:COG1117 225 FFYLGELVEFGPTEQIFTNPKDK 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-256 |
2.73e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 4 IELSAPQQTAASQATLLDVKDLRVTfatPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSA 83
Cdd:COG3845 242 VLLRVEKAPAEPGEVVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA---SGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 84 TFNGREILNLPERELNRLRaeqISMIFQDPM-TSLNPYMRVGEQLmeVLMLHKS--------MSKAEAFEESVRMLDA-- 152
Cdd:COG3845 316 RLDGEDITGLSPRERRRLG---VAYIPEDRLgRGLVPDMSVAENL--ILGRYRRppfsrggfLDRKAIRAFAEELIEEfd 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 153 VKMPEARKRMRMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVV 232
Cdd:COG3845 391 VRTPGPDTPARS----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEI 465
|
250 260
....*....|....*....|....
gi 495069250 233 AGICDKVLVMYAGRTMEYGKAREV 256
Cdd:COG3845 466 LALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
34-253 |
6.49e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 117.04 E-value: 6.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGR--IGGSAtFNGREILNlpERELNRLRaEQISMI 109
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRSGTlnIAGNH-FDFSKTPS--DKAIRELR-RNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 110 FQDpmTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK11124 88 FQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495069250 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGKA 253
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
19-242 |
1.02e-30 |
|
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: 115.95 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPD-GDV--TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG-LLAANGRIGGSATFNGREILNLP 94
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQqGGVrlPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnYLPDSGRILVRHEGAWVDLAQAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 95 ERELNRLRAEQISMIFQdpmtslnpYMRVGEQL--MEVLM---LHKSMSKAEAFEESVRMLDAVKMPEarKRMRMYPHEF 169
Cdd:TIGR02324 81 PREVLEVRRKTIGYVSQ--------FLRVIPRVsaLEVVAeplLERGVPREAARARARELLARLNIPE--RLWHLPPATF 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:TIGR02324 151 SGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
34-251 |
2.07e-30 |
|
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: 114.66 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsaTFNGREILNLPERELNrlraeqISMIFQD 112
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRI----YIGGRDVTDLPPKDRD------IAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pmTSLNPYMRVGEQLMEVLMLHKsMSKAEaFEESVRmlDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:cd03301 81 --YALYPHMTVYDNIAFGLKLRK-VPKDE-IDERVR--EVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 193 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-262 |
2.21e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.64 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREILNlPE 95
Cdd:PRK14239 4 PILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYS-PR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRLRAEqISMIFQDPmtslNPY-MRVGEQLMEVLMLHKSMSKA---EAFEESVRmlDAVKMPEARKRMRMYPHEFSG 171
Cdd:PRK14239 79 TDTVDLRKE-IGMVFQQP----NPFpMSIYENVVYGLRLKGIKDKQvldEAVEKSLK--GASIWDEVKDRLHDSALGLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
|
250
....*....|.
gi 495069250 252 KAREVFYDPAH 262
Cdd:PRK14239 230 DTKQMFMNPKH 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-251 |
1.70e-29 |
|
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: 112.59 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFAtPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNLPereL 98
Cdd:cd03244 3 IEFKNVSLRYR-PNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSI----LIDGVDISKIG---L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRaEQISMIFQDPMT-------SLNPYMRVG-EQLMEVLmlhksmskaeafeESVRMLDAVKMPEARKRMRMypHE-- 168
Cdd:cd03244 74 HDLR-SRISIIPQDPVLfsgtirsNLDPFGEYSdEELWQAL-------------ERVGLKEFVESLPGGLDTVV--EEgg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 169 --FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGiCDKVLVMYAG 245
Cdd:cd03244 138 enLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE---AFkDCTVLTIAHRLDTIID-SDRILVLDKG 213
|
....*.
gi 495069250 246 RTMEYG 251
Cdd:cd03244 214 RVVEFD 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-245 |
1.73e-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: 111.97 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFATPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGgsatFNGReilNLPERElnrlRAE 104
Cdd:cd03226 4 NISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSIL----LNGK---PIKAKE----RRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 QISMIFQDPMTSLnpYMR-VGEQLMEVLM-LHKSMSKAEAfeesvrMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMA 182
Cdd:cd03226 72 SIGYVMQDVDYQL--FTDsVREELLLGLKeLDAGNEQAET------VLKDLDLYALKER---HPLSLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 183 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
38-275 |
2.99e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNlPERELNRLRaEQISMIFQDPmtsl 117
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS---GKIIIDGVDITD-KKVKLSDIR-KKVGLVFQYP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 118 nPYmrvgeQLMEvlmlhKSMSKAEAFEESVRML--DAVKMpEARKRMRMY-----------PHEFSGGMRQRVMIAMALL 184
Cdd:PRK13637 93 -EY-----QLFE-----ETIEKDIAFGPINLGLseEEIEN-RVKRAMNIVgldyedykdksPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPY 264
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
250
....*....|.
gi 495069250 265 SIGLlnAVPRL 275
Cdd:PRK13637 241 SIGL--AVPQV 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-268 |
3.41e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGreiLNLPERELNRLRaEQI 106
Cdd:PRK13640 11 VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDG---ITLTAKTVWDIR-EKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 107 SMIFQDPMTSLnpymrVGEQLMEVLML---HKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMAL 183
Cdd:PRK13640 87 GIVFQNPDNQF-----VGATVGDDVAFgleNRAVPRPEMIKIVRDVLADVGMLDYIDSE---PANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 184 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGKAREVFYDPAHP 263
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
....*
gi 495069250 264 YSIGL 268
Cdd:PRK13640 238 KEIGL 242
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-264 |
7.18e-29 |
|
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: 114.05 E-value: 7.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 41 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRI--GGSATFNGREILNLP-ERelnrlRAeqISMIFQDpmTS 116
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIvlNGRTLFDSRKGIFLPpEK-----RR--IGYVFQE--AR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMpearkrMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPY 264
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-228 |
7.26e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 110.26 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGrigGSATFNGREILNLPERe 97
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKT-TLLrILAGLLPPSA---GEVLWNGEPIRDARED- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 lnrlRAEQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKSMSKAEAFEEsvrMLDAVKMPEARKRmrmYPHEFSGGMRQRV 177
Cdd:COG4133 73 ----YRRRLAYLGHADG--LKPELTVRENLRFWAALYGLRADREAIDE---ALEAVGLAGLADL---PVRQLSAGQKRRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 228
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-263 |
7.57e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.77 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFAtpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIG-GSATFNGREILNLP 94
Cdd:PRK11264 2 SAIEVKNLVKKFH----GQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRvGDITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 95 ERELNRLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMR 174
Cdd:PRK11264 77 KGLIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS---YPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGKAR 254
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
....*....
gi 495069250 255 EVFYDPAHP 263
Cdd:PRK11264 230 ALFADPQQP 238
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-257 |
8.17e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.75 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTafaLMGLLAanGRI---GGSATFNGREILNLPE 95
Cdd:COG4559 1 MLEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKS-T---LLKLLT--GELtpsSGEVRLNGRPLAAWSP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRLRA---EQISMIFqdPMTSLnpymrvgeqlmEVLML---HKSMSKAEAFEESVRMLDAVKMpeARKRMRMYPhEF 169
Cdd:COG4559 71 WELARRRAvlpQHSSLAF--PFTVE-----------EVVALgraPHGSSAAQDRQIVREALALVGL--AHLAGRSYQ-TL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 170 SGGMRQRVMIAMAlLC--------RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLV 241
Cdd:COG4559 135 SGGEQQRVQLARV-LAqlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILL 212
|
250
....*....|....*.
gi 495069250 242 MYAGRTMEYGKAREVF 257
Cdd:COG4559 213 LHQGRLVAQGTPEEVL 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-251 |
1.00e-28 |
|
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: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFAL-MGLLAAN-GRIggsaTFNGREIlnlpeRELNR--LR 102
Cdd:COG1132 345 VSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKS-TLVNLlLRFYDPTsGRI----LIDGVDI-----RDLTLesLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 103 aEQISMIFQDPMtslnpymrvgeqlmevlMLHKS------MSKAEAFEESVRmlDAVKMPEARKRMRMYPH--------- 167
Cdd:COG1132 414 -RQIGVVPQDTF-----------------LFSGTirenirYGRPDATDEEVE--EAAKAAQAHEFIEALPDgydtvvger 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 168 --EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAG 245
Cdd:COG1132 474 gvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDG 550
|
....*.
gi 495069250 246 RTMEYG 251
Cdd:COG1132 551 RIVEQG 556
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
38-268 |
2.41e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNlpeRELNRLRaEQISMIFQDP--- 113
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEI----FYNNQAITD---DNFEKLR-KHIGIVFQNPdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 -MTSLNPYmRVGEQLMEVLMLHKSMSK--AEAFEEsVRMLDavkmpearkRMRMYPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK13648 96 fVGSIVKY-DVAFGLENHAVPYDEMHRrvSEALKQ-VDMLE---------RADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 191 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGL 268
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGL 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-262 |
2.52e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 110.32 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN--GRIGGSATFNGREILNlPERE 97
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeeARVEGEVRLFGRNIYS-PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNRLRaEQISMIFQDPmtSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVR--MLDAVKMPEARKRMRMYPHEFSGGMRQ 175
Cdd:PRK14267 80 PIEVR-REVGMVFQYP--NPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwaLKKAALWDEVKDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARE 255
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
....*..
gi 495069250 256 VFYDPAH 262
Cdd:PRK14267 235 VFENPEH 241
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
33-264 |
2.68e-28 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 111.34 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 33 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafalmgLLAAN-------GRIggsaTFNGREILNLPERELNRlraeQ 105
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT------LRMINrlieptsGRI----LIDGEDIRDLDPVELRR----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 106 ISMIFQDpmTSLNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRMRmYPHEFSGGMRQRVMIAMALLC 185
Cdd:COG1125 78 IGYVIQQ--IGLFPHMTVAENIATVPRLLG-WDKERIRARVDELLELVGLDPEEYRDR-YPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD------LGvvagicDKVLVMYAGRTMEYGKAREVFYD 259
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDidealkLG------DRIAVMREGRIVQYDTPEEILAN 227
|
....*
gi 495069250 260 PAHPY 264
Cdd:COG1125 228 PANDF 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-263 |
3.10e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.06 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREI--------- 90
Cdd:PRK10619 6 LNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPSE--GSIVVNGQTInlvrdkdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 91 LNLPERELNRLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEaRKRMRmYPHEFS 170
Cdd:PRK10619 79 LKVADKNQLRLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE-RAQGK-YPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250
....*....|...
gi 495069250 251 GKAREVFYDPAHP 263
Cdd:PRK10619 234 GAPEQLFGNPQSP 246
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
248-312 |
3.12e-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: 104.41 E-value: 3.12e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 248 MEYGKAREVFYDPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC 312
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-246 |
3.13e-28 |
|
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: 109.03 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPERELNRLRaEQISMIFQD 112
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELpTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 P--MTSLNPYMRVGEQLMEVLMLHKSMSKaeafeesvRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:cd03292 87 FrlLPDRNVYENVAFALEVTGVPPREIRK--------RVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 191 IADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-247 |
4.77e-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: 106.74 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELN 99
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS---GEILVDGKEVSFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRaeqISMIFQdpmtslnpymrvgeqlmevlmlhksmskaeafeesvrmldavkmpearkrmrmypheFSGGMRQRVMI 179
Cdd:cd03216 74 RAG---IAMVYQ---------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
34-263 |
5.08e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREILNlPERELNRLRAEQiSMIFQD 112
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEEItSGDLIVDGLKVND-PKVDERLIRQEA-GMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pmTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEarkRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PRK09493 86 --FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 193 DEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHP 263
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-257 |
7.15e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.82 E-value: 7.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFaTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREilnLPEREL 98
Cdd:PRK13650 4 IIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES---GQIIIDGDL---LTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRaEQISMIFQDPMTSLnpymrVG---EQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQ 175
Cdd:PRK13650 77 WDIR-HKIGMVFQNPDNQF-----VGatvEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKERE---PARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGKARE 255
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
..
gi 495069250 256 VF 257
Cdd:PRK13650 227 LF 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-256 |
1.08e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 107.52 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPERELN 99
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP---RSGSIRFDGRDITGLPPHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLraeQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKmpEARKRMrmyPHEFSGGMRQRVMI 179
Cdd:cd03224 74 RA---GIGYVPEGRR--IFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK--ERRKQL---AGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-260 |
2.35e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.24 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatPDGDVtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIlNLPEREL 98
Cdd:PRK13639 1 ILETRDLKYSY--PDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS---GEVLIKGEPI-KYDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRaEQISMIFQDPMTSLnpYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQRVM 178
Cdd:PRK13639 74 LEVR-KTVGIVFQNPDDQL--FAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFY 258
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
..
gi 495069250 259 DP 260
Cdd:PRK13639 227 DI 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
41-246 |
2.41e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.21 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 41 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPERELNRLRAEQISMIFQdpMTSLNPY 120
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 121 MRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMpEARKRMRmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:PRK11629 102 FTALENVAMPLLIGK-KKPAEINSRALEMLAAVGL-EHRANHR--PSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495069250 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGR 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-259 |
2.50e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.40 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFatPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGREIlNLPER 96
Cdd:PRK13636 4 YILKVEELNYNY--SDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRI----LFDGKPI-DYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ELNRLRaEQISMIFQDP---MTSLNPYMRVGEQLMEVlmlhkSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGM 173
Cdd:PRK13636 76 GLMKLR-ESVGMVFQDPdnqLFSASVYQDVSFGAVNL-----KLPEDEVRKRVDNALKRTGIEHLKDKP---THCLSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKA 253
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
....*.
gi 495069250 254 REVFYD 259
Cdd:PRK13636 227 KEVFAE 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-251 |
4.64e-27 |
|
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: 105.76 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEReln 99
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS---GEITFDGKSYQKNIEA--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 rlrAEQISMIFQDPmtSLNPYMRVGEQLmEVLMLHKSMSKAEAFEesvrMLDAVKMPE-ARKRMRmyphEFSGGMRQRVM 178
Cdd:cd03268 71 ---LRRIGALIEAP--GFYPNLTARENL-RLLARLLGIRKKRIDE----VLDVVGLKDsAKKKVK----GFSLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-246 |
4.76e-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: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGeTLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPErEL 98
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILATLTPpSSGTIRIDGQDVLKQPQ-KL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLraeqISMIFQDPMTSlnPYMRVGEQL--MEVLmlhKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQR 176
Cdd:cd03264 71 RRR----IGYLPQEFGVY--PNFTVREFLdyIAWL---KGIPSKEVKARVDEVLELVNLGDRAKK---KIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-228 |
5.42e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNlPERE 97
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS---GEITLDGVPVTG-PGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 lnrlRAeqisMIFQDpmTSLNPYMRVGEQLMEVLMLhKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQRV 177
Cdd:COG4525 78 ----RG----VVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-228 |
6.74e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.26 E-value: 6.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANGRIGGSATFNGREILNLPerel 98
Cdd:COG4136 2 LSLENLTITL----GGRPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIaGTLSPAFSASGEVLLNGRRLTALP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 nrlrAEQ--ISMIFQDPMtsLNPYMRVGEQLMevLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQR 176
Cdd:COG4136 73 ----AEQrrIGILFQDDL--LFPHLSVGENLA--FALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRAR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-246 |
7.30e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.71 E-value: 7.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTF--ATPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTafaLMGLLAanGRI---GGSATFNGREILNLP 94
Cdd:COG1101 2 LELKNLSKTFnpGTVN-EKRALDGLNLTIEEGDFVTVIGSNGAGKS-T---LLNAIA--GSLppdSGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 95 ERElnrlRAEQISMIFQDPMTSLNPYMRVGEQLM------EVLMLHKSMSKA--EAFEESVRMLDavkMP-EARKRMRMy 165
Cdd:COG1101 75 EYK----RAKYIGRVFQDPMMGTAPSMTIEENLAlayrrgKRRGLRRGLTKKrrELFRELLATLG---LGlENRLDTKV- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 166 pHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH------DLGvvagicDKV 239
Cdd:COG1101 147 -GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeqalDYG------NRL 219
|
....*..
gi 495069250 240 LVMYAGR 246
Cdd:COG1101 220 IMMHEGR 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-261 |
9.44e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.50 E-value: 9.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 13 AASQATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANGrigGSATFNGREIL 91
Cdd:PRK09452 8 PSSLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIaGFETPDS---GRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 92 NLPerelnrlrAEQ--ISMIFQDpmTSLNPYMRVGEQLMEVLmlhkSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEF 169
Cdd:PRK09452 80 HVP--------AENrhVNTVFQS--YALFPHMTVFENVAFGL----RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 225
|
250
....*....|..
gi 495069250 250 YGKAREVFYDPA 261
Cdd:PRK09452 226 DGTPREIYEEPK 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-257 |
1.00e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.01 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG-LLAANGRIggsaTFNGREILNLPER 96
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEV----RLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ELNRLRAeqismifqdpmtslnpymrvgeqlmeVLMLHKSMSKAEAFEESVRM-------------------LDAVKMPE 157
Cdd:PRK13548 73 ELARRRA--------------------------VLPQHSSLSFPFTVEEVVAMgraphglsraeddalvaaaLAQVDLAH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 158 ARKRMrmYPhEFSGGMRQRVMIAMALL------CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGV 231
Cdd:PRK13548 127 LAGRD--YP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNL 203
|
250 260
....*....|....*....|....*.
gi 495069250 232 VAGICDKVLVMYAGRTMEYGKAREVF 257
Cdd:PRK13548 204 AARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
38-268 |
1.21e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.64 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILN-LPERELNRLRaEQISMIFQDPMts 116
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTS---GTVTIGERVITAgKKNKKLKPLR-KKVGIVFQFPE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 lnpymrvgEQLMEVLMLHK--------SMSKAEAFEESVRMLDAVKMPEarKRMRMYPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK13634 96 --------HQLFEETVEKDicfgpmnfGVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 189 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGL 268
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGL 245
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-252 |
1.31e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.10 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 36 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREilnlPERELNRLrAEQISMIFqdpmt 115
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTS---GEVRVLGYV----PFKRRKEF-ARRIGVVF----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 116 slnpymrvG--EQL------MEVLMLHKSMSK--AEAFEESVRMLdaVKMPE--------ARK-----RMRMyphEfsgg 172
Cdd:COG4586 102 --------GqrSQLwwdlpaIDSFRLLKAIYRipDAEYKKRLDEL--VELLDlgelldtpVRQlslgqRMRC---E---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 mrqrvmIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:COG4586 165 ------LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-256 |
1.37e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTafaLMGLLAanGRI---GGSATFNGREIlnl 93
Cdd:COG1129 2 EPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKS-T---LMKILS--GVYqpdSGEILLDGEPV--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 peRELNRLRAEQ--ISMIFQDPmtSLNPYMRVGEQLM--EVLMLHKSMSKAEAFEESVRMLDAVKMPE-ARKRMRmyphE 168
Cdd:COG1129 69 --RFRSPRDAQAagIAIIHQEL--NLVPNLSVAENIFlgREPRRGGLIDWRAMRRRARELLARLGLDIdPDTPVG----D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
....*...
gi 495069250 249 EYGKAREV 256
Cdd:COG1129 220 GTGPVAEL 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-268 |
2.00e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.95 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREILNLPEREL 98
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE---EFEGKVKIDGELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRlraeQISMIFQDPMTSLnpymrVGEQLMEVL---MLHKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQ 175
Cdd:PRK13642 80 RR----KIGMVFQNPDNQF-----VGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKARE 255
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE 226
|
250
....*....|...
gi 495069250 256 VFYDPAHPYSIGL 268
Cdd:PRK13642 227 LFATSEDMVEIGL 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
49-249 |
3.16e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.09 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 49 GETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPERELNRLRAEQISMIFQDPMtsLNPYMRVGEQL 127
Cdd:PRK10584 36 GETIALIGESGSGKS----TLLAILAGlDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFM--LIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 128 mEVLMLHKSMSKAEAFEESVRMLDAVKMPearKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 207
Cdd:PRK10584 110 -ELPALLRGESSRQSRNGAKALLEQLGLG---KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495069250 208 MTLLNELKREFNTAIIMITHDLgVVAGICDKVLVMYAGRTME 249
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQLQE 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-270 |
3.46e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 9 PQQTAASQAT-LLDVKDLRVTFatpDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFN 86
Cdd:PRK11607 8 PQAKTRKALTpLLEIRNLTKSF---DGQ-HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGfEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 87 GREILNLPERElnrlraEQISMIFQDpmTSLNPYMRVgEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMrmyP 166
Cdd:PRK11607 80 GVDLSHVPPYQ------RPINMMFQS--YALFPHMTV-EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---P 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 167 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
250 260
....*....|....*....|....*..
gi 495069250 247 TMEYGKAREVFYDPAHPYS---IGLLN 270
Cdd:PRK11607 228 FVQIGEPEEIYEHPTTRYSaefIGSVN 254
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-255 |
3.55e-26 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 104.16 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafalMGLLAangR----IGGSATFNGREILNLPereLNRL 101
Cdd:cd03249 6 VSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTV----VSLLE---RfydpTSGEILLDGVDIRDLN---LRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 102 RaEQISMIFQDPMTSlnpYMRVGEQLmevlmlhkSMSKAEAFEESVRmlDAVKMPEARKRMRMYPHEF-----------S 170
Cdd:cd03249 76 R-SQIGLVSQEPVLF---DGTIAENI--------RYGKPDATDEEVE--EAAKKANIHDFIMSLPDGYdtlvgergsqlS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
....*
gi 495069250 251 GKARE 255
Cdd:cd03249 219 GTHDE 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
43-263 |
7.39e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.91 E-value: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 43 NFSLRAGETLGIVGESGSGKSqtafALMGLLA-----ANGRIggsaTFNGREILNLP--ERElnrlraeqISMIFQDpmT 115
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS----TLLNLIAgflppDSGRI----LWNGQDLTALPpaERP--------VSMLFQE--N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 116 SLNPYMRVGEQLmeVLMLHKSMSKAEAFEESVR-MLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:COG3840 81 NLFPHLTVAQNI--GLGLRPGLKLTAEQRAQVEqALERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHP 263
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-251 |
8.21e-26 |
|
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: 102.49 E-value: 8.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFAtPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNLPereL 98
Cdd:cd03369 7 IEVENLSVRYA-PDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKI----EIDGIDISTIP---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLRaEQISMIFQDPM-------TSLNPY-MRVGEQLMEVLMLHKSMSKaeafeesvrmldavkmpearkrmrmypheFS 170
Cdd:cd03369 78 EDLR-SSLTIIPQDPTlfsgtirSNLDPFdEYSDEEIYGALRVSEGGLN-----------------------------LS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTME 249
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE---EFtNSTILTIAHRLRTIID-YDKILVMDAGEVKE 203
|
..
gi 495069250 250 YG 251
Cdd:cd03369 204 YD 205
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
34-264 |
9.11e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 105.96 E-value: 9.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTafalmgLL-AANGRI---GGSATFNGREILNLPERELNRLRAEQISMI 109
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKS-T------LVrCLNRLIeptAGEVLIDGEDITKLSKKELRELRRKKMSMV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 110 FQdpmtslnpymRVGeqlmevLMLHKS-------------MSKAEAFEESVRMLDAV--KMPEARkrmrmYPHEFSGGMR 174
Cdd:COG4175 111 FQ----------HFA------LLPHRTvlenvafgleiqgVPKAERRERAREALELVglAGWEDS-----YPDELSGGMQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 175 QRVMIAMALLCRPKLLIADEPTTALD----VTVQAQIMTLLNELKRefnTaIIMITHDL------GvvagicDKVLVMYA 244
Cdd:COG4175 170 QRVGLARALATDPDILLMDEAFSALDplirREMQDELLELQAKLKK---T-IVFITHDLdealrlG------DRIAIMKD 239
|
250 260
....*....|....*....|
gi 495069250 245 GRTMEYGKAREVFYDPAHPY 264
Cdd:COG4175 240 GRIVQIGTPEEILTNPANDY 259
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-251 |
1.36e-25 |
|
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: 102.06 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPerel 98
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA---GFATVDGFDVVKEP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 nrlRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQRVM 178
Cdd:cd03266 74 ---AEARRRLGFVSDSTGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRR---VGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-256 |
1.76e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 106.81 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFATPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGriGGSATFNGREILNLPER- 96
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTS--GEVNVRVGDEWVDMTKPg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ELNRLRAEQ-ISMIFQDpmTSLNPYMRVGEQLMEVLMLhkSMSKAEAFEESVRMLDAVKMPE--ARKRMRMYPHEFSGGM 173
Cdd:TIGR03269 357 PDGRGRAKRyIGILHQE--YDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLKMVGFDEekAEEILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKA 253
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
...
gi 495069250 254 REV 256
Cdd:TIGR03269 513 EEI 515
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
35-248 |
2.03e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 102.03 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 35 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGreilNLPERELNRLRAeQISMIFQDPm 114
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS---GEVRVAG----LVPWKRRKKFLR-RIGVVFGQK- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 115 tslnpymrvgEQL------MEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:cd03267 104 ----------TQLwwdlpvIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 189 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-264 |
2.39e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.12 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPERELNRLRAEQISMIFQDpmTSL 117
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRLIEPTR--GQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 118 NPYMRVgeqlMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:PRK10070 118 MPHMTV----LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 198 ALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPY 264
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-255 |
2.74e-25 |
|
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: 101.54 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangRI----GGSATFNGREILNLperELNRLR 102
Cdd:cd03253 6 VTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLF---RFydvsSGSILIDGQDIREV---TLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 103 aEQISMIFQDpmTSL-------N-PYMRVG---EQLMEVlmlhksmSKAEAFEESVrmldaVKMPEA-------RKRMrm 164
Cdd:cd03253 75 -RAIGVVPQD--TVLfndtigyNiRYGRPDatdEEVIEA-------AKAAQIHDKI-----MRFPDGydtivgeRGLK-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 165 ypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYA 244
Cdd:cd03253 138 ----LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKD 210
|
250
....*....|.
gi 495069250 245 GRTMEYGKARE 255
Cdd:cd03253 211 GRIVERGTHEE 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-260 |
4.12e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 35 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA---ANGRIGGSATFNGREILNLPERELNRlraeQISMIFQ 111
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 112 DPmtSLNPYMRVGEQLMEVLMLHKSMSKAEA---FEESVRMLDAVKmpEARKRMRMYPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK14246 98 QP--NPFPHLSIYDNIAYPLKSHGIKEKREIkkiVEECLRKVGLWK--EVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495069250 189 LLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDP 260
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-257 |
4.78e-25 |
|
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: 105.60 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPERELNRLraeq 105
Cdd:COG4618 335 NLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP---TAGSVRLDGADLSQWDREELGRH---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 106 ISMIFQDPmtslnpymrvgeqlmevlmlhksmskaEAFEESV-----RM--LDAVKMPEARKRMRMypHEF--------- 169
Cdd:COG4618 408 IGYLPQDV---------------------------ELFDGTIaeniaRFgdADPEKVVAAAKLAGV--HEMilrlpdgyd 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 170 ----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAgICDKV 239
Cdd:COG4618 459 trigeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKL 536
|
250
....*....|....*...
gi 495069250 240 LVMYAGRTMEYGKAREVF 257
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVL 554
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-259 |
5.01e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.99 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREI--LNLPErelnrLRaE 104
Cdd:PRK13632 13 VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS---GEIKIDGITIskENLKE-----IR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 QISMIFQDPMTSLnpymrVGeqlmevlmlhksmSKAE---AFEESVRMLDAVKMP----EARKRMRMY------PHEFSG 171
Cdd:PRK13632 84 KIGIIFQNPDNQF-----IG-------------ATVEddiAFGLENKKVPPKKMKdiidDLAKKVGMEdyldkePQNLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYG 251
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQG 224
|
....*...
gi 495069250 252 KAREVFYD 259
Cdd:PRK13632 225 KPKEILNN 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-256 |
6.32e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 6.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 15 SQATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTafaLM----GLLAAN-GRIggsaTFNGRE 89
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKS-T---LMkilyGLYQPDsGEI----LIDGKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 90 I-LNLPeRELNRLRaeqISMIFQDPMtsLNPYMRVgeqlMEVLMLhksmskaeAFEESVRMLdaVKMPEARKR----MRM 164
Cdd:COG3845 69 VrIRSP-RDAIALG---IGMVHQHFM--LVPNLTV----AENIVL--------GLEPTKGGR--LDRKAARARirelSER 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 165 YP---------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALdvTVQ--AQIMTLLNELKREfNTAIIMITHDLGVVA 233
Cdd:COG3845 129 YGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVM 205
|
250 260
....*....|....*....|...
gi 495069250 234 GICDKVLVMYAGRTMEYGKAREV 256
Cdd:COG3845 206 AIADRVTVLRRGKVVGTVDTAET 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-259 |
7.45e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.78 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILN-LPERELNRLRaEQISMIFQDPMTS 116
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT---GTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LnpYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:PRK13646 98 L--FEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYD 259
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-233 |
7.57e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.19 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPE 95
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGClDKPTSGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRLRAEQISMIFQdpMTSLNPYMrVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEarkRMRMYPHEFSGGMRQ 175
Cdd:PRK10535 78 DALAQLRREHFGFIFQ--RYHLLSHL-TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVA 233
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAA 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-278 |
7.91e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.85 E-value: 7.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERElnrlraEQISMIFQDp 113
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS---GHIRFHGTDVSRLHARD------RKVGFVFQH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 mTSLNPYMRVGEQL---MEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK10851 83 -YALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 191 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGLLN 270
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
....*...
gi 495069250 271 AVPRLDAE 278
Cdd:PRK10851 239 EVNRLQGT 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-247 |
9.41e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 104.24 E-value: 9.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA---NGRIGGSATFNGREIL--NL 93
Cdd:PRK13549 5 LLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKS----TLMKVLSGvypHGTYEGEIIFEGEELQasNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 PERElnrlrAEQISMIFQDPMtsLNPYMRVGEQ--LMEVLMLHKSMSKAEAFEESVRMLDAVKM---PEARKRmrmyphE 168
Cdd:PRK13549 77 RDTE-----RAGIAIIHQELA--LVKELSVLENifLGNEITPGGIMDYDAMYLRAQKLLAQLKLdinPATPVG------N 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT 247
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRH 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
39-260 |
1.17e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREI-LNLPERELNRLRaEQISMIFQDPMTsl 117
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS---GTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 118 npymrvgeQLMEVLMLHKSM--------SKAEAFEESVRMLDAVKMPEarKRMRMYPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK13641 97 --------QLFENTVLKDVEfgpknfgfSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDP 260
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
37-268 |
2.19e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.16 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 37 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNlpERELNRLRaEQISMIFQDPMTS 116
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE---GKVYVDGLDTSD--EENLWDIR-NKAGMVFQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LnpymrVGEQLMEVLMLHKSMSKAEAFEESVRM---LDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:PRK13633 98 I-----VATIVEEDVAFGPENLGIPPEEIRERVdesLKKVGMYEYRRHA---PHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGL 268
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKKIGL 243
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-261 |
2.38e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTF--ATPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG--------RIGGSATFNGR 88
Cdd:PRK13631 21 ILRVKNLYCVFdeKQEN-ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYgtiqvgdiYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 89 EILNLPERELN--RLRaEQISMIFQDPmtslnPYMRVGEQLMEVLM---LHKSMSKAEAFEESVRMLdaVKMPEARKRMR 163
Cdd:PRK13631 100 ITNPYSKKIKNfkELR-RRVSMVFQFP-----EYQLFKDTIEKDIMfgpVALGVKKSEAKKLAKFYL--NKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 164 MYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMY 243
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMD 250
|
250
....*....|....*...
gi 495069250 244 AGRTMEYGKAREVFYDPA 261
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQH 268
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
38-257 |
3.13e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.08 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngRIGGSATFNGREILNLPE-RELNRLRAEqISMIFQDPMTS 116
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIIS--ETGQTIVGDYAIPANLKKiKEVKRLRKE-IGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LnpYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:PRK13645 103 L--FQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVF 257
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-277 |
3.16e-24 |
|
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: 100.65 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 54 IVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERelnrLRAeqISMIFQDpmTSLNPYMRVGEQLMEVLml 133
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS---GSIMLDGEDVTNVPPH----LRH--INMVFQS--YALFPHMTVEENVAFGL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 134 hkSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNE 213
Cdd:TIGR01187 68 --KMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495069250 214 LKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGLLNAVPRLDA 277
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEA 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-256 |
3.18e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPER 96
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ELNRlraeQISMIFQDpmTSLNPYMRVgEQLMEvLMLHKSMSKAEAFEESVRMldAVKMPEARKRMRMYPH----EFSGG 172
Cdd:PRK09536 74 AASR----RVASVPQD--TSLSFEFDV-RQVVE-MGRTPHRSRFDTWTETDRA--AVERAMERTGVAQFADrpvtSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMItHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGP 222
|
....
gi 495069250 253 AREV 256
Cdd:PRK09536 223 PADV 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-261 |
5.91e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLrvTFATPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsaTFNGREILNLPE 95
Cdd:PRK13647 2 DNIIEVEDL--HFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRV----KVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRlraeQISMIFQDP---MTSLNPYMRV--GEQLMEvlmlhksMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFS 170
Cdd:PRK13647 75 KWVRS----KVGLVFQDPddqVFSSTVWDDVafGPVNMG-------LDKDEVERRVEEALKAVRMWDFRDKP---PYHLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 171 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:PRK13647 141 YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
250
....*....|.
gi 495069250 251 GkAREVFYDPA 261
Cdd:PRK13647 220 G-DKSLLTDED 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-246 |
6.11e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 102.05 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 4 IELSAPQQTAASQATLLDVKDLrvtfaTPDGDVtavnDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSA 83
Cdd:PRK15439 253 LELPGNRRQQAAGAPVLTVEDL-----TGEGFR----NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG---GRI 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 84 TFNGREILNLPERelNRLRA--------EQISMIFQDPMTSLNPYMrvgeqlmevlMLHKSMS-----KAEA--FEESVR 148
Cdd:PRK15439 321 MLNGKEINALSTA--QRLARglvylpedRQSSGLYLDAPLAWNVCA----------LTHNRRGfwikpARENavLERYRR 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 149 MLDaVKMPEARKRMRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 228
Cdd:PRK15439 389 ALN-IKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSD 462
|
250
....*....|....*...
gi 495069250 229 LGVVAGICDKVLVMYAGR 246
Cdd:PRK15439 463 LEEIEQMADRVLVMHQGE 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-246 |
9.08e-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: 101.44 E-value: 9.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllAANGRIGGSATFNGREIlnlPERELNRLRAEQISMIFQD-PMTSL 117
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGKFEGNVFINGKPV---DIRNPAQAIRAGIAMVPEDrKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 118 NPYMRVGEQL-MEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYP-HEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:TIGR02633 351 VPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495069250 196 TTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
39-246 |
1.26e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.16 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllAANGRIGGSATFNGREI-LNLPERELnrlrAEQISMIFQD-PMTS 116
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGRWEGEIFIDGKPVkIRNPQQAI----AQGIAMVPEDrKRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LNPYMRVGEQLmeVLMLHKSMSKAEAFEESvRMLDAVKmpEARKRMRM-YPHEF------SGGMRQRVMIAMALLCRPKL 189
Cdd:PRK13549 352 IVPVMGVGKNI--TLAALDRFTGGSRIDDA-AELKTIL--ESIQRLKVkTASPElaiarlSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 190 LIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-261 |
1.36e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.97 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 17 ATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPER 96
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRS---GSIRFDGEDITGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ELNRLRaeqISM------IFqdpmtslnPYMRVGEQLMEVLMLHKSMSK-AEAFEesvRMLDAVkmPEARKRMRMYPHEF 169
Cdd:COG0410 74 RIARLG---IGYvpegrrIF--------PSLTVEENLLLGAYARRDRAEvRADLE---RVYELF--PRLKERRRQRAGTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTME 249
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVL 216
|
250
....*....|..
gi 495069250 250 YGKAREVFYDPA 261
Cdd:COG0410 217 EGTAAELLADPE 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-246 |
1.38e-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: 95.36 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRlraeQ 105
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS---GRVRLDGADISQWDPNELGD----H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 106 ISMIFQDpmtslnpymrvgeqlmevlmlhksmskAEAFEESVRmlDAVkmpearkrmrmypheFSGGMRQRVMIAMALLC 185
Cdd:cd03246 78 VGYLPQD---------------------------DELFSGSIA--ENI---------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLA-SADRILVLEDGR 172
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-227 |
1.84e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.04 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 7 SAPQQTAASQATLLDVKDLRVtfATPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGL-LAANGRIGGSAt 84
Cdd:COG4178 350 EAASRIETSEDGALALEDLTL--RTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKS-TLLrAIAGLwPYGSGRIARPA- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 85 fnGREILNLPERelnrlraeqismifqdpmtslnPYMRVGEqLMEVL---MLHKSMSKAEAfeesVRMLDAVKMPEARKR 161
Cdd:COG4178 425 --GARVLFLPQR----------------------PYLPLGT-LREALlypATAEAFSDAEL----REALEAVGLGHLAER 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 162 M---RMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkREFNTAIIMITH 227
Cdd:COG4178 476 LdeeADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-246 |
2.08e-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: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRlraeQI 106
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTS---GSVLLDGTDIRQLDPADLRR----NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 107 SMIFQDPMTSlnpYMRVGEQLMevlmlhksMSKAEAfeESVRMLDAVKMPEARKRMRMYPHEF-----------SGGMRQ 175
Cdd:cd03245 81 GYVPQDVTLF---YGTLRDNIT--------LGAPLA--DDERILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-256 |
5.29e-23 |
|
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: 95.63 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFA-TPDGDVtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsaTFNGREILNLperELNRLRA 103
Cdd:cd03252 5 HVRFRyKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRV----LVDGHDLALA---DPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 104 eQISMIFQDPmTSLNPYMRvgeqlmEVLMLHKSMSKAEAFEESVRMLDA----VKMPEARKRM-RMYPHEFSGGMRQRVM 178
Cdd:cd03252 77 -QVGVVLQEN-VLFNRSIR------DNIALADPGMSMERVIEAAKLAGAhdfiSELPEGYDTIvGEQGAGLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKAREV 256
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
42-257 |
5.92e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 95.68 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 42 LNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANGRIggsaTFNGREILNLPERELNRLRAeqisMIFQDPMTSLNpy 120
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLPGQGEI----LLNGRPLSDWSAAELARHRA----YLSQQQSPPFA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 121 MRVGEQLMevLMLHKSMSKAEAFEESVRMLDAVKMpeARKRMRMYpHEFSGGMRQRVMIAMALL-------CRPKLLIAD 193
Cdd:COG4138 84 MPVFQYLA--LHQPAGASSEAVEQLLAQLAEALGL--EDKLSRPL-TQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495069250 194 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVF 257
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGIT-VVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-227 |
7.55e-23 |
|
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: 94.65 E-value: 7.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 32 PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREilnlPERELNRlraEQISMIFQ 111
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQP----RKPDQFQ---KCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 112 DpmTSLNPYMRVGEQL--MEVLMLHKSMSKA--EAFEESVRMLDAVKMPEARKRMRmyphEFSGGMRQRVMIAMALLCRP 187
Cdd:cd03234 89 D--DILLPGLTVRETLtyTAILRLPRKSSDAirKKRVEDVLLRDLALTRIGGNLVK----GISGGERRRVSIAVQLLWDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495069250 188 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 227
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
34-278 |
8.24e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 8.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRlraeQISMIFQDP 113
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS---GTVFLGDKPISMLSSRQLAR----RLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 MT------------SLNPYM----RVG---EQLMEvlmlhKSMSKAEAFEESVRMLDavkmpearkrmrmyphEFSGGMR 174
Cdd:PRK11231 86 LTpegitvrelvayGRSPWLslwgRLSaedNARVN-----QAMEQTRINHLADRRLT----------------DLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAR 254
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
250 260
....*....|....*....|....
gi 495069250 255 EVFydpahpySIGLLNAVPRLDAE 278
Cdd:PRK11231 224 EVM-------TPGLLRTVFDVEAE 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
27-242 |
1.46e-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: 98.13 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRlraeQI 106
Cdd:TIGR02857 327 VSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE---GSIAVNGVPLADADADSWRD----QI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 107 SMIFQdpmtslNPYMRVGeQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYP-----HEFSGGMRQRVMIAM 181
Cdd:TIGR02857 399 AWVPQ------HPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVM 242
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-246 |
1.82e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.77 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSQtafaLMGLL-AANGRIGGSATFNGREILNL-PERELnrlrAEQISMIFQD---- 112
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTE----LMKVLyGALPRTSGYVTLDGHEVVTRsPQDGL----ANGIVYISEDrkrd 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 ------------PMTSLNPYMRVGEQLmevlmlhKSMSKAEAFEESVRMLDaVKMPEARKRMRMypheFSGGMRQRVMIA 180
Cdd:PRK10762 340 glvlgmsvkenmSLTALRYFSRAGGSL-------KHADEQQAVSDFIRLFN-IKTPSMEQAIGL----LSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-256 |
2.99e-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: 93.30 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNL-PERelnrlraeqiSMIFQDpmTS 116
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLISGlAQPTSGGVILEGKQITEPgPDR----------MVVFQN--YS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LNPYMRVGEQL-MEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:TIGR01184 65 LLPWLTVRENIaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 196 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| 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 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPERELNRLRaEQISMIFQD 112
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKS----TLLKLICGIERpSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 PMTSLNpyMRVGEQLMEVLMLhksmskAEAFEESVR-----MLDAVKMPEarkRMRMYPHEFSGGMRQRVMIAMALLCRP 187
Cdd:PRK10908 88 HHLLMD--RTVYDNVAIPLII------AGASGDDIRrrvsaALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 188 KLLIADEPTTALDVTVQAQIMTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-246 |
4.32e-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: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaaNGR---IGGSATFNGREILNLPER 96
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG----HPKyevTSGSILLDGEDILELSPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 97 ElnrlRA-EQISMIFQDPM------------TSLNpymRVGEQLMEVLMLHKSMSKAeafeesvrmLDAVKMPEA-RKRm 162
Cdd:COG0396 73 E----RArAGIFLAFQYPVeipgvsvsnflrTALN---ARRGEELSAREFLKLLKEK---------MKELGLDEDfLDR- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 163 rmYPHE-FSGGMRQRVMIA-MALLcRPKLLIADEPTTALDVTVqAQIMT-LLNELKREfNTAIIMITH-----DLGVVag 234
Cdd:COG0396 136 --YVNEgFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIDA-LRIVAeGVNKLRSP-DRGILIITHyqrilDYIKP-- 208
|
250
....*....|..
gi 495069250 235 icDKVLVMYAGR 246
Cdd:COG0396 209 --DFVHVLVDGR 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
15-260 |
5.13e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.13 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 15 SQATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLP 94
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG---GTILLRGQHIEGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 95 ERELNRL---RAEQISMIFQDpMTSLNPYMRVGEQLMEVLMLHKSM-------SKAEAFEESVRMLDAVKMPEARKRMrm 164
Cdd:PRK11300 74 GHQIARMgvvRTFQHVRLFRE-MTVIENLLVAQHQQLKTGLFSGLLktpafrrAESEALDRAATWLERVGLLEHANRQ-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 165 yPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 244
Cdd:PRK11300 151 -AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
250
....*....|....*.
gi 495069250 245 GRTMEYGKAREVFYDP 260
Cdd:PRK11300 230 GTPLANGTPEEIRNNP 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-251 |
5.33e-22 |
|
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: 91.46 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFATPDGDVTA--VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLaANGRIGGSATFNGReilNLPERE 97
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEVLINGR---PLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNRlraeQISMIFQDpmtslnpymrvgeqlmevLMLHKSMSKAEAFEESVRMldavkmpeaRKrmrmypheFSGGMRQRV 177
Cdd:cd03213 80 FRK----IIGYVPQD------------------DILHPTLTVRETLMFAAKL---------RG--------LSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDL-GVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-251 |
6.14e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREIlnlpeRELNR--LRaE 104
Cdd:PRK13657 340 VSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINL--LQRVFDPQSGRILIDGTDI-----RTVTRasLR-R 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 QISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKSMSKAEA---FEESVRMLDAVkmpeARKRMRMypheFSGGMRQRVM 178
Cdd:PRK13657 410 NIAVVFQDAGlfnRSIEDNIRVGRPDATDEEMRAAAERAQAhdfIERKPDGYDTV----VGERGRQ----LSGGERQRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
37-261 |
7.92e-22 |
|
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: 92.22 E-value: 7.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 37 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRLraeQISMIFQDPmtS 116
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS---GKILLDGQDITKLPMHKRARL---GIGYLPQEA--S 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LNPYMRVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRMRMYpheFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:cd03218 86 IFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHITHLRKSKASS---LSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 197 TALDVTVQAQIMTLLNELKrefNTAI-IMIT-HDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPA 261
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILK---DRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-251 |
8.18e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.84 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDlrVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEreln 99
Cdd:cd03247 1 LSINN--VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQ---GEITLDGVPVSDLEK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 rLRAEQISMIFQDPM---TSLnpYMRVGEQlmevlmlhksmskaeafeesvrmldavkmpearkrmrmypheFSGGMRQR 176
Cdd:cd03247 72 -ALSSLISVLNQRPYlfdTTL--RNNLGRR------------------------------------------FSGGERQR 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYG 251
Cdd:cd03247 107 LALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
31-256 |
9.14e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 31 TPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTafaLMGLLA-----------ANGRIGG----SATFN----GRE-- 89
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKS-T---LLKLIAgileptsgrveVNGRVSAllelGAGFHpeltGREni 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 90 -----ILNLPERELNRLRAEqismIfqdpmtslnpymrvgeqlmevlmlhksmskaEAFEEsvrmL-DAVKMPearkrMR 163
Cdd:COG1134 110 ylngrLLGLSRKEIDEKFDE----I-------------------------------VEFAE----LgDFIDQP-----VK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 164 MYphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMY 243
Cdd:COG1134 146 TY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
250
....*....|...
gi 495069250 244 AGRTMEYGKAREV 256
Cdd:COG1134 221 KGRLVMDGDPEEV 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-267 |
1.04e-21 |
|
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: 95.66 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA---NGRIGGSATFNGREILNLPE 95
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKS----TLMKILSGvypHGTWDGEIYWSGSPLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRlraEQISMIFQDPMtsLNPYMRVGEQLM---EVLMLHKSMSKAEAFEESVRMLDAVK---MPEARKRMrmyphEF 169
Cdd:TIGR02633 73 RDTER---AGIVIIHQELT--LVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQldaDNVTRPVG-----DY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR--- 246
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQhva 221
|
250 260 270
....*....|....*....|....*....|....
gi 495069250 247 -------------TMEYGKAREVFYdPAHPYSIG 267
Cdd:TIGR02633 222 tkdmstmseddiiTMMVGREITSLY-PHEPHEIG 254
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-227 |
1.27e-21 |
|
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: 89.91 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFATPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGGSAtfnGREILNLPERelnrlrae 104
Cdd:cd03223 5 NLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWpWGSGRIGMPE---GEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 qismifqdpmtslnPYMRVGeQLMEVLMlhksmskaeafeesvrmldavkmpearkrmrmYP--HEFSGGMRQRVMIAMA 182
Cdd:cd03223 73 --------------PYLPLG-TLREQLI--------------------------------YPwdDVLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495069250 183 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrefnTAIIMITH 227
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-255 |
1.61e-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: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDlrVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-----ANGRIggsaTFNGREILNLp 94
Cdd:cd03251 1 VEFKN--VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPrfydvDSGRI----LIDGHDVRDY- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 95 erELNRLRaEQISMIFQDpmtslnpymrvgeqlmeVLMLHKSM------SKAEAFEESVRmlDAVKMPEArkrmrmypHE 168
Cdd:cd03251 70 --TLASLR-RQIGLVSQD-----------------VFLFNDTVaeniayGRPGATREEVE--EAARAANA--------HE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 169 F-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDL 229
Cdd:cd03251 120 FimelpegydtvigergvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRL 197
|
250 260
....*....|....*....|....*.
gi 495069250 230 GVVAGIcDKVLVMYAGRTMEYGKARE 255
Cdd:cd03251 198 STIENA-DRIVVLEDGKIVERGTHEE 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-256 |
1.96e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 91.53 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 42 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsaTFNGREILNLPERELNRLRA---EQISMIFqdpmtsln 118
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSI----QFAGQPLEAWSAAELARHRAylsQQQTPPF-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 119 pymrvgeqLMEV---LMLHKSMSKAEAFEESV--RMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALL-----CRP- 187
Cdd:PRK03695 83 --------AMPVfqyLTLHQPDKTRTEAVASAlnEVAEALGLDDKLGRS---VNQLSGGEWQRVRLAAVVLqvwpdINPa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 188 -KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:PRK03695 152 gQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-251 |
2.39e-21 |
|
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: 89.89 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTfatpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaANGRI-GGSATFNGREILNLPEREL 98
Cdd:cd03217 1 LEIKDLHVS----VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVtEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLraeQISMIFQDPMtslnpymrvgeqlmEVlmlhksmskaeafeESVRMLDAVKmpearkrmrmYPHE-FSGGMRQRV 177
Cdd:cd03217 75 ARL---GIFLAFQYPP--------------EI--------------PGVKNADFLR----------YVNEgFSGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI-CDKVLVMYAGRTMEYG 251
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
42-257 |
2.59e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 42 LNFSLRAgeTLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGrEILNLPERELNRLRaEQISMIFQDPMTSLNpYM 121
Cdd:PRK13638 22 LDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQK---GAVLWQG-KPLDYSKRGLLALR-QQVATVFQDPEQQIF-YT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 122 RVGEQLMEVLmlhKSMSKAEAfEESVRMLDAVKMPEArKRMRMYPHE-FSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:PRK13638 94 DIDSDIAFSL---RNLGVPEA-EITRRVDEALTLVDA-QHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 201 VTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICDKVLVMYAGRTMEYGKAREVF 257
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-229 |
4.42e-21 |
|
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: 93.96 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 5 ELSAPQQ-TAASQATLLDVKDLRVTFatpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSA 83
Cdd:TIGR02868 319 EGSAPAAgAVGLGKPTLELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP---LQGEV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 84 TFNGREILNLPERELNRLraeqISMIFQDPM---TSLNPYMRVG------EQLMEVLmlhksmskaeafeESVRMLDAVK 154
Cdd:TIGR02868 393 TLDGVPVSSLDQDEVRRR----VSVCAQDAHlfdTTVRENLRLArpdatdEELWAAL-------------ERVGLADWLR 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 155 MPEARKRMRMYPH--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDL 229
Cdd:TIGR02868 456 ALPDGLDTVLGEGgaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-251 |
6.15e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 1 MSTIELSAPQQTAASQATL-LDVKDLRVTfaTPDGDVTAVNdLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGri 79
Cdd:PRK11174 330 TPLAHPQQGEKELASNDPVtIEAEDLEIL--SPDGKTLAGP-LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 80 ggSATFNGREilnLPERELNRLRaEQISMIFQDPmtslnpymrvgeQLME-VLMLHKSMSKAEAFEESVRMLDAvkmpea 158
Cdd:PRK11174 405 --SLKINGIE---LRELDPESWR-KHLSWVGQNP------------QLPHgTLRDNVLLGNPDASDEQLQQALE------ 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 159 rkrmRMYPHEF-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFN 219
Cdd:PRK11174 461 ----NAWVSEFlpllpqgldtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQT 536
|
250 260 270
....*....|....*....|....*....|..
gi 495069250 220 TaiIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:PRK11174 537 T--LMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
34-261 |
8.91e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 91.70 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGREILNlperelNRLRAEQISMIFQD 112
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQI----FIDGEDVTH------RSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pmTSLNPYMRVGEQLMEVL-MLhkSMSKAEAFE---ESVRMLDAVKMpEARkrmrmYPHEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK11432 87 --YALFPHMSLGENVGYGLkML--GVPKEERKQrvkEALELVDLAGF-EDR-----YVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 189 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPA 261
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-262 |
9.33e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.16 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 37 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREILNLpeRELNRLRaEQISMIFQDPm 114
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYRYSGDVLLGGRSIFNY--RDVLEFR-RRVGMLFQRP- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 115 tslNPY-MRVGEQLMEVLMLHKSMSK------AEAFEESVRMLDAVKmpearKRMRMYPHEFSGGMRQRVMIAMALLCRP 187
Cdd:PRK14271 111 ---NPFpMSIMDNVLAGVRAHKLVPRkefrgvAQARLTEVGLWDAVK-----DRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 188 KLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAH 262
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-264 |
1.20e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.09 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 41 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGReILNLPERELNrLRAEQ--ISMIFQDpmTSL 117
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQkGRI----VLNGR-VLFDAEKGIC-LPPEKrrIGYVFQD--ARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 118 NPYMRV-GEqlmevlmLHKSMSK--AEAFEESVRMLDAVKMpearkrMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK11144 88 FPHYKVrGN-------LRYGMAKsmVAQFDKIVALLGIEPL------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPA-HPY 264
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-240 |
1.78e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.02 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriggsatfngreilnlpERE 97
Cdd:PRK09544 3 SLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD------------------EGV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 LNRLRAEQISMIFQDpmTSLNPYMRVgeQLMEVLMLHKSMSKAEafeesvrMLDAVKMPEARKRMRMYPHEFSGGMRQRV 177
Cdd:PRK09544 61 IKRNGKLRIGYVPQK--LYLDTTLPL--TVNRFLRLRPGTKKED-------ILPALKRVQAGHLIDAPMQKLSGGETQRV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 240
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
33-257 |
3.06e-20 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 87.67 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 33 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPErelNRLRaEQISMIFQD 112
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDIRDISR---KSLR-SMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pmtslnPYMRVGEqLMEVLMLHKSMSKAEAFEESVRMLDAvkMPEARKRMRMYPHE-------FSGGMRQRVMIAMALLC 185
Cdd:cd03254 86 ------TFLFSGT-IMENIRLGRPNATDEEVIEAAKEAGA--HDFIMKLPNGYDTVlgenggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 186 RPKLLIADEPTTALDV----TVQAQIMTLLNelkrefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKAREVF 257
Cdd:cd03254 157 DPKILILDEATSNIDTetekLIQEALEKLMK------GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
38-229 |
9.36e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRI---GGSATFNGREIlNLPERElnrlRAeqisMIFQDpm 114
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKT----TLLNLIA--GFVpyqHGSITLDGKPV-EGPGAE----RG----VVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 115 TSLNPYMRVGEQLMEVLMLhKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 495069250 195 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 229
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-294 |
9.84e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 9.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 16 QATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangrigGSATFNGREIL--NL 93
Cdd:PRK11247 9 QGTPLLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLA------GLETPSAGELLagTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 PereLNRLRaEQISMIFQDpmTSLNPYMRVgeqLMEVLMLHKSMSKAEAFEesvrMLDAVKMPEarkRMRMYPHEFSGGM 173
Cdd:PRK11247 75 P---LAEAR-EDTRLMFQD--ARLLPWKKV---IDNVGLGLKGQWRDAALQ----ALAAVGLAD---RANEWPAALSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTmeygkA 253
Cdd:PRK11247 139 KQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-----G 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495069250 254 REVFYDPAHPYSIGllnaVPRLDA-EGESL---LTIPGNPPNLLR 294
Cdd:PRK11247 214 LDLTVDLPRPRRRG----SARLAElEAEVLqrvMSRGESEPTRLR 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-246 |
1.37e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 35 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREILnlPERELNRLRaEQISMIFQD-- 112
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDKRAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITESrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 -----PMTSLNPYMRVGEQLME------VLMLHKSMSKAEAfeESVRMLDAVKMPEARKRMRmyphEFSGGMRQRVMIAM 181
Cdd:PRK09700 349 dngffPNFSIAQNMAISRSLKDggykgaMGLFHEVDEQRTA--ENQRELLALKCHSVNQNIT----ELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-255 |
1.46e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 89.39 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangRI----GGSATFNGREILNLPERELNRLR 102
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIP---RFyepdSGQILLDGHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 103 A--EQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEEsvRMLDAVKMPEARKRMRMyphefSGGMRQRVMIA 180
Cdd:TIGR02203 409 AlvSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVD--KLPLGLDTPIGENGVLL-----SGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGRTMEYGKARE 255
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-251 |
2.02e-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: 85.28 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 23 KDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriGGSATFNGREIlnlperelnrlR 102
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLLA-----GIYPPDSGTVT-----------V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 103 AEQISMIFqDPMTSLNPYMRVGEQLMEVLMLHkSMSKAE--AFEESVRML----DAVKMPearkrMRMYphefSGGMRQR 176
Cdd:cd03220 82 RGRVSSLL-GLGGGFNPELTGRENIYLNGRLL-GLSRKEidEKIDEIIEFselgDFIDLP-----VKTY----SSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 251
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-257 |
2.08e-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: 85.91 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGRI----GGSATFNGREILNL 93
Cdd:COG1119 2 PLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLI--TGDLpptyGNDVRLFGERRGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 PERELnRLRAEQISMIFQDpmtslnpYMRVGEQLMEVLM--------LHKSMSKAEAfEESVRMLDAVKMpeARKRMRMY 165
Cdd:COG1119 72 DVWEL-RKRIGLVSPALQL-------RFPRDETVLDVVLsgffdsigLYREPTDEQR-ERARELLELLGL--AHLADRPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 166 pHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG-VVAGIcDKVLVMYA 244
Cdd:COG1119 141 -GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVLLLKD 218
|
250
....*....|...
gi 495069250 245 GRTMEYGKAREVF 257
Cdd:COG1119 219 GRVVAAGPKEEVL 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-260 |
2.10e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.47 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPereLN 99
Cdd:COG1137 4 LEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS---GRIFLDGEDITHLP---MH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RlRA-------EQISMIFQDpMTslnpymrVGEQLMEVLMLHKsMSKAEAFEESVRMLDAVKMPEARKRMRMYpheFSGG 172
Cdd:COG1137 74 K-RArlgigylPQEASIFRK-LT-------VEDNILAVLELRK-LSKKEREERLEELLEEFGITHLRKSKAYS---LSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALD-VTVqAQIMTLLNELKrEFNTAIImIT-HD----LgvvaGICDKVLVMYAGR 246
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVL-ITdHNvretL----GICDRAYIISEGK 213
|
250
....*....|....
gi 495069250 247 TMEYGKAREVFYDP 260
Cdd:COG1137 214 VLAEGTPEEILNNP 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-256 |
2.63e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.56 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPERELNRlraeQ 105
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP---TSGSVRLDGADLKQWDRETFGK----H 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 106 ISmifqdpmtslnpYMRVGEQLMEVlMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEF-----------SGGMR 174
Cdd:TIGR01842 394 IG------------YLPQDVELFPG-TVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYdtvigpggatlSGGQR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 175 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGIcDKVLVMYAGRTMEYGKAR 254
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGCV-DKILVLQDGRIARFGERD 538
|
..
gi 495069250 255 EV 256
Cdd:TIGR01842 539 EV 540
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
27-255 |
2.98e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.54 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGreiLNLPERELNRLRaEQI 106
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDE---GEILLDG---HDLRDYTLASLR-NQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 107 SMI------FQDPMTSLNPYMRvgeqlmevlmlHKSMSKAEaFEESVRMLDAV----KMPEARKRMrmyPHE----FSGG 172
Cdd:PRK11176 420 ALVsqnvhlFNDTIANNIAYAR-----------TEQYSREQ-IEEAARMAYAMdfinKMDNGLDTV---IGEngvlLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGK 252
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
...
gi 495069250 253 ARE 255
Cdd:PRK11176 562 HAE 564
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-252 |
4.25e-19 |
|
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: 84.14 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 43 NFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPERElnrlraEQISMIFQDpmTSLNPYMR 122
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP---ASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 123 VGEQLmeVLMLHKSMsKAEAfEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 202
Cdd:TIGR01277 87 VRQNI--GLGLHPGL-KLNA-EQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495069250 203 VQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:TIGR01277 163 LREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-260 |
5.27e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.24 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFAtpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEREL 98
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS---GSVLIRGEPITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NRLraeqISMIFQDPMTSL-NPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDavkMPEARKRMrmyPHEFSGGMRQRV 177
Cdd:PRK13652 77 RKF----VGLVFQNPDDQIfSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLG---LEELRDRV---PHHLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVF 257
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
...
gi 495069250 258 YDP 260
Cdd:PRK13652 227 LQP 229
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
44-242 |
6.64e-19 |
|
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: 84.13 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 44 FSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRI---GGSATFNGREILNLPERElnrlraeqiSMIFQDPMTSLNP 119
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVkvaGASPGKGWRHIGYVPQRH---------EFAWDFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 120 YMRVGEQLMEVLmlhkSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:TIGR03771 72 VMSGRTGHIGWL----RRPCVADFAAVRDALRRVGLTELADRP---VGELSGGQRQRVLVARALATRPSVLLLDEPFTGL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495069250 200 DVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:TIGR03771 145 DMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL 186
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-253 |
7.43e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 84.31 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgRIGGSATFNGREILNLPERE 97
Cdd:CHL00131 6 PILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYK-ILEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 lnrlRAEQ-ISMIFQDPMTSlnpymrVGEQLMEVLML-----HKSMSKAEA-----FEESVRMLDAVKMpEARKRMRMYP 166
Cdd:CHL00131 81 ----RAHLgIFLAFQYPIEI------PGVSNADFLRLaynskRKFQGLPELdplefLEIINEKLKLVGM-DPSFLSRNVN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 167 HEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGIC-DKVLVMYA 244
Cdd:CHL00131 150 EGFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKpDYVHVMQN 227
|
....*....
gi 495069250 245 GRTMEYGKA 253
Cdd:CHL00131 228 GKIIKTGDA 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
53-260 |
8.00e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 53 GIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREILnlpERE--LNRLRaEQISMIFQDPmtSLNPyMRVGEQL- 127
Cdd:PRK14258 37 AIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNQNIY---ERRvnLNRLR-RQVSMVHPKP--NLFP-MSVYDNVa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 128 --MEVLMLHKSMSKAEAFEESVRmlDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 205
Cdd:PRK14258 110 ygVKIVGWRPKLEIDDIVESALK--DADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASM 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 206 QIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA-----GRTMEYGKAREVFYDP 260
Cdd:PRK14258 188 KVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-282 |
8.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 26 RVTFATPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGGSATFNGrEILNLPE-RELnrlra 103
Cdd:PRK13644 6 NVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTG-DFSKLQGiRKL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 104 eqISMIFQDPMTSLnpymrVGEQLMEVLML---HKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIA 180
Cdd:PRK13644 79 --VGIVFQNPETQF-----VGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRHRS---PKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 181 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAgICDKVLVMYAGRTMEYGKAREVFYDP 260
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV 226
|
250 260
....*....|....*....|..
gi 495069250 261 AHPYsIGLlnAVPRLDAEGESL 282
Cdd:PRK13644 227 SLQT-LGL--TPPSLIELAENL 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-298 |
9.31e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 85.24 E-value: 9.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIlnlPEREln 99
Cdd:PRK13537 8 IDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA---GSISLCGEPV---PSRA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAEQISMIFQdpMTSLNPYMRVGEQLMeVLMLHKSMSKAEAFEESVRMLDAVKMpEARKRMRMypHEFSGGMRQRVMI 179
Cdd:PRK13537 76 RHARQRVGVVPQ--FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKL-ENKADAKV--GELSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 180 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAR----- 254
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHalies 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 495069250 255 -------EVFYDPAHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKG 298
Cdd:PRK13537 229 eigcdviEIYGPDPVALRDELAPLAERTEISGETLFCYVRDPEPLHARLKG 279
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-260 |
1.53e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 86.70 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRlraeQ 105
Cdd:TIGR00958 484 VSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG---GQVLLDGVPLVQYDHHYLHR----Q 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 106 ISMIFQDPmtslnpymrvgeqlmeVLM---LHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEF-----------SG 171
Cdd:TIGR00958 557 VALVGQEP----------------VLFsgsVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYdtevgekgsqlSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAqimtLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
....*....
gi 495069250 252 KAREVFYDP 260
Cdd:TIGR00958 696 THKQLMEDQ 704
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-262 |
1.96e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 11 QTAASQATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQT--AFALMGLLAANGRIGGSATFNGR 88
Cdd:PRK14243 2 STLNGTETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrCFNRLNDLIPGFRVEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 89 EiLNLPERELNRLRaEQISMIFQDPmtslNPYMR-VGEQLM---EVLMLHKSMSkaEAFEESVRmlDAVKMPEARKRMRM 164
Cdd:PRK14243 78 N-LYAPDVDPVEVR-RRIGMVFQKP----NPFPKsIYDNIAygaRINGYKGDMD--ELVERSLR--QAALWDEVKDKLKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 165 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYA 244
Cdd:PRK14243 148 SGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNV 225
|
250 260
....*....|....*....|....*..
gi 495069250 245 ---------GRTMEYGKAREVFYDPAH 262
Cdd:PRK14243 226 eltegggryGYLVEFDRTEKIFNSPQQ 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-257 |
7.90e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 14 ASQATLLdVKDLRVTFATPDgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGgsatfngreILN 92
Cdd:PRK15056 2 MQQAGIV-VNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVrLASGKIS---------ILG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 93 LPERElnRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVkmpeARKRMRMYPH----E 168
Cdd:PRK15056 69 QPTRQ--ALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAAL----ARVDMVEFRHrqigE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICDKVlVMYAGRTM 248
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYT-VMVKGTVL 220
|
....*....
gi 495069250 249 EYGKAREVF 257
Cdd:PRK15056 221 ASGPTETTF 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
38-259 |
1.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.71 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPE-RELNRLRaEQISMIFQDPMTs 116
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ---GSVRVDDTLITSTSKnKDIKQIR-KKVGLVFQFPES- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 lnpymrvgeQLMEVLMLHKSMSKAEAFeeSVRMLDAVKMpeARKRMRMY----------PHEFSGGMRQRVMIAMALLCR 186
Cdd:PRK13649 97 ---------QLFEETVLKDVAFGPQNF--GVSQEEAEAL--AREKLALVgiseslfeknPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 187 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYD 259
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-252 |
1.34e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.34 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 8 APQQTAASQATLLDVKDlrVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAN-----GRIggs 82
Cdd:PRK11160 327 PTTSTAAADQVSLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAwdpqqGEI--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 83 aTFNGREILNLPERELnrlRAeQISMIFQdpmtslnpymRV---GEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEAR 159
Cdd:PRK11160 398 -LLNGQPIADYSEAAL---RQ-AISVVSQ----------RVhlfSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 160 KRMRMYPHE----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGI 235
Cdd:PRK11160 463 KGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF 540
|
250
....*....|....*..
gi 495069250 236 cDKVLVMYAGRTMEYGK 252
Cdd:PRK11160 541 -DRICVMDNGQIIEQGT 556
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
5-252 |
1.43e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 5 ELSAPQQTAASQATLLDVKDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSAT 84
Cdd:TIGR00955 7 NSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 85 FNGREIlnlpERELNRLRAeqiSMIFQDPMtsLNPYMRVGEQLMEVLML--HKSMSKAEAFEESVRMLDAVKMPEARK-- 160
Cdd:TIGR00955 87 LNGMPI----DAKEMRAIS---AYVQQDDL--FIPTLTVREHLMFQAHLrmPRRVTKKEKRERVDEVLQALGLRKCANtr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 161 -----RMRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGI 235
Cdd:TIGR00955 158 igvpgRVK----GLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFEL 233
|
250
....*....|....*..
gi 495069250 236 CDKVLVMYAGRTMEYGK 252
Cdd:TIGR00955 234 FDKIILMAEGRVAYLGS 250
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
34-252 |
1.83e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsatfngrEILNLPERELNRLRAEQISMIFQd 112
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDaGKI---------TVLGVPVPARARLARARIGVVPQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pMTSLNPYMRVGEQLMeVLMLHKSMSKAEAFEESVRMLDAVKMpEARKRMRMypHEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PRK13536 122 -FDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARL-ESKADARV--SDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 193 DEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGK 252
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVLEAGRKIAEGR 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-256 |
2.48e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA---ANGRI----------------- 79
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyepTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 80 ---------GGSATFNGREILNLPERELNRLRaEQISMIFQDPMtSLNPYMRVGEQLMEVLmlHKSMSKA-EAFEESVRM 149
Cdd:TIGR03269 77 kvgepcpvcGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEAL--EEIGYEGkEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 150 LDAVKMPEarkRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 229
Cdd:TIGR03269 153 IEMVQLSH---RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*..
gi 495069250 230 GVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-246 |
2.62e-17 |
|
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: 79.44 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFATPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNR 100
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG---GQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 101 lraeQISMIFQDPMT---SLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMyphefSGGMRQRV 177
Cdd:cd03248 89 ----KVSLVGQEPVLfarSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL-----SGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGR 246
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-246 |
2.63e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.63 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 43 NFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANGrigGSATFNGREILNLPERElnrlraEQISMIFQDpmTSLNPYM 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIaGFLTPAS---GSLTLNGQDHTTTPPSR------RPVSMLFQE--NNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 122 RVGEQLmeVLMLHKSMSKAEAFEESVR-MLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 200
Cdd:PRK10771 87 TVAQNI--GLGLNPGLKLNAAQREKLHaIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495069250 201 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-246 |
4.03e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 78.69 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 41 DLNFSLRAGETLGIVGESGSGKSQTAFALMG-LLAANGRIggsaTFNGREILNLPERElnrlraEQISMIFQDpmTSLNP 119
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRV----LINGVDVTAAPPAD------RPVSMLFQE--NNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 120 YMRVgEQ---LMEVLMLHKSMSKAEAFEESVRmldavKMPEARKRMRMyPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:cd03298 84 HLTV-EQnvgLGLSPGLKLTAEDRQAIEVALA-----RVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495069250 197 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-249 |
4.63e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 81.76 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA---ANGRIGGSATFNGREilnlpe 95
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKS----TLMKVLSgvyPHGSYEGEILFDGEV------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRLRA-EQ--ISMIFQDpmTSLNPYMRVGEQLMevlmLHKSMSK------AEAFEESVRMLDAVKMPEArkrmrmyP 166
Cdd:NF040905 67 CRFKDIRDsEAlgIVIIHQE--LALIPYLSIAENIF----LGNERAKrgvidwNETNRRARELLAKVGLDES-------P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 167 HEFSG----GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVM 242
Cdd:NF040905 134 DTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVL 212
|
....*..
gi 495069250 243 YAGRTME 249
Cdd:NF040905 213 RDGRTIE 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
34-233 |
5.39e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIGGSAtfnGREILNLPER-ELNR---LRAEQ-IS 107
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRAG---GARVAYVPQRsEVPDslpLTVRDlVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 108 MIFQDPMTSLNPYMRvgeqlmevlmlhksmskaEAFEESVRMLDAVKMPEARKRMRmypHEFSGGMRQRVMIAMALLCRP 187
Cdd:NF040873 80 MGRWARRGLWRRLTR------------------DDRAAVDDALERVGLADLAGRQL---GELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495069250 188 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVA 233
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-246 |
6.61e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 81.31 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 9 PQQTAASQATLLDVKDLrvtfatpdgdvTAVN-----DLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSA 83
Cdd:PRK10982 240 PDKENKPGEVILEVRNL-----------TSLRqpsirDVSFDLHKGEILGIAGLVGAKRTDIVETLFGI---REKSAGTI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 84 TFNGREILNlperelnRLRAEQISMIF-----QDPMTSLNPYMRVGeqlmevlmLHKSMSKAEAFEESVRMLDAVKMPEA 158
Cdd:PRK10982 306 TLHGKKINN-------HNANEAINHGFalvteERRSTGIYAYLDIG--------FNSLISNIRNYKNKVGLLDNSRMKSD 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 159 RK------RMRMYPHE-----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 227
Cdd:PRK10982 371 TQwvidsmRVKTPGHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISS 449
|
250
....*....|....*....
gi 495069250 228 DLGVVAGICDKVLVMYAGR 246
Cdd:PRK10982 450 EMPELLGITDRILVMSNGL 468
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
49-280 |
9.06e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.08 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 49 GETLGIVGESGSGKSQTAFALMGLLAANGriggsatFNGREILNlpERELNRLRAEQISMIFQDPMtsLNPYMRVGEQLM 128
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNN-------FTGTILAN--NRKPTKQILKRTGFVTQDDI--LYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 129 --EVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRM--RMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ 204
Cdd:PLN03211 163 fcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 205 AQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARE-------VFYDPAHP-----YSIGLLNAV 272
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDamayfesVGFSPSFPmnpadFLLDLANGV 322
|
....*...
gi 495069250 273 PRLDAEGE 280
Cdd:PLN03211 323 CQTDGVSE 330
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
34-269 |
1.29e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.69 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATFNGREILN-LPERELNrlraeqISMIFQD 112
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGDLFIGEKRMNdVPPAERG------VGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pmTSLNPYMRVGEQLMEVLMLHKSmSKAEA---FEESVRMLDAVKMPEARkrmrmyPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK11000 84 --YALYPHLSVAENMSFGLKLAGA-KKEEInqrVNQVAEVLQLAHLLDRK------PKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 190 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYDPAHPYSIGLL 269
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
34-256 |
1.62e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.82 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMG-LLAANGrigGSATFNGREILNLPERELnrlrAEQISMIFQD 112
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLPPDS---GEVLVDGLDVATTPSREL----AKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 PmtSLNPYMRVGEqlmevlmL--------HKSMSKAEAFEESVRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALL 184
Cdd:COG4604 84 N--HINSRLTVRE-------LvafgrfpySKGRLTAEDREIIDEAIAYLDLEDLADR---YLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495069250 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
37-259 |
2.61e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.24 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 37 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREILNLPERELNRlraEQISMIFQDPmtS 116
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP---RDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEA--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 196
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM---GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 197 TALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYD 259
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-259 |
4.43e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.43 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTF--ATPDgDVTAVNDLNFSLRAGETLGIVGESGSGKsqTAF-----ALmgLLAANGRI-------------GG 81
Cdd:PRK13651 5 VKNIVKIFnkKLPT-ELKALDNVSVEINQGEFIAIIGQTGSGK--TTFiehlnAL--LLPDTGTIewifkdeknkkktKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 82 SATFNGREILNLPERE----LNRLRaEQISMIFQdpmtsLNPYmrvgeQLMEVLMLHK------SM--SKAEAFEESVRM 149
Cdd:PRK13651 80 KEKVLEKLVIQKTRFKkikkIKEIR-RRVGVVFQ-----FAEY-----QLFEQTIEKDiifgpvSMgvSKEEAKKRAAKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 150 LDAVKMPEARkrMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDL 229
Cdd:PRK13651 149 IELVGLDESY--LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDL 225
|
250 260 270
....*....|....*....|....*....|
gi 495069250 230 GVVAGICDKVLVMYAGRTMEYGKAREVFYD 259
Cdd:PRK13651 226 DNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-228 |
4.90e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTafaLMGLLAanGRI---GGSATFNGREIL-----NL 93
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS-T---LLKILA--GELepdSGEVSIPKGLRIgylpqEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 PE--------------RELNRLRAE--QISMIFQDPMTSLNPYMRVGEQlMEVLMLHKSMSKAEafeesvRMLDAVKMPE 157
Cdd:COG0488 71 PLdddltvldtvldgdAELRALEAEleELEAKLAEPDEDLERLAELQEE-FEALGGWEAEARAE------EILSGLGFPE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 158 ARKRMRMypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtVQAqIMTLLNELKReFNTAIIMITHD 228
Cdd:COG0488 144 EDLDRPV--SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLKN-YPGTVLVVSHD 208
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-255 |
9.44e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 77.94 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIlnlpeRELNR--LRAe 104
Cdd:COG5265 363 VSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTS---GRILIDGQDI-----RDVTQasLRA- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 QISMIFQDpmTSL-------NpyMRVGeqlmevlmlhksmsKAEAFEESVRmlDAVKMPEArkrmrmypHEF-------- 169
Cdd:COG5265 433 AIGIVPQD--TVLfndtiayN--IAYG--------------RPDASEEEVE--AAARAAQI--------HDFieslpdgy 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 170 -----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDK 238
Cdd:COG5265 485 dtrvgerglklSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADE 561
|
250
....*....|....*..
gi 495069250 239 VLVMYAGRTMEYGKARE 255
Cdd:COG5265 562 ILVLEAGRIVERGTHAE 578
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-256 |
1.40e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 15 SQATLLDVKDLRVTfatpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGllaanGRI---GGSATFNGREIL 91
Cdd:PRK11831 3 SVANLVDMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKT-TLLRLIG-----GQIapdHGEILFDGENIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 92 NLPERELNRLRaEQISMIFQDP--MTSLNPYMRVGEQLMEvlmlHKSMSkAEAFEESVRM-LDAVKMPEARKRMrmyPHE 168
Cdd:PRK11831 73 AMSRSRLYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQLP-APLLHSTVMMkLEAVGLRGAAKLM---PSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 169 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 248
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
....*...
gi 495069250 249 EYGKAREV 256
Cdd:PRK11831 224 AHGSAQAL 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
38-259 |
2.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.54 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSATFNGREilnlpERELNRLRaEQISMIFQDPM 114
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEgkvTVGDIVVSSTSK-----QKEIKPVR-KKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 115 TslnpymrvgeQLMEVLMLHK--------SMSKAEAFEESVRMLDAVKMpeARKRMRMYPHEFSGGMRQRVMIAMALLCR 186
Cdd:PRK13643 95 S----------QLFEETVLKDvafgpqnfGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 187 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFYD 259
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-246 |
2.05e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.75 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFAT-PDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllAANGR-IGGSATFNGREI----- 90
Cdd:NF040905 256 VVFEVKNWTVYHPLhPERKV--VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGRnISGTVFKDGKEVdvstv 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 91 -------------------LNLPErELNRlraeQISMifqdpmTSLNPYMRVGeqlmeVLMLHKSMSKAEAFeesvrmld 151
Cdd:NF040905 332 sdaidaglayvtedrkgygLNLID-DIKR----NITL------ANLGKVSRRG-----VIDENEEIKVAEEY-------- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 152 avkmpeaRKRMRMYPH-------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIM 224
Cdd:NF040905 388 -------RKKMNIKTPsvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIV 459
|
250 260
....*....|....*....|..
gi 495069250 225 ITHDLGVVAGICDKVLVMYAGR 246
Cdd:NF040905 460 ISSELPELLGMCDRIYVMNEGR 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
39-251 |
3.00e-15 |
|
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: 73.07 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNG---REILNLPERELNRLRAEQISMifqdpmt 115
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGipyKEFAEKYPGEIIYVSEEDVHF------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 116 slnPYMRVGEQLMEVLMLhksmsKAEAFeesVRmldavkmpearkrmrmyphEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:cd03233 96 ---PTLTVRETLDFALRC-----KGNEF---VR-------------------GISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 196 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVA-GICDKVLVMYAGRTMEYG 251
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQIYYG 202
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-261 |
3.10e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREILNLPEREL 98
Cdd:PRK11650 4 LKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMVAGLERItSGEIWIGGRVVNELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 NrlraeqISMIFQDpmTSLNPYMRVgEQLMEVLMLHKSMSKAEAFEesvRMLDAVKMPE-----ARKrmrmyPHEFSGGM 173
Cdd:PRK11650 77 D------IAMVFQN--YALYPHMSV-RENMAYGLKIRGMPKAEIEE---RVAEAARILElepllDRK-----PRELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQiMTL-LNELKREFNTAIIMITHD------LGvvagicDKVLVMYAGR 246
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGGV 212
|
250
....*....|....*
gi 495069250 247 TMEYGKAREVFYDPA 261
Cdd:PRK11650 213 AEQIGTPVEVYEKPA 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-250 |
5.34e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 2 STIELSAPQqTAASQATLLDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRI-- 79
Cdd:COG0488 299 KTVEIRFPP-PERLGKKVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLLA--GELep 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 80 -GGSATFnGREIlnlperelnrlraeQISMIFQDpMTSLNPYMRVGEQLMEVlmlhksmsKAEAFEESVR-----ML--- 150
Cdd:COG0488 368 dSGTVKL-GETV--------------KIGYFDQH-QEELDPDKTVLDELRDG--------APGGTEQEVRgylgrFLfsg 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 151 DavkmpEARKRMRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHDL 229
Cdd:COG0488 424 D-----DAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-----LEEALDDFPGTVLLVSHDR 489
|
250 260
....*....|....*....|.
gi 495069250 230 GVVAGICDKVLVMYAGRTMEY 250
Cdd:COG0488 490 YFLDRVATRILEFEDGGVREY 510
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-277 |
5.53e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 3 TIELSAPQQTAAS--QATLLDVKDLRVTFAtpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIG 80
Cdd:PTZ00243 1290 VIEPASPTSAAPHpvQAGSLVFEGVQMRYR--EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV---CG 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 81 GSATFNGREILNLPERELNRlraeQISMIFQDPM-------TSLNPYMR-----VGEQLMEVLMLHKSMSKAEAFEEsvR 148
Cdd:PTZ00243 1365 GEIRVNGREIGAYGLRELRR----QFSMIPQDPVlfdgtvrQNVDPFLEassaeVWAALELVGLRERVASESEGIDS--R 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 149 MLDAvkmpearkrmrmyPHEFSGGMRQRVMIAMALLCRPKLLI-ADEPTT----ALDVTVQAQIMTLLNelkrefNTAII 223
Cdd:PTZ00243 1439 VLEG-------------GSNYSVGQRQLMCMARALLKKGSGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVI 1499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 495069250 224 MITHDLGVVAGiCDKVLVMYAGRTMEYGKAREVFYDPAHPYSiGLLNAVPRLDA 277
Cdd:PTZ00243 1500 TIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNRQSIFH-SMVEALGRSEA 1551
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
34-256 |
3.74e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPERELNRlraeQISMIFQDP 113
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHIQHYASKEVAR----RIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 MTSLNpyMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:PRK10253 91 TTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 194 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-242 |
4.19e-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: 68.63 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafalmgllaangriggsaTFngreilnlpereln 99
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKS--------------------TL-------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 rlraeqISMIfqdpmtslnpymrvgeqlmevlmlhksMSKAEAFEESVRMLDAVKMPearkrmrmYPHEFSGGMRQRVMI 179
Cdd:cd03221 43 ------LKLI---------------------------AGELEPDEGIVTWGSTVKIG--------YFEQLSGGEKMRLAL 81
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495069250 180 AMALLCRPKLLIADEPTTALDV-TVQAqimtLLNELKrEFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:cd03221 82 AKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALK-EYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-256 |
4.99e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-ANGRIGGSATFNGREILNLPerelNRLRAEQ-ISMIFQ 111
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSgIHEPTKGTITINNINYNKLD----HKLAAQLgIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 112 -----DPMTSL-NPYmrVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLC 185
Cdd:PRK09700 88 elsviDELTVLeNLY--IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 186 RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
42-257 |
7.34e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 42 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGREILNLPERELNRLraeqISMIFQDPMT----- 115
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRI----MIDDCDVAKFGLTDLRRV----LSIIPQSPVLfsgtv 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 116 --SLNPYMRVGE-QLMEVlmLHKSMSKaEAFEESVRMLDAvKMPEARKrmrmyphEFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PLN03232 1327 rfNIDPFSEHNDaDLWEA--LERAHIK-DVIDRNPFGLDA-EVSEGGE-------NFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 193 DEPTTALDVTVQAQIMTLLNElkrEFNT-AIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKAREVF 257
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE---EFKScTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
34-261 |
8.77e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.74 E-value: 8.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPErELNRlraEQISMIFQDP 113
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS---GTLLFEGEDISTLKP-EIYR---QQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 MTslnpymrVGEQLMEVLM----LHKSMSKAEAFeesVRMLDAVKMPEA--RKRMrmypHEFSGGMRQRVMIAMALLCRP 187
Cdd:PRK10247 91 TL-------FGDTVYDNLIfpwqIRNQQPDPAIF---LDDLERFALPDTilTKNI----AELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495069250 188 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMyagrTMEYGKAREVFYDPA 261
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL----QPHAGEMQEARYELA 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
39-262 |
1.53e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.86 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL----AANG-RIGGSATFNGREILNLPERELNRLRA-----EQISM 108
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGaRVTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 109 IFQ-DPMTSLNPYMrvgeqlmevlmlHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMAL---- 183
Cdd:PRK13547 97 AFSaREIVLLGRYP------------HARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 184 -----LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREVFy 258
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL- 243
|
....
gi 495069250 259 DPAH 262
Cdd:PRK13547 244 TPAH 247
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-259 |
4.48e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.12 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 18 TLLDVKDLRVTFATPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPE-- 95
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RELNRLRAeQISMIFQdpmtSLNPYMRVgeQLMEVLMLhKSMSKAEAFEESVRMLDAVKMPEA-----RKRMRMYPHE-- 168
Cdd:PRK09984 79 RDIRKSRA-NTGYIFQ----QFNLVNRL--SVLENVLI-GALGSTPFWRTCFSWFTREQKQRAlqaltRVGMVHFAHQrv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 169 --FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGr 246
Cdd:PRK09984 151 stLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG- 229
|
250
....*....|...
gi 495069250 247 tmeygkarEVFYD 259
Cdd:PRK09984 230 --------HVFYD 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
42-251 |
8.15e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 42 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGREILNLPERELNRLraeqISMIFQDPMT----- 115
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRI----LIDGCDISKFGLMDLRKV----LGIIPQAPVLfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 116 --SLNPYmrvGEqlmevlmlHKSMSKAEAFE-----ESVRM----LDAvKMPEARKrmrmyphEFSGGMRQRVMIAMALL 184
Cdd:PLN03130 1330 rfNLDPF---NE--------HNDADLWESLErahlkDVIRRnslgLDA-EVSEAGE-------NFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 185 CRPKLLIADEPTTALDVTVQAQIMTLLNElkrEFNT-AIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIRE---EFKScTMLIIAHRLNTIID-CDRILVLDAGRVVEFD 1454
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-246 |
8.77e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlperelnrlraeqismifqDP 113
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPV---------------------DA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 mTSLNPYMRVGeqlmevlmlhkSMSkaEAF----EESVR---MLDA--VKMPEARKRMRM-----------YPHEFSG-- 171
Cdd:NF033858 333 -GDIATRRRVG-----------YMS--QAFslygELTVRqnlELHArlFHLPAAEIAARVaemlerfdladVADALPDsl 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 172 --GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 246
Cdd:NF033858 399 plGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMN-EAERCDRISLMHAGR 474
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-261 |
1.48e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 32 PDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGreiLNLPERELNRLRAeQISMIF 110
Cdd:TIGR00957 1296 EDLDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEI----IIDG---LNIAKIGLHDLRF-KITIIP 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 111 QDPM-------TSLNPYMRVGEQ----LMEVLMLHKSMSKAEAfeesvrMLDAvKMPEARKRMrmyphefSGGMRQRVMI 179
Cdd:TIGR00957 1367 QDPVlfsgslrMNLDPFSQYSDEevwwALELAHLKTFVSALPD------KLDH-ECAEGGENL-------SVGQRQLVCL 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 180 AMALLCRPKLLIADEPTTALDVT----VQAQIMTllnelkrEFNTAIIM-ITHDLGVVAGICdKVLVMYAGRTMEYG--- 251
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLEtdnlIQSTIRT-------QFEDCTVLtIAHRLNTIMDYT-RVIVLDKGEVAEFGaps 1504
|
250
....*....|...
gi 495069250 252 ---KAREVFYDPA 261
Cdd:TIGR00957 1505 nllQQRGIFYSMA 1517
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-251 |
1.62e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.20 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 28 TFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGreiLNLPERELNRLRAE-- 104
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSeGDIRFHD---IPLTKLQLDSWRSRla 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 ---QISMIFQDPMTSlNpymrvgeqlmevLMLHKSMSKAEAFEESVRML----DAVKMP-----EARKRMRMypheFSGG 172
Cdd:PRK10789 393 vvsQTPFLFSDTVAN-N------------IALGRPDATQQEIEHVARLAsvhdDILRLPqgydtEVGERGVM----LSGG 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 251
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-251 |
1.78e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFAtpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGR-----IGGSATFNGREILNL 93
Cdd:PRK09580 1 MLSIKDLHVSVE----DKAILRGLNLEVRPGEVHAIMGPNGSGKS----TLSATLA--GRedyevTGGTVEFKGKDLLEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 94 PERElnrlRA-EQISMIFQDPM------------TSLNPYMRVGEQlmEVLmlhKSMSKAEAFEESVRMLdavKMPEARk 160
Cdd:PRK09580 71 SPED----RAgEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPL---DRFDFQDLMEEKIALL---KMPEDL- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 161 RMRMYPHEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGI-CDK 238
Cdd:PRK09580 138 LTRSVNVGFSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIkPDY 215
|
250
....*....|...
gi 495069250 239 VLVMYAGRTMEYG 251
Cdd:PRK09580 216 VHVLYQGRIVKSG 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-246 |
2.95e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.73 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRVTFAtPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIlnlpERELNRL 101
Cdd:TIGR01257 931 VKNLVKIFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS---GTVLVGGKDI----ETNLDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 102 RaEQISMIFQDPMtsLNPYMRVGEQLMEVLMLhKSMSKAEAFEESVRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAM 181
Cdd:TIGR01257 1002 R-QSLGMCPQHNI--LFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEE---AQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 182 ALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-256 |
5.54e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 10 QQTAASQATLLDVKDlrVTFATPDGdvTAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGR----IGGSATF 85
Cdd:PRK10575 2 QEYTNHSDTTFALRN--VSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKST-------LLKMLGRhqppSEGEILL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 86 NGREIlnlpERELNRLRAEQISMIFQ-----DPMTsLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAvkMPEARK 160
Cdd:PRK10575 71 DAQPL----ESWSSKAFARKVAYLPQqlpaaEGMT-VRELVAIGRYPWHGALGRFGAADREKVEEAISLVGL--KPLAHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 161 RMrmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 240
Cdd:PRK10575 144 LV----DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLV 219
|
250
....*....|....*.
gi 495069250 241 VMYAGRTMEYGKAREV 256
Cdd:PRK10575 220 ALRGGEMIAQGTPAEL 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-246 |
5.94e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 36 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSA-TF-NGREILNlperelnrlraEQISMIF 110
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAgsiLIDGQEmRFaSTTAALA-----------AGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 111 QDpmTSLNPYMRVGEQLMevL--------MLHKSMSKAEAFEESVRMLDAVKmPEARKRmrmyphEFSGGMRQRVMIAMA 182
Cdd:PRK11288 86 QE--LHLVPEMTVAENLY--LgqlphkggIVNRRLLNYEAREQLEHLGVDID-PDTPLK------YLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 183 LLcRPKLLIA-DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11288 155 LA-RNARVIAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-227 |
8.58e-12 |
|
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: 65.93 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngriggsaTFNGReiLNLPERelnrlraeqi 106
Cdd:TIGR00954 457 IPLVTPNGDVL-IESLSFEVPSGNNLLICGPNGCGKS-SLFRILGELWP--------VYGGR--LTKPAK---------- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 107 SMIFQDPMtslNPYMRVG---EQL---MEVL-MLHKSMSKAEAfeesVRMLDAVKMPEARKR------MRMYPHEFSGGM 173
Cdd:TIGR00954 515 GKLFYVPQ---RPYMTLGtlrDQIiypDSSEdMKRRGLSDKDL----EQILDNVQLTHILEReggwsaVQDWMDVLSGGE 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495069250 174 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITH 227
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-245 |
1.12e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 36 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRI---GGSATFNGreilnlPerelnrlRAEQ---ISM 108
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDaGSIlylGKEVTFNG------P-------KSSQeagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 109 IFQDpmtsLN--PYMRVGEQLM---EV-----LMLHKSMskaeaFEESVRMLDAVKMPEARKRMRmypHEFSGGMRQRVM 178
Cdd:PRK10762 84 IHQE----LNliPQLTIAENIFlgrEFvnrfgRIDWKKM-----YAEADKLLARLNLRFSSDKLV---GELSIGEQQMVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 179 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-232 |
1.58e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFATPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREilNLPERELN 99
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDPTE--GDIIINDSH--NLKDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAeQISMIFQDPMT--------------SLNPYMRVGEQLMEVLMLHKSMSK---------AEAFEESVRMLDAVKMP 156
Cdd:PTZ00265 457 WWRS-KIGVVSQDPLLfsnsiknnikyslySLKDLEALSNYYNEDGNDSQENKNkrnscrakcAGDLNDMSNTTDSNELI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 157 EARKRM-------------RMYPHEF-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ 204
Cdd:PTZ00265 536 EMRKNYqtikdsevvdvskKVLIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260
....*....|....*....|....*...
gi 495069250 205 AQIMTLLNELKREFNTAIIMITHDLGVV 232
Cdd:PTZ00265 616 YLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-256 |
2.01e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.91 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLrvTFATPDGDV-TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSATFNGreilnlpere 97
Cdd:PRK13545 24 LKDL--FFRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKgtvDIKGSAALIA---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 98 lnrlraeqISMIFQDPMTslnpymrvGEQLMEVLMLHKSMSKAEAFEESVRMLDavkMPEARKRMRMYPHEFSGGMRQRV 177
Cdd:PRK13545 92 --------ISSGLNGQLT--------GIENIELKGLMMGLTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:PRK13545 153 GFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-246 |
3.23e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 43 NFSLRAGETLGIVGESGSGKSQtafaLMGLL-AANGRIGGSATFNGRE-------------ILNLPErelNRlRAEQISm 108
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSE----LMKLLyGATRRTAGQVYLDGKPidirsprdairagIMLCPE---DR-KAEGII- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 109 ifqdPMTS----LNPYMRvGEQLMEVLMLHKSMSKAEAfEESVRMLdAVKMPEARKRMRmyphEFSGGMRQRVMIAMALL 184
Cdd:PRK11288 344 ----PVHSvadnINISAR-RHHLRAGCLINNRWEAENA-DRFIRSL-NIKTPSREQLIM----NLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495069250 185 CRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-242 |
8.14e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 37 TAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriggsatfngREILNLPERELNRLRAEQISmifqdpmts 116
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLLA-------------GALKGTPVAGCVDVPDNQFG--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 lnpymrvgeqlmEVLMLHKSMSKAEAFEESVRMLDAVKMPEA---RKRmrmyPHEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:COG2401 98 ------------REASLIDAIGRKGDFKDAVELLNAVGLSDAvlwLRR----FKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495069250 194 EPTTALDVTVqAQIMTL-LNELKREFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:COG2401 162 EFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-241 |
9.01e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFATPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALM----------------------------- 70
Cdd:PTZ00265 1166 IEIMDVNFRYISRP-NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 71 ------GLLAAN-------GRIGGSATF--NGREIL----NLPERELNRLRaEQISMIFQDPM---TSLNPYMRVGEQ-- 126
Cdd:PTZ00265 1245 deeqnvGMKNVNefsltkeGGSGEDSTVfkNSGKILldgvDICDYNLKDLR-NLFSIVSQEPMlfnMSIYENIKFGKEda 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 127 -LMEVlmlhKSMSKAEAFEESVRML----DAVKMPearkrmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 201
Cdd:PTZ00265 1324 tREDV----KRACKFAAIDEFIESLpnkyDTNVGP--------YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 495069250 202 TVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLV 241
Cdd:PTZ00265 1392 NSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-257 |
1.18e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.43 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 8 APQQTAASQATLL-----DVKDlrVTFATPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGS 82
Cdd:PRK10790 324 GPRQQYGNDDRPLqsgriDIDN--VSFAYRDDNLV-LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT---EGE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 83 ATFNGREILNLPERELNRlraeQISMIFQDPMTslnpymrVGEQLMEVLMLHKSMSKAEAFE--ESVRMLDAVK-MPEA- 158
Cdd:PRK10790 398 IRLDGRPLSSLSHSVLRQ----GVAMVQQDPVV-------LADTFLANVTLGRDISEEQVWQalETVQLAELARsLPDGl 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 159 RKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDK 238
Cdd:PRK10790 467 YTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADT 543
|
250
....*....|....*....
gi 495069250 239 VLVMYAGRTMEYGKAREVF 257
Cdd:PRK10790 544 ILVLHRGQAVEQGTHQQLL 562
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-246 |
1.40e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.79 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 27 VTFATPDGDVTA---VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGRE--------ILNLPE 95
Cdd:cd03250 6 ASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPGSIayvsqepwIQNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 96 RElnrlraeqiSMIFQDPMtslNPymrvgEQLMEVLmlhksmsKAEAFEESVRMLDAVKMPEArkrmrmypHE----FSG 171
Cdd:cd03250 83 RE---------NILFGKPF---DE-----ERYEKVI-------KACALEPDLEILPDGDLTEI--------GEkginLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT--LLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGR 246
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-251 |
3.02e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 47 RAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGGSAT-------FNGREILNLpereLNRLRAEQISMIFQDPMTSLN 118
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNlGKFDDPPDwdeildeFRGSELQNY----FTKLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 119 PYMRVGEqlmeVLMLHKSMSKAEAFEESVRMLdavkmpEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 198
Cdd:cd03236 100 PKAVKGK----VGELLKKKDERGKLDELVDQL------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495069250 199 LDVTVQAQIMTLLNELKREFNtAIIMITHDLGVVAGICDKVLVMYaGRTMEYG 251
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY-GEPGAYG 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
34-256 |
4.34e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAlmgllaanGRIGGSATfnGREILNLPERELNRlRAEQISMIFQDP 113
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP--------AHV*GPDA--GRRPWRF*TWCANR-RALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 MTSLNPYMRVGEQLMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMyphEFSGGMRQRVMIAMALLCRPKLLIAD 193
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495069250 194 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
42-232 |
1.40e-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: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 42 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpeRELNRLRAEQISMIFQDPmtSLNPYM 121
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP---DSGEVRWNGTPL-----AEQRDEPHENILYLGHLP--GLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 122 RVGEQLMEVLMLHKSMSKA--EAFEEsVRMLDAVKMPearkrmrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTieDALAA-VGLTGFEDLP---------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 495069250 200 DVTVQAQIMTLLNE-LKRefNTAIIMITH-DLGVV 232
Cdd:TIGR01189 159 DKAGVALLAGLLRAhLAR--GGIVLLTTHqDLGLV 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
49-250 |
1.51e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 49 GETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELNRLRAEQISMIFQDPmtslnpymRVGEQLM 128
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADG---GSYTFPGNWQLAWVNQETPALPQPALEYVIDGD--------REYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 129 EVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPH--------------EFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PRK10636 96 AQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHglgfsneqlerpvsDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 195 PTTALDvtVQAQIMtlLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 250
Cdd:PRK10636 176 PTNHLD--LDAVIW--LEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-245 |
6.14e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.72 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIL-NLPERELNRLRAEQISMIfqDPMTS 116
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS---GDATVAGKSILtNISDVHQNMGYCPQFDAI--DDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 117 LNPYMRVGEQLMEVlmlhksmsKAEAFEESVRM-LDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEP 195
Cdd:TIGR01257 2029 GREHLYLYARLRGV--------PAEEIEKVANWsIQSLGLSLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495069250 196 TTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 245
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-232 |
1.16e-08 |
|
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: 54.42 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 42 LNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsatfngreilNLPERELNRLRAE-QISMIFQDPMTSLNP 119
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRV------------LLNGGPLDFQRDSiARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 120 YMRVGEQLMevlMLHKSMSKAEAFEESVRM-LDAVKMPEArkrmrmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 198
Cdd:cd03231 87 TLSVLENLR---FWHADHSDEQVEEALARVgLNGFEDRPV--------AQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|....*
gi 495069250 199 LDVTVQAQIMTLLNElKREFNTAIIMITH-DLGVV 232
Cdd:cd03231 156 LDKAGVARFAEAMAG-HCARGGMVVLTTHqDLGLS 189
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
34-246 |
1.29e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREILNLPERELNRlraEQISMIFQD 112
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATsGRIVFDGKDITDWQTAKIMR---EAVAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pmtslnpyMRVGEQLM--EVLMLHKSMSKAEAFEESVRMLDAVkMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLL 190
Cdd:PRK11614 89 --------RRVFSRMTveENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 191 IADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGH 214
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-250 |
1.49e-08 |
|
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: 54.86 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFAtpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsaTFNGREILNLPERELN 99
Cdd:cd03289 3 MTVKDLTAKYT--EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDI----QIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRA--EQISMIFQDPM-TSLNPYMRVGEQlmEVLMLHKSMSKAEAFEESVRMLDAVKMPEArkrmrmypHEFSGGMRQR 176
Cdd:cd03289 77 KAFGviPQKVFIFSGTFrKNLDPYGKWSDE--EIWKVAEEVGLKSVIEQFPGQLDFVLVDGG--------CVLSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 177 VMIAMALLCRPKLLIADEPTTALD-VTVQaqimTLLNELKREFNT-AIIMITHDLGVVAGiCDKVLVMYAGRTMEY 250
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDpITYQ----VIRKTLKQAFADcTVILSEHRIEAMLE-CQRFLVIEENKVRQY 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
38-256 |
3.09e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.05 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 38 AVNDLNFSLRAGETLGIVGESGSGKSQTAfalmgllaanGRIGGSatfngreilnLPERELNRLRAEQISMIFQDpmTSL 117
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLS----------NIIGGS----------LSPTVGKVDRNGEVSVIAIS--AGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 118 NPYMrVGEQLMEVLMLHKSMSKAEAFEesvRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 197
Cdd:PRK13546 97 SGQL-TGIENIEFKMLCMGFKRKEIKA---MTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 198 ALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKAREV 256
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-228 |
3.10e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriggsatfngREILnLPERELNRLRAEQISMIFQDP 113
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILN-------------GEVL-LDDGRIIYEQDLIVARLQQDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 114 MTSL--NPYMRVGEQLMEV---LMLHKSMSKAEAFEESVRMLDAV-----------------KMPEARKRMRMYPH---- 167
Cdd:PRK11147 76 PRNVegTVYDFVAEGIEEQaeyLKRYHDISHLVETDPSEKNLNELaklqeqldhhnlwqlenRINEVLAQLGLDPDaals 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495069250 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKrEFNTAIIMITHD 228
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLK-TFQGSIIFISHD 212
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
42-266 |
4.40e-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: 53.37 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 42 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRIggsaTFNGREILNLPereLNRLRAeQISMIFQDPMT----- 115
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKI----VIDGIDISKLP---LHTLRS-RLSIILQDPILfsgsi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 116 --SLNPYMRVGE----QLMEVLMLhKSMSKAEAfeesvRMLDAVKMPEARKrmrmypheFSGGMRQRVMIAMALLCRPKL 189
Cdd:cd03288 112 rfNLDPECKCTDdrlwEALEIAQL-KNMVKSLP-----GGLDAVVTEGGEN--------FSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 190 LIADEPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGKAREVFYDPAHPYS 265
Cdd:cd03288 178 LIMDEATASIDMAteniLQKVVMTAFAD------RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
.
gi 495069250 266 I 266
Cdd:cd03288 251 S 251
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
49-231 |
5.68e-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: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 49 GETLGIVGESGSGKSQTAFALMGLLAANGriGGSATFNGREILNLPERELNRlraeqismifqdpmtslnpymrvgeqlm 128
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG--GGVIYIDGEDILEEVLDQLLL---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 129 evlmlhksmskaeafeesvrmldavkmpearKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM 208
Cdd:smart00382 52 -------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180
....*....|....*....|....*...
gi 495069250 209 -----TLLNELKREFNTAIIMITHDLGV 231
Cdd:smart00382 101 lleelRLLLLLKSEKNLTVILTTNDEKD 128
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
170-256 |
7.55e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFN-TAIIMI------THDLgvvagiCDKVLVM 242
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIyqcsqdAYEL------FDKVIVL 284
|
90
....*....|....
gi 495069250 243 YAGRTMEYGKAREV 256
Cdd:TIGR00956 285 YEGYQIYFGPADKA 298
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-214 |
7.99e-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: 51.86 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 23 KDLRVTFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAN---GRIGGSATFNGREIlnlpERELN 99
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKT----TLLDVLAGRktaGVITGEILINGRPL----DKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLR--AEQismifqdpMTSLNPYMRVGEQLMevlmlhksmskaeaFEESVRMLDavkmPEARKrmrmyphefsggmrqRV 177
Cdd:cd03232 79 RSTgyVEQ--------QDVHSPNLTVREALR--------------FSALLRGLS----VEQRK---------------RL 117
|
170 180 190
....*....|....*....|....*....|....*..
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNEL 214
Cdd:cd03232 118 TIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
41-234 |
8.35e-08 |
|
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: 53.40 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 41 DLNFSLRAGETLGIVGESGSGKSqTAFALM-GL---------LAANGRIGGSA-------TFNGREILNLPERELNRL-- 101
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKS-TLLRIMaGVdkdfngearPQPGIKVGYLPqepqldpTKTVRENVEEGVAEIKDAld 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 102 RAEQISMIFQDP---MTSLNPYMRVGEQLMEVLMLHKSMSKAEafeesvRMLDAVKMPEARKRMRmyphEFSGGMRQRVM 178
Cdd:TIGR03719 102 RFNEISAKYAEPdadFDKLAAEQAELQEIIDAADAWDLDSQLE------IAMDALRCPPWDADVT----KLSGGERRRVA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 179 IAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 234
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHDryfLDNVAG 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-227 |
8.81e-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: 53.76 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFaTPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsaTFNGreiLNLPERELN 99
Cdd:TIGR01271 1218 MDVQGLTAKY-TEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEI----QIDG---VSWNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRAE-----QISMIFQDPM-TSLNPYMRVGEQlmEVLMLHKSMSKAEAFEESVRMLDAVKMPEArkrmrmypHEFSGGM 173
Cdd:TIGR01271 1289 TWRKAfgvipQKVFIFSGTFrKNLDPYEQWSDE--EIWKVAEEVGLKSVIEQFPDKLDFVLVDGG--------YVLSNGH 1358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 174 RQRVMIAMALLCRPKLLIADEPTTALD-VTVQaqimTLLNELKREF-NTAIIMITH 227
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDpVTLQ----IIRKTLKQSFsNCTVILSEH 1410
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-228 |
2.55e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 34 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRIGGSatfNGREILNLPERELNRLRAEQismifqd 112
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPvSGEIGLA---KGIKLGYFAQHQLEFLRADE------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 113 pmTSLNPYMRVGEQLMEVLMlhKSMSKAEAFEEsvrmlDAVKMPEARkrmrmypheFSGGMRQRVMIAMALLCRPKLLIA 192
Cdd:PRK10636 393 --SPLQHLARLAPQELEQKL--RDYLGGFGFQG-----DKVTEETRR---------FSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190
....*....|....*....|....*....|....*..
gi 495069250 193 DEPTTALDVTV-QAqimtlLNELKREFNTAIIMITHD 228
Cdd:PRK10636 455 DEPTNHLDLDMrQA-----LTEALIDFEGALVVVSHD 486
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-217 |
3.65e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 43 NFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPERELNRLraeqISMIFQDPMTSLnpyMR 122
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPL---LSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNTDM---LS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 123 VGEqlmevlmlhksmskaEAFEESVR--MLDAVKMPEarkRMRMYPHEF-------------SGGMRQRVMIAMALLCRP 187
Cdd:PRK10938 93 PGE---------------DDTGRTTAeiIQDEVKDPA---RCEQLAQQFgitalldrrfkylSTGETRKTLLCQALMSEP 154
|
170 180 190
....*....|....*....|....*....|
gi 495069250 188 KLLIADEPTTALDVTVQAQIMTLLNELKRE 217
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-254 |
3.76e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 9 PQQTAASQATLLDVKDLRVTFAtpdgdvtavndlNFSL-------RAGETLGIVGESGSGKSQTAFALMGLL-AANGRIG 80
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLG------------DFSLeveggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLkPDEGEVD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 81 GSATfngreILNLPERelnrLRAEQismifqdpmtslnpYMRVGEQLMEVL-MLHKSMSKAEAFE--ESVRMLDavkmpe 157
Cdd:PRK13409 398 PELK-----ISYKPQY----IKPDY--------------DGTVEDLLRSITdDLGSSYYKSEIIKplQLERLLD------ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 158 arKRMRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICD 237
Cdd:PRK13409 449 --KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISD 522
|
250
....*....|....*..
gi 495069250 238 KVLVmYAGRTMEYGKAR 254
Cdd:PRK13409 523 RLMV-FEGEPGKHGHAS 538
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-255 |
4.59e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 10 QQTAASQATLLDVKDLRVTFATpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGRE 89
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS---GTLEIGGNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 90 ILNLperelNRLRAEQ--ISMIFQDPMtsLNPYMRVGEQLMevLMLHKSMSKAEAFEESVRMLDAvkmpearkrmRMYPH 167
Cdd:PRK15439 75 CARL-----TPAKAHQlgIYLVPQEPL--LFPNLSVKENIL--FGLPKRQASMQKMKQLLAALGC----------QLDLD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 168 EFSGGM----RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMY 243
Cdd:PRK15439 136 SSAGSLevadRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMR 214
|
250
....*....|..
gi 495069250 244 AGRTMEYGKARE 255
Cdd:PRK15439 215 DGTIALSGKTAD 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-231 |
6.05e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.49 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTfatpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlperELN 99
Cdd:PRK13539 3 LEGEDLACV----RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP---AAGTIKLDGGDI------DDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 RLRaEQISMI-FQDPMtslNPYMRVGEQLmevlmlhksmskaeAFEESVRMLDAVKMPEARKRMRMYP------HEFSGG 172
Cdd:PRK13539 70 DVA-EACHYLgHRNAM---KPALTVAENL--------------EFWAAFLGGEELDIAAALEAVGLAPlahlpfGYLSAG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 173 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITH-DLGV 231
Cdd:PRK13539 132 QKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-257 |
7.69e-07 |
|
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: 51.10 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 28 TFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafaLMGLLAANGRIGGSATFNGrEILNLPERELNRLRAEQIS 107
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 108 MIFQDPMTSlNPYMRVGEQ--LMEVLMLHKSMSKAEAFEESVRMldavkmpearkrmrmyphefSGGMRQRVMIAMALLC 185
Cdd:TIGR00957 719 ILFGKALNE-KYYQQVLEAcaLLPDLEILPSGDRTEIGEKGVNL--------------------SGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495069250 186 RPKLLIADEPTTALDVTVQAQI-------MTLLNELKRefntaiIMITHDLGVVAGIcDKVLVMYAGRTMEYGKAREVF 257
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIfehvigpEGVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-243 |
8.00e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 46 LRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGGSAT-------FNGREILNLpereLNRLRAEQISmifqdpmTSL 117
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNlGDYDEEPSwdevlkrFRGTELQDY----FKKLANGEIK-------VAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 118 NPymrvgeQLMEVLmlhksmskAEAFEESVR-MLDAV----KMPEARKRMRMYP------HEFSGGMRQRVMIAMALLCR 186
Cdd:COG1245 165 KP------QYVDLI--------PKVFKGTVReLLEKVdergKLDELAEKLGLENildrdiSELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 187 PKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMY 243
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
168-255 |
1.03e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 168 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVmYAGRT 247
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV-FEGEP 533
|
....*...
gi 495069250 248 MEYGKARE 255
Cdd:COG1245 534 GVHGHASG 541
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-243 |
1.12e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 46 LRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGGSAT-------FNGREILNLPEReL--NRLRA-------EQISM 108
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlGDYEEEPSwdevlkrFRGTELQNYFKK-LynGEIKVvhkpqyvDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 109 IFQDpmtslnpymRVGEQLMEVlmlhksmSKAEAFEESVRMLDAVKMPEarKRMRmyphEFSGGMRQRVMIAMALLCRPK 188
Cdd:PRK13409 175 VFKG---------KVRELLKKV-------DERGKLDEVVERLGLENILD--RDIS----ELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 189 LLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMY 243
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-112 |
1.14e-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: 50.18 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 6 LSAPQQTAASQATLLDVKDLRVTFATPDGDVT-AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSAT 84
Cdd:COG4615 314 ADAAAPPAPADFQTLELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE---SGEIL 390
|
90 100
....*....|....*....|....*...
gi 495069250 85 FNGREIlnlPERELNRLRaEQISMIFQD 112
Cdd:COG4615 391 LDGQPV---TADNREAYR-QLFSAVFSD 414
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
29-229 |
1.17e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 48.87 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 29 FATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG-LLAANGRIGGSATfNGREILNLPERELNRLR---AE 104
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNK-NESEPSFEATRSRNRYSvayAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 105 Q----ISMIFQDPMTSLNPYMRvgeqlmevlMLHKSMSKAEAFEESVRMLDAVKMPEARKRmrmyPHEFSGGMRQRVMIA 180
Cdd:cd03290 86 QkpwlLNATVEENITFGSPFNK---------QRYKAVTDACSLQPDIDLLPFGDQTEIGER----GINLSGGQRQRICVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495069250 181 MALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 229
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
36-246 |
2.96e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 36 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPERELnrlRAEQISMIFQDpmt 115
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS---GSILFQGKEIDFKSSKEA---LENGISMVHQE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 116 sLNPYMRVgeQLMEVLMLHKSMSKAeAFEESVRMLDAVKMPEARKRMRMYPHE----FSGGMRQRVMIAMALLCRPKLLI 191
Cdd:PRK10982 82 -LNLVLQR--SVMDNMWLGRYPTKG-MFVDQDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 192 ADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGR 246
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLK-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 |
3.22e-06 |
|
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: 47.79 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 45 SLRAGETLGIVGESGSGKSQTAFALMGLLAANGriggsatfnGREILNLPERELnrlRAEQISMIFQdpmtslnpyMRVG 124
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDE---------GDIEIELDTVSY---KPQYIKADYE---------GTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 125 EQLMEVLmlhKSMSKAEAFEESVrmLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ 204
Cdd:cd03237 80 DLLSSIT---KDFYTHPYFKTEI--AKPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495069250 205 AQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVmYAGRTMEYGKA 253
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEGEPSVNGVA 199
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
32-231 |
3.48e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 32 PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAlmgllaangriGGSATFNGREILNLPerelnrlRAEQISMIFQ 111
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-----------GLYASGKARLISFLP-------KFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 112 DPMTSLnpyMRVGeqlMEVLMLHKSMSKaeafeesvrmldavkmpearkrmrmypheFSGGMRQRVMIAMALLCRPK--L 189
Cdd:cd03238 66 DQLQFL---IDVG---LGYLTLGQKLST-----------------------------LSGGELQRVKLASELFSEPPgtL 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495069250 190 LIADEPTTALDvtvQAQIMTLLNELKR---EFNTaIIMITHDLGV 231
Cdd:cd03238 111 FILDEPSTGLH---QQDINQLLEVIKGlidLGNT-VILIEHNLDV 151
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
54-228 |
5.28e-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: 46.45 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 54 IVGESGSGKSQT----AFALMGLLAANGRIGgsatFNGREILNLPERelnrlRAeQISMIFQDPMTSLNPYMRVGEQLME 129
Cdd:cd03240 27 IVGQNGAGKTTIiealKYALTGELPPNSKGG----AHDPKLIREGEV-----RA-QVKLAFENANGKKYTITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 130 VLMLHKsmskaeafEESVRMLdavkmPEARKRMrmyphefSGGMRQ------RVMIAMALLCRPKLLIADEPTTALDV-T 202
Cdd:cd03240 97 VIFCHQ--------GESNWPL-----LDMRGRC-------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeN 156
|
170 180
....*....|....*....|....*.
gi 495069250 203 VQAQIMTLLNELKREFNTAIIMITHD 228
Cdd:cd03240 157 IEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
41-234 |
1.26e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 41 DLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREIlnlperelNRLRAEqismiFQDPM----- 114
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKT----SLLRILAGLARpDAGEVLWQGEPI--------RRQRDE-----YHQDLlylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 115 -----TSLNPYmrvgEQLMEVLMLHKSMSKAEAFEesvrMLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKL 189
Cdd:PRK13538 82 qpgikTELTAL----ENLRFYQRLHGPGDDEALWE----ALAQVGL---AGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495069250 190 LIADEPTTALDVTVQAQIMTLLNE-LKRefNTAIIMITH-DLGVVAG 234
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQ--GGMVILTTHqDLPVASD 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
147-253 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 147 VRMLDAVKMPEA------RKRMRMYPH--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREF 218
Cdd:cd03222 42 VKILAGQLIPNGdndewdGITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
90 100 110
....*....|....*....|....*....|....*
gi 495069250 219 NTAIIMITHDLGVVAGICDKVLVMYaGRTMEYGKA 253
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGIA 155
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-228 |
1.90e-05 |
|
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: 46.08 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 20 LDVKDLRVTFatpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMgllaangriggsatfNGREILNLPERELn 99
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKS-TLFRMI---------------TGQEQPDSGTIEI- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 100 rlrAEQISMIFQDPM-TSLNPYMRVGEQL---MEVLMLHKSMSKAEAFEESVRMldavKMPEARKRMRmyphEFSGGMRQ 175
Cdd:TIGR03719 382 ---GETVKLAYVDQSrDALDPNKTVWEEIsggLDIIKLGKREIPSRAYVGRFNF----KGSDQQKKVG----QLSGGERN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495069250 176 RVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 228
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD 499
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
170-233 |
2.39e-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: 2.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 170 SGGMRQRVMIAMAL-LCRPK---LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVA 233
Cdd:cd03227 79 SGGEKELSALALILaLASLKprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAE 145
|
|
| 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 495069250 170 SGGMRQRVMIAMALLCR---PKLLIADEPTTAL---DVtvqAQIMTLLNELKREFNTaIIMITHDLGVV 232
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGNT-VVVIEHNLDVI 895
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-201 |
2.65e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 22 VKDLRV-TFATPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANG------------RIGGSATFNGR 88
Cdd:PLN03073 175 IKDIHMeNFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKT-TFLRYMAMHAIDGipkncqilhveqEVVGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 89 EILNlPERELNRLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKSMSKAeaFEESVRMLDAVKMPEARKR------- 161
Cdd:PLN03073 254 CVLN-TDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQR--LEEIYKRLELIDAYTAEARaasilag 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495069250 162 -------MRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 201
Cdd:PLN03073 331 lsftpemQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-251 |
3.41e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 32 PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngRIGGSATFNGReILNLPerelnrlraeQISMIF- 110
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP--RSDASVVIRGT-VAYVP----------QVSWIFn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 111 ---QDPMTSLNPYMRVG-EQLMEVLMLHKSMSkaeafeesvrMLDAVKMPEARKRMRmyphEFSGGMRQRVMIAMALLCR 186
Cdd:PLN03130 693 atvRDNILFGSPFDPERyERAIDVTALQHDLD----------LLPGGDLTEIGERGV----NISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 187 PKLLIADEPTTALDVTVQAQIMTllNELKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYG 251
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-227 |
3.66e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 19 LLDVKDLRVTFAtpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNlperel 98
Cdd:PRK13540 1 MLDVIELDFDYH----DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK---GEILFERQSIKK------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 99 nRLRAEQISMIFQDPMTSLNPYMRVGEQLMevLMLHKSmSKAEAFEESVRMLDAVKMPEarkrmrmYP-HEFSGGMRQRV 177
Cdd:PRK13540 68 -DLCTYQKQLCFVGHRSGINPYLTLRENCL--YDIHFS-PGAVGITELCRLFSLEHLID-------YPcGLLSSGQKRQV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495069250 178 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITH 227
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
164-246 |
3.83e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 164 MYphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLnelkrEFNTAIIMITHDLGVVAGICDKVLVM 242
Cdd:PLN03073 625 MY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVV 697
|
....
gi 495069250 243 YAGR 246
Cdd:PLN03073 698 SEGK 701
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
170-234 |
6.84e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 6.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495069250 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 234
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHDryfLDNVAG 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
170-228 |
1.52e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 170 SGGMRQRVMIAmALLCRP-KLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 228
Cdd:PRK11147 442 SGGERNRLLLA-RLFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-257 |
5.83e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.89 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 39 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA----ANGRIGGSATFngreilnlperelnrlrAEQISMIFQdpm 114
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaetSSVVIRGSVAY-----------------VPQVSWIFN--- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 115 TSLNPYMRVGEQLmEVLMLHKSMSkAEAFEESVRMLDAVKMPEARKRMRmyphEFSGGMRQRVMIAMALLCRPKLLIADE 194
Cdd:PLN03232 693 ATVRENILFGSDF-ESERYWRAID-VTALQHDLDLLPGRDLTEIGERGV----NISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495069250 195 PTTALDVTVQAQIMT--LLNELKREFNTAIIMITHDLGVVagicDKVLVMYAGRTMEYGKAREVF 257
Cdd:PLN03232 767 PLSALDAHVAHQVFDscMKDELKGKTRVLVTNQLHFLPLM----DRIILVSEGMIKEEGTFAELS 827
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
170-217 |
7.09e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 7.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 495069250 170 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRE 217
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
47-214 |
8.06e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 47 RAGETLGIVGESGSGKSqtafALMGLLAanGRIGGSATFNGREILNLPERELNRLRAeqISMIFQDPMTSLNPYMRVGEQ 126
Cdd:TIGR00956 787 KPGTLTALMGASGAGKT----TLLNVLA--ERVTTGVITGGDRLVNGRPLDSSFQRS--IGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 127 LMEVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYPHE-FSGGMRQRVMIAMALLCRPKLLI-ADEPTTALDVTVQ 204
Cdd:TIGR00956 859 FSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170
....*....|
gi 495069250 205 AQIMTLLNEL 214
Cdd:TIGR00956 939 WSICKLMRKL 948
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
170-240 |
8.31e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 8.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495069250 170 SGGMRQRVMIAMALLC---RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAgICDKVL 240
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI-IEHNMHVVK-VADYVL 882
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
167-229 |
1.27e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.03 E-value: 1.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495069250 167 HEFSGGMRQRVMIAMAL---LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 229
Cdd:COG1106 201 SEESDGTKRLLALAGALldaLAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHST 266
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
172-228 |
3.54e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 3.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 495069250 172 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELkREFNTAIIMITHD 228
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVL-NERNSTMIIISHD 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
45-208 |
4.39e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 45 SLRAGETLGIVGESGSGKSqtafALMGLLAanGRIGGSATFNGREILNLPERELNRLRaeqIS-MIFQDPMTSlnPYMRV 123
Cdd:PLN03140 902 AFRPGVLTALMGVSGAGKT----TLMDVLA--GRKTGGYIEGDIRISGFPKKQETFAR---ISgYCEQNDIHS--PQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495069250 124 GEQLM--EVLMLHKSMSKAEAFEESVRMLDAVKMPEARKRMRMYP--HEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 199
Cdd:PLN03140 971 RESLIysAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
....*....
gi 495069250 200 DVTVQAQIM 208
Cdd:PLN03140 1051 DARAAAIVM 1059
|
|
| |
