|
Name |
Accession |
Description |
Interval |
E-value |
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-347 |
0e+00 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 770.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 19 NAQLEQNQNVLLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKFNGR 98
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 99 EILNLPEKQLNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHE 178
Cdd:PRK09473 82 EILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTM 258
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 259 EYGQARDVFYHPSHPYSIGLLNAVPRLDAEGDSLMTIPGNPPNLLRLPKGCPFQPRCQYAMDRCASAPALESFGEGRLRA 338
Cdd:PRK09473 242 EYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFGPGRLRA 321
|
....*....
gi 899869912 339 CYKPVGELV 347
Cdd:PRK09473 322 CFKPVEELL 330
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
29-342 |
0e+00 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 551.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKFNGREILNLPEKQL 108
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVM 188
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFY 268
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 269 HPSHPYSIGLLNAVPRLDAEGDSLMTIPGNPPNLLRLPKGCPFQPRCQYAMDRCASA-PALESFGEGRLRACYKP 342
Cdd:COG0444 241 NPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEePPLREVGPGHRVACHLY 315
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-304 |
1.25e-145 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 421.79 E-value: 1.25e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNG-RIGGSAKFNGREILNLPEKQ 107
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAaHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRV 187
Cdd:COG4172 86 LRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 899869912 268 YHPSHPYSIGLLNAVPRLDAEgdslmTIPGNPPNLLR 304
Cdd:COG4172 246 AAPQHPYTRKLLAAEPRGDPR-----PVPPDAPPLLE 277
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
29-261 |
1.72e-125 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 359.13 E-value: 1.72e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGREILNLPEKQL 108
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK---PTSGSIIFDGKDLLKLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEEsIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVM 188
Cdd:cd03257 78 -KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKE-AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
28-339 |
1.52e-119 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 347.87 E-value: 1.52e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 28 VLLDVKDLTVTF-------STPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGRE 99
Cdd:COG4608 6 PLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePTSGEI----LFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 100 ILNLPEKQLNRLRAEeISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKM-PEARKRmrmYPHE 178
Cdd:COG4608 82 ITGLSGRELRPLRRR-MQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR---YPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTM 258
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 259 EYGQARDVFYHPSHPYSIGLLNAVPRLDAEGDS-LMTIPGNPPNLLRLPKGCPFQPRCQYAMDRCAS-APALESFGEGRL 336
Cdd:COG4608 238 EIAPRDELYARPLHPYTQALLSAVPVPDPERRReRIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATeEPPLREVGPGHQ 317
|
...
gi 899869912 337 RAC 339
Cdd:COG4608 318 VAC 320
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-345 |
3.31e-110 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 324.39 E-value: 3.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSA-KFNGREILNLPEKQ 107
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKlEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRV 187
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 268 YHPSHPYSIGLLNAVPRLDAEGDSLMTIPGNPPNLLRLPKGCPFQPRCQYAMDRC-ASAPALESFGEGRLRaCYKPVGE 345
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCrAEEPALNMLAGRQSK-CHYPLDD 320
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-288 |
2.24e-109 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 328.40 E-value: 2.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 20 AQLEQNQNVLLDVKDLTVTF-STPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNG 97
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSI----LFDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 98 REILNLPEKQLNRLRAEeISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARkrMRMYPH 177
Cdd:COG1123 327 KDLTKLSRRSLRELRRR-VQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDL--ADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRT 257
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
250 260 270
....*....|....*....|....*....|.
gi 899869912 258 MEYGQARDVFYHPSHPYSIGLLNAVPRLDAE 288
Cdd:COG1123 484 VEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
29-305 |
8.47e-109 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 327.25 E-value: 8.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKFNGREILNLPEkql 108
Cdd:COG1123 4 LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nRLRAEEISMIFQDPMTSLNPyMRVGEQLMEVLQLHKkMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 188
Cdd:COG1123 79 -ALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLG-LSRAEARARVLELLEAVGLERRLDR---YPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFY 268
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 899869912 269 HPShpysigLLNAVPRLDAEGDSLMTIPGNPPNLLRL 305
Cdd:COG1123 233 APQ------ALAAVPRLGAARGRAAPAAAAAEPLLEV 263
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-286 |
7.59e-100 |
|
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: 304.69 E-value: 7.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 22 LEQNQNVLLDVKDLTVTFSTPDG-------DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIggsaK 94
Cdd:COG4172 268 VPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEI----R 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 95 FNGREILNLPEKQLNRLRAEeISMIFQDPMTSLNPYMRVGEQLMEVLQLHK-KMSKSEAFEESIRMLDAVKM-PEARKRm 172
Cdd:COG4172 344 FDGQDLDGLSRRALRPLRRR-MQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHR- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 173 rmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:COG4172 422 --YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM 499
|
250 260 270
....*....|....*....|....*....|....
gi 899869912 253 YAGRTMEYGQARDVFYHPSHPYSIGLLNAVPRLD 286
Cdd:COG4172 500 KDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-330 |
3.34e-96 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 288.53 E-value: 3.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 24 QNQNVLLDVKDLTVTFSTPDGD---------VTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsa 93
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDGEV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 94 KFNGREILNLPEKQLNRLRaEEISMIFQDPMTSLNPYMRVGEQLMEVLQL-HKKMSKSEAFEESIRMLDAVKM-PEARKR 171
Cdd:PRK15079 79 AWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLlPNLINR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 172 mrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLV 251
Cdd:PRK15079 158 ---YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 252 MYAGRTMEYGQARDVFYHPSHPYSIGLLNAVPRLDAEGDSLMTI---PGNPPNLLRLPKGCPFQPRCQYAMDRCA-SAPA 327
Cdd:PRK15079 235 MYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIqllEGELPSPINPPSGCVFRTRCPIAGPECAkTRPV 314
|
...
gi 899869912 328 LES 330
Cdd:PRK15079 315 LEG 317
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-304 |
5.94e-94 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 289.30 E-value: 5.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRI--GGSAKFNGREILNLPEK 106
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQR 186
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 899869912 267 FYHPSHPYSIGLLNAVPrldaEGDSLmTIPGNPPNLLR 304
Cdd:PRK15134 245 FSAPTHPYTQKLLNSEP----SGDPV-PLPEPASPLLD 277
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-342 |
2.38e-93 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 281.41 E-value: 2.38e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIggSA---KFNGREILNLPE 105
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHV--TAdrfRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 KQLNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVL---QL------HKKMSKSEAfeesIRMLDAVKMPEARKRMRMYP 176
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpswTFkgkwwqRFKWRKKRA----IELLHRVGIKDHKDIMNSYP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 177 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 257 TMEYGQARDVFYHPSHPYSIGLLNAVP--RLDAEGDS-LMTIPGNPPNLLRLPKGCPFQPRCQYAMDRCASAPALESFgE 333
Cdd:COG4170 237 TVESGPTEQILKSPHHPYTKALLRSMPdfRQPLPHKSrLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRKI-K 315
|
....*....
gi 899869912 334 GRLRACYKP 342
Cdd:COG4170 316 GHEFACHFP 324
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-287 |
3.55e-93 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 290.22 E-value: 3.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 16 LEQNAQLEQNQnvLLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKF 95
Cdd:PRK10261 1 MPHSDELDARD--VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 96 ----NGREILNLPE---KQLNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEA 168
Cdd:PRK10261 79 llrrRSRQVIELSEqsaAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 169 RKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNK 248
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADR 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 899869912 249 VLVMYAGRTMEYGQARDVFYHPSHPYSIGLLNAVPRLDA 287
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLGA 277
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
28-340 |
1.86e-89 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 271.45 E-value: 1.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 28 VLLDVKDLTVTFS------TPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREIL 101
Cdd:PRK11308 4 PLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTG---GELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 102 NlPEKQLNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKM-PEARKRmrmYPHEFS 180
Cdd:PRK11308 81 K-ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YPHMFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 181 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEY 260
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 261 GQARDVFYHPSHPYSIGLLNAVPRLDAEGDSL-MTIPGNPPNLLRLPKGCPFQPRCQYAMDRCAS-APALESFGeGRLRA 338
Cdd:PRK11308 237 GTKEQIFNNPRHPYTQALLSATPRLNPDDRRErIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQeQPQLRDYD-GRLVA 315
|
..
gi 899869912 339 CY 340
Cdd:PRK11308 316 CF 317
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
29-288 |
1.35e-88 |
|
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: 266.28 E-value: 1.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQL 108
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS---GEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRlraeEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMsksEAFEESIRMLDAVKMPEA-RKRmrmYPHEFSGGMRQRV 187
Cdd:COG1124 78 RR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSfLDR---YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250 260
....*....|....*....|.
gi 899869912 268 YHPSHPYSIGLLNAVPRLDAE 288
Cdd:COG1124 228 AGPKHPYTRELLAASLAFERA 248
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
48-281 |
1.46e-78 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 239.96 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 48 AVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRI-GGSAKFNGREILNLpekqlnRLRAEEISMIFQDPMTS 126
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQtSGEILLDGRPLLPL------SIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 127 LNPYMRVGEQLMEVLQLHKKMSKsEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 206
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 207 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGLLNA 281
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
29-343 |
5.33e-76 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 237.01 E-value: 5.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSA-KFNGREILNLPEKQ 107
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRmRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQ--LHK-------KMSKSEAFEesirMLDAVKMPEARKRMRMYPHE 178
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPgwTYKgrwwqrfGWRKRRAIE----LLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTM 258
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 259 EYGQARDVFYHPSHPYSIGLLNAVP---RLDAEGDSLMTIPGNPPNLLRLPKGCPFQPRCQYAMDRCASAPALESFgEGR 335
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPdfgSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTGA-KNH 317
|
....*...
gi 899869912 336 LRACYKPV 343
Cdd:PRK15093 318 LYACHFPL 325
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-279 |
3.28e-68 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 222.66 E-value: 3.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 22 LEQNQNVLLDVKDLTVTFSTPDG-------DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGgsak 94
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPIRKGilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIW---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 95 FNGREILNLPEKQLNRLRaEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKK-MSKSEAFEESIRMLDAVKM-PEARKRm 172
Cdd:PRK15134 344 FDGQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLdPETRHR- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 173 rmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:PRK15134 422 --YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
250 260
....*....|....*....|....*..
gi 899869912 253 YAGRTMEYGQARDVFYHPSHPYSIGLL 279
Cdd:PRK15134 500 RQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
29-281 |
5.15e-65 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 206.61 E-value: 5.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDG-----DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREIln 102
Cdd:COG4167 4 LLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEpTSGEI----LINGHKL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 103 lpEKQLNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKM-PEarkRMRMYPHEFSG 181
Cdd:COG4167 78 --EYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPE---HANFYPHMLSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 182 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYG 232
|
250 260
....*....|....*....|
gi 899869912 262 QARDVFYHPSHPYSIGLLNA 281
Cdd:COG4167 233 KTAEVFANPQHEVTKRLIES 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-286 |
1.20e-64 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 215.49 E-value: 1.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 18 QNAQLEQNQNV----LLDVKDLTVTFSTPDG-------DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASN 86
Cdd:PRK10261 298 QEPPIEQDTVVdgepILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 87 GrigGSAKFNGREILNLPEKQLNRLRaEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKM- 165
Cdd:PRK10261 378 G---GEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLl 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 166 PEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGI 245
Cdd:PRK10261 454 PEHAWR---YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERI 530
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 899869912 246 CNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGLLNAVPRLD 286
Cdd:PRK10261 531 SHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVAD 571
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
29-282 |
1.27e-63 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 202.74 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAsnGRI---GGSAKFNGRE-----I 100
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLY--FDLaptSGSVYYRDRDggprdL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 101 LNLPEKQLNRLRAEEISMIFQDPMTSLNpyMRV------GEQLMEVLQLHKKMSKSEAfeesIRMLDAVKMPEARkrMRM 174
Cdd:COG4107 82 FALSEAERRRLRRTDWGMVYQNPRDGLR--MDVsaggniAERLMAAGERHYGDIRARA----LEWLERVEIPLER--IDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 175 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYA 254
Cdd:COG4107 154 LPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKN 233
|
250 260
....*....|....*....|....*...
gi 899869912 255 GRTMEYGQARDVFYHPSHPYSIGLLNAV 282
Cdd:COG4107 234 GRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
27-256 |
4.56e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 197.57 E-value: 4.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIggsaKFNGREILNLP 104
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPTSGEV----LIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 EKQLNRLRAEEISMIFQDPmtSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEarkRMRMYPHEFSGGMR 184
Cdd:COG1136 77 ERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 899869912 185 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICNKVLVMYAGR 256
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
30-256 |
1.34e-55 |
|
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: 180.76 E-value: 1.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLLASNGRigGSAKFNGREILNLPEKQLN 109
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPTS--GEVRVDGTDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEEISMIFQDPmtSLNPYMRVGEQLMEVLQLHKKmSKSEAFEESIRMLDAVKMPEarkRMRMYPHEFSGGMRQRVMI 189
Cdd:cd03255 78 AFRRRHIGFVFQSF--NLLPDLTALENVELPLLLAGV-PKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 190 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICNKVLVMYAGR 256
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
32-271 |
6.79e-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: 177.00 E-value: 6.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIggsaKFNGREILNLPEKQLN 109
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLerPTSGSV----LVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEeISMIFQ--DPMTSLNpymrVGEQLMEVLQLHKkMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRV 187
Cdd:cd03258 79 KARRR-IGMIFQhfNLLSSRT----VFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKADA---YPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
....
gi 899869912 268 YHPS 271
Cdd:cd03258 230 ANPQ 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
32-305 |
6.11e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 177.58 E-value: 6.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIggsaKFNGREILNLPEKQLN 109
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-TLIRCINLLerPTSGSV----LVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEeISMIFQDP--MTSLNpymrVGEQLMEVLQLHKkMSKSEafeesIR-----MLDAVKMPEARKRmrmYPHEFSGG 182
Cdd:COG1135 79 AARRK-IGMIFQHFnlLSSRT----VAENVALPLEIAG-VPKAE-----IRkrvaeLLELVGLSDKADA---YPSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQ 262
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 899869912 263 ARDVFYHPSHPYSIGLLNAVPRLDAEGDSLMTIPGNPPN--LLRL 305
Cdd:COG1135 225 VLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGGgrLVRL 269
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
29-263 |
2.53e-51 |
|
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: 170.31 E-value: 2.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLA-----SNGRIggsaKFNGREILNL 103
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLLAgldrpTSGTV----RLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 PEKQLNRLRAEEISMIFQDPMtsLNPYMRVGEQLMEVLQLhkkMSKSEAFEESIRMLDAVKMPEarkRMRMYPHEFSGGM 183
Cdd:COG4181 80 DEDARARLRARHVGFVFQSFQ--LLPTLTALENVMLPLEL---AGRRDARARARALLERVGLGH---RLDHYPAQLSGGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 184 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICNKVLVMYAGRTMEYGQA 263
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRLVEDTAA 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
26-274 |
3.94e-51 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 169.77 E-value: 3.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 26 QNVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLP 104
Cdd:COG1127 2 SEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPDSGEI----LVDGQDITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 EKQLNRLRAEeISMIFQDP--MTSLNpymrVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGG 182
Cdd:COG1127 74 EKELYELRRR-IGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKM---PSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALD-VTVqAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
250
....*....|...
gi 899869912 262 qARDVFYHPSHPY 274
Cdd:COG1127 225 -TPEELLASDDPW 236
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
45-281 |
6.06e-51 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 169.88 E-value: 6.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 45 DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrigGSAKFNGREILNLPEKQLNRLRAEEISMIFQDPM 124
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA-----GVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 TSLNPYMRVGEQLMEVLQLHKKMSKSEAFeesIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 204
Cdd:PRK10418 90 SAFNPLHTMHTHARETCLALGKPADDATL---TAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 205 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGLLNA 281
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
30-266 |
1.01e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.70 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGLLASNGrigGSAKFNGREILNLPEKQL 108
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIrMLLGLLRPTS---GEVRVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRlraeeISMIFQDPmtSLNPYMRVGEQLMEVLQLHKkMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 188
Cdd:COG1131 73 RR-----IGYVPQEP--ALYPDLTVRENLRFFARLYG-LPRKEARERIDELLELFGLTDAADR---KVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-282 |
2.48e-49 |
|
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: 165.77 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGR-----EILNL 103
Cdd:TIGR02323 3 LLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDH---GTATYIMRsgaelELYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 PEKQLNRLRAEEISMIFQDPMTSLNpyMRV------GEQLMEVLQLHKKMSKSEAfeesIRMLDAVKMPeaRKRMRMYPH 177
Cdd:TIGR02323 76 SEAERRRLMRTEWGFVHQNPRDGLR--MRVsaganiGERLMAIGARHYGNIRATA----QDWLEEVEID--PTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRT 257
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....*
gi 899869912 258 MEYGQARDVFYHPSHPYSIGLLNAV 282
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
29-275 |
3.90e-48 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 162.79 E-value: 3.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAsnGRI---GGSAKFNGR-----EI 100
Cdd:PRK11701 6 LLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKT----TLLNALS--ARLapdAGEVHYRMRdgqlrDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 101 LNLPEKQLNRLRAEEISMIFQDPMTSLNpyMRV------GEQLMEVLQLHKKMSKSEAfeesIRMLDAVKMPEARkrMRM 174
Cdd:PRK11701 76 YALSEAERRRLLRTEWGFVHQHPRDGLR--MQVsaggniGERLMAVGARHYGDIRATA----GDWLERVEIDAAR--IDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 175 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYA 254
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250 260
....*....|....*....|.
gi 899869912 255 GRTMEYGQARDVFYHPSHPYS 275
Cdd:PRK11701 228 GRVVESGLTDQVLDDPQHPYT 248
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
29-282 |
2.15e-47 |
|
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: 161.13 E-value: 2.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFST-----PDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNL 103
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQ---GTVSFRGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 PEKQLNRLRaEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEarKRMRMYPHEFSGGM 183
Cdd:TIGR02769 79 DRKQRRAFR-RDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 184 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQA 263
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
250
....*....|....*....
gi 899869912 264 RDVFYHpSHPYSIGLLNAV 282
Cdd:TIGR02769 236 AQLLSF-KHPAGRNLQSAV 253
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
30-270 |
5.28e-47 |
|
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: 159.03 E-value: 5.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILnlpEKQL 108
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEV----LVDGKDIT---KKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRaEEISMIFQDP-----MTSlnpymrVGEqlmEV----LQLhkKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEF 179
Cdd:COG1122 71 RELR-RKVGLVFQNPddqlfAPT------VEE---DVafgpENL--GLPREEIRERVEEALELVGLEHLADR---PPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTME 259
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
250
....*....|.
gi 899869912 260 YGQARDVFYHP 270
Cdd:COG1122 215 DGTPREVFSDY 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
30-274 |
2.84e-46 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 157.28 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALM-GLLASNGrigGSAKFNGREILNLPEKQL 108
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKS-TLLRLIvGLLRPDS---GEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRAEeISMIFQDP--MTSLNpymrVGEQLMEVLQLHKKMSKSEaFEESIRM-LDAVKMPEARKRMrmyPHEFSGGMRQ 185
Cdd:cd03261 73 YRLRRR-MGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEE-IREIVLEkLEAVGLRGAEDLY---PAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARD 265
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 899869912 266 VFYHPsHPY 274
Cdd:cd03261 224 LRASD-DPL 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
37-256 |
1.56e-45 |
|
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: 154.55 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLasnGRIGGSAKFNGREILNLPEKQLNRlraeEI 116
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDLTKLSLKELRR----KV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 117 SMIFQDPMTSL-NPymRVGEQLMEVLqLHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLC 195
Cdd:cd03225 78 GLVFQNPDDQFfGP--TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 196 RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
28-252 |
4.21e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.86 E-value: 4.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 28 VLLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGLL-ASNGRIggsaKFNGREILNLPE 105
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLrLIAGLEkPTSGEV----LVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 kqlnrlraeEISMIFQDPmtSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQ 185
Cdd:COG1116 81 ---------DRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---YPHQLSGGMRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
29-313 |
8.43e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 156.80 E-value: 8.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPekq 107
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPDSGRI----LLDGRDVTGLP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 lnrlrAEE--ISMIFQDPmtSLNPYMRVGEQLMEVLQlHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQ 185
Cdd:COG3842 74 -----PEKrnVGMVFQDY--ALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADR---YPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARD 265
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 899869912 266 VFYHPSHPYS---IGLLNAVP-RLDAEGDSLMTIPGNPpnlLRLPKGCPFQP 313
Cdd:COG3842 223 IYERPATRFVadfIGEANLLPgTVLGDEGGGVRTGGRT---LEVPADAGLAA 271
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
29-272 |
3.69e-44 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 152.64 E-value: 3.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDG-----DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRiggsakfngrEILnL 103
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG----------ELL-I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 PEKQLN----RLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMpeARKRMRMYPHEF 179
Cdd:PRK15112 73 DDHPLHfgdySYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL--LPDHASYYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTME 259
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250
....*....|...
gi 899869912 260 YGQARDVFYHPSH 272
Cdd:PRK15112 231 RGSTADVLASPLH 243
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
29-256 |
4.28e-44 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 150.96 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLPEKQ 107
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLdNPTSGEV----LFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRAEEISMIFQdpMTSLNPYMRVGEQLMEVLqLHKKMSKSEAFEESIRMLDAVKMpeaRKRMRMYPHEFSGGMRQRV 187
Cdd:TIGR02211 77 RAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPL-LIGKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICNKVLVMYAGR 256
Cdd:TIGR02211 151 AIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQ 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
30-252 |
1.79e-43 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 149.54 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALM-GLL-ASNGRIggsaKFNGREIlnlpeKQ 107
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIaGLErPTSGEV----LVDGEPV-----TG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRlraeEISMIFQDPmtSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRV 187
Cdd:cd03293 71 PGP----DRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
33-273 |
2.59e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 152.65 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 33 KDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIggsaKFNGREILNLPEKQLNR 110
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLerPTSGRV----LVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 111 LRaEEISMIFQ--DPMTSLNPYMRVGEQLmEVLQLHKKMSKSEAFEesirMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 188
Cdd:PRK11153 80 AR-RQIGMIFQhfNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTE----LLELVGLSDKADR---YPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFY 268
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
....*
gi 899869912 269 HPSHP 273
Cdd:PRK11153 231 HPKHP 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
29-267 |
3.85e-43 |
|
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: 149.42 E-value: 3.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGLL-ASNGRIggsaKFNGREILNLPEK 106
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLkPSSGEV----LLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QlnrlRAEEISMIFQDPMTSLNpyMRVgeqlMEVLQL----HKKMSKS------EAFEESIRMLDAvkmpeARKRMRMYp 176
Cdd:COG1120 72 E----LARRIAYVPQEPPAPFG--LTV----RELVALgrypHLGLFGRpsaedrEAVEEALERTGL-----EHLADRPV- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 177 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:COG1120 136 DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
250
....*....|.
gi 899869912 257 TMEYGQARDVF 267
Cdd:COG1120 216 IVAQGPPEEVL 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
47-282 |
5.41e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 149.84 E-value: 5.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 47 TAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLNRLRaEEISMIFQDPMTS 126
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQ---GNVSWRGEPLAKLNRAQRKAFR-RDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 127 LNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPE--ARKRmrmyPHEFSGGMRQRVMIAMALLCRPKLLIADE 204
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsvLDKR----PPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 205 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEyGQARDVFYHPSHPYSIGLLNAV 282
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE-TQPVGDKLTFSSPAGRVLQNAV 254
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
29-273 |
1.79e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.45 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIggsaKFNGREIlNLPEK 106
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLeePDSGTI----TVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRAEeISMIFQdpmtSLN--PYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEarkRMRMYPHEFSGGMR 184
Cdd:COG1126 71 DINKLRRK-VGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 185 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQAR 264
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMT-MVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
....*....
gi 899869912 265 DVFYHPSHP 273
Cdd:COG1126 222 EFFENPQHE 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
30-256 |
3.91e-42 |
|
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: 144.46 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQL 108
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEI----KVLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRlraeeISMIFQDPmtSLNPYMRVGEQLmevlqlhkkmskseafeesirmldavkmpearkrmrmyphEFSGGMRQRVM 188
Cdd:cd03230 73 RR-----IGYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
30-261 |
2.01e-41 |
|
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: 143.81 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQL 108
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErPDSGEI----LIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NrlraeeISMIFQDPmtSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 188
Cdd:cd03259 73 N------IGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
30-256 |
5.60e-41 |
|
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: 141.56 E-value: 5.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGREIlNLPEKQLN 109
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE---PDSGSILIDGEDL-TDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRaEEISMIFQDPmtSLNPYMRVGEQLMEVLqlhkkmskseafeesirmldavkmpearkrmrmyphefSGGMRQRVMI 189
Cdd:cd03229 73 PLR-RRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 190 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
49-207 |
7.34e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.48 E-value: 7.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 49 VNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQLNRlraeEISMIFQDPmtSL 127
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTI----LLDGQDLTDDERKSLRK----EIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 128 NPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKR-MRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 206
Cdd:pfam00005 71 FPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 899869912 207 T 207
Cdd:pfam00005 150 A 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
31-261 |
7.42e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 141.42 E-value: 7.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 31 DVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGLL-ASNGRIggsaKFNGREILNLPEKQL 108
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLkPSSGEI----LLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRAeeismifqdpmtslnpYMrvgEQLMEVLQLhkkmskseafeesirmldavkmpeARKRMRMYpHEFSGGMRQRVM 188
Cdd:cd03214 72 ARKIA----------------YV---PQALELLGL------------------------AHLADRPF-NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
29-267 |
9.38e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.92 E-value: 9.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGLLAsngRIGGSAKFNGREilnlPEKQ 107
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP---PTSGTVRLFGKP----PRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRL----RAEEISMIFqdPMT-----SLNPYMRVGeqlmevlqLHKKMSKSEAfEESIRMLDAVKMPE-ARKRMRmyph 177
Cdd:COG1121 74 RRRIgyvpQRAEVDWDF--PITvrdvvLMGRYGRRG--------LFRRPSRADR-EAVDEALERVGLEDlADRPIG---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMyAGRT 257
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGL 216
|
250
....*....|
gi 899869912 258 MEYGQARDVF 267
Cdd:COG1121 217 VAHGPPEEVL 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
43-263 |
3.17e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.96 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 43 DGDVTAVNALNFDLRAGETLGIVGESGSGKSQtafaLMGLLA-----SNGRIggsaKFNGREILNLPEKQLNRLRaEEIS 117
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYgeerpTSGQV----LVNGQDLSRLKRREIPYLR-RRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 118 MIFQDpmTSLNPYMRVGEQLMEVLQLHKKmSKSEAFEESIRMLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLCRP 197
Cdd:COG2884 83 VVFQD--FRLLPDRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 899869912 198 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQA 263
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
32-252 |
6.83e-39 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 137.28 E-value: 6.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGLLAsngRIGGSAKFNGREILNLPEK---- 106
Cdd:cd03235 2 VEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLK---PTSGSIRVFGKPLEKERKRigyv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 ----QLNR---LRAEEISMifqdpmTSLNPYMRvgeqlmevlqLHKKMSKSEaFEESIRMLDAVKMPE-ARKRMRmyphE 178
Cdd:cd03235 74 pqrrSIDRdfpISVRDVVL------MGLYGHKG----------LFRRLSKAD-KAKVDEALERVGLSElADRQIG----E 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
37-283 |
7.74e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 138.72 E-value: 7.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNlpEKQLNRLRaEE 115
Cdd:TIGR04520 6 VSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPTSGKV----TVDGLDTLD--EENLWEIR-KK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ISMIFQDPMTSLnpymrVGEQL-------MEVLQL-HKKMSK--SEAfeesirmLDAVKMPEARKRMrmyPHEFSGGMRQ 185
Cdd:TIGR04520 79 VGMVFQNPDNQF-----VGATVeddvafgLENLGVpREEMRKrvDEA-------LKLVGMEDFRDRE---PHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQARD 265
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPRE 222
|
250
....*....|....*...
gi 899869912 266 VFYHPSHPYSIGLlnAVP 283
Cdd:TIGR04520 223 IFSQVELLKEIGL--DVP 238
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
29-266 |
5.23e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.95 E-value: 5.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIggsaKFNGREILNLPEK 106
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKS-TLLRCLNGLvePTSGEI----LVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRAEeISMIFQDPmtSLNPYMRVgeqlME---------------VLQLHKKMSKSEAFEesirMLDAVKMPE-ARK 170
Cdd:COG3638 74 ALRRLRRR-IGMIFQQF--NLVPRLSV----LTnvlagrlgrtstwrsLLGLFPPEDRERALE----ALERVGLADkAYQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 171 RmrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVL 250
Cdd:COG3638 143 R----ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
250
....*....|....*.
gi 899869912 251 VMYAGRTMEYGQARDV 266
Cdd:COG3638 219 GLRDGRVVFDGPPAEL 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
44-271 |
1.13e-37 |
|
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: 134.67 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLP--EKQLNrlraeeisMIF 120
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEI----LLDGKDITNLPphKRPVN--------TVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 121 QDpmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLL 200
Cdd:cd03300 79 QN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 201 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPS 271
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
30-266 |
1.13e-37 |
|
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: 134.87 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGLL-ASNGRIggsaKFNGREILNLPEKQ 107
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFnLISGFLrPTSGSV----LFDGEDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRaeeISMIFQDPmtSLNPYMRVGEQLMEVLQLHKK---------MSKSEAFEESIRMLDAVKMPEARKRMrmyPHE 178
Cdd:cd03219 72 IARLG---IGRTFQIP--RLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRP---AGE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICNKVLVMYAGRTM 258
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
....*...
gi 899869912 259 EYGQARDV 266
Cdd:cd03219 223 AEGTPDEV 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
52-271 |
3.38e-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: 133.62 E-value: 3.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAFALMGLLasnGRIGGSAKFNGREILNL-PEKqlnrlraEEISMIFQDpmTSLNPY 130
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFI---KPDSGKILLNGKDITNLpPEK-------RDISYVPQN--YALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 131 MRVGEQLMEVLQlHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 210
Cdd:cd03299 86 MTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDHLLNR---KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 211 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPS 271
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
32-256 |
5.59e-37 |
|
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: 130.44 E-value: 5.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLNRl 111
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS---GEILIDGKDIAKLPLEELRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 112 raeEISMIFQdpmtslnpymrvgeqlmevlqlhkkmskseafeesirmldavkmpearkrmrmypheFSGGMRQRVMIAM 191
Cdd:cd00267 74 ---RIGYVPQ---------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 192 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
52-262 |
6.91e-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: 132.45 E-value: 6.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSqTAFALMGLLASNGRigGSAKFNGREILNLPEKQLNRLRaEEISMIFQDpmTSLNPYM 131
Cdd:TIGR02982 24 INLEINPGEIVILTGPSGSGKT-TLLTLIGGLRSVQE--GSLKVLGQELHGASKKQLVQLR-RRIGYIFQA--HNLLGFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 132 RVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 211
Cdd:TIGR02982 98 TARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 899869912 212 TVQAQIMTLLNELKREFNTAIIMITHDlgvvagicNKVLVMyAGRT--MEYGQ 262
Cdd:TIGR02982 175 KSGRDVVELMQKLAKEQGCTILMVTHD--------NRILDV-ADRIlqMEDGK 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
30-288 |
7.30e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 135.66 E-value: 7.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREIL-NLPEKQ 107
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDSGRI----VLNGRDLFtNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNrlraeeISMIFQDPMtsLNPYMRVGEQLMEVLQlHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRV 187
Cdd:COG1118 75 RR------VGFVFQHYA--LFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
250 260
....*....|....*....|.
gi 899869912 268 YHPSHPYSIGLLNAVPRLDAE 288
Cdd:COG1118 223 DRPATPFVARFLGCVNVLRGR 243
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
32-250 |
1.01e-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: 131.20 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLLASNGRigGSAKFNGREILNLPEKQLNRL 111
Cdd:TIGR03608 1 LKNISKKF----GDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFDS--GQVYLNGQETPPLNSKKASKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 112 RAEEISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKmSKSEAFEESIRMLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAM 191
Cdd:TIGR03608 74 RREKLGYLFQN--FALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 192 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLgVVAGICNKVL 250
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
37-256 |
2.19e-36 |
|
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: 129.43 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQLNRLraee 115
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEI----LIDGVDLRDLDLESLRKN---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ISMIFQDPmtslnpymrvgeqlmeVLqlhkkmskseaFEESIRmldavkmpearkrmrmyphE--FSGGMRQRVMIAMAL 193
Cdd:cd03228 78 IAYVPQDP----------------FL-----------FSGTIR-------------------EniLSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 194 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICNKVLVMYAGR 256
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
29-266 |
4.86e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 130.75 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREilnlPEKQL 108
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS---GSILIDGED----VRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRaEEISMIFQDPMtsLNPYMRVGEQLMEVLQLHKKMSKS--EAFEESIRMLDavkMPEARKRmrmYPHEFSGGMRQR 186
Cdd:COG4555 70 REAR-RQIGVLPDERG--LYDRLTVRENIRYFAELYGLFDEElkKRIEELIELLG---LEEFLDR---RVGELSTGMKKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
30-261 |
6.05e-36 |
|
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: 129.93 E-value: 6.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILnlpeKQLN 109
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS---GTAYINGYSIR----TDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRaEEISMIFQDPMtsLNPYMRVgeqlMEVLQLH---KKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQR 186
Cdd:cd03263 72 AAR-QSLGYCPQFDA--LFDELTV----REHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
30-266 |
6.05e-36 |
|
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: 130.38 E-value: 6.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFStpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLN 109
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS---GSVLIDGTDINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEeISMIFQDPmtSLNPYMRVGEQLM-----------EVLQLHKKMSKSEAFEesirMLDAVKMPE-ARKRMRmyph 177
Cdd:cd03256 75 QLRRQ-IGMIFQQF--NLIERLSVLENVLsgrlgrrstwrSLFGLFPKEEKQRALA----ALERVGLLDkAYQRAD---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRT 257
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
....*....
gi 899869912 258 MEYGQARDV 266
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
44-274 |
1.28e-35 |
|
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: 130.46 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLasNGRI---GGSAKFNGREILNLPEKQLNRLRAEEISMIF 120
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCI--NRLIeptSGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 121 QDpmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLL 200
Cdd:cd03294 109 QS--FALLPHRTVLENVAFGLEV-QGVPRAEREERAAEALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 201 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPY 274
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
30-266 |
2.04e-35 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 128.45 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQT--AFALMGLLASNGRIGGSAKFNGREILNLPEKQ 107
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLlrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNrLRAEeISMIFQDPmtslNPY-MRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRmRMYPHEFSGGMRQR 186
Cdd:cd03260 77 LE-LRRR-VGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
30-256 |
3.02e-35 |
|
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: 127.65 E-value: 3.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREIlNLPEKQLN 109
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS---GTIIIDGLKL-TDDKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEeISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEarkRMRMYPHEFSGGMRQRVMI 189
Cdd:cd03262 73 ELRQK-VGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 190 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
37-274 |
3.38e-35 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 128.57 E-value: 3.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDvTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREILNLPEKQLNRlraeE 115
Cdd:cd03295 6 VTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEI----FIDGEDIREQDPVELRR----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ISMIFQDpmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRMRmYPHEFSGGMRQRVMIAMALLC 195
Cdd:cd03295 77 IGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAEFADR-YPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 196 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPY 274
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
30-261 |
3.82e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 127.40 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLN 109
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS---GEVLFDGKPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEEismifqdpmtSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPE-ARKRMRmyphEFSGGMRQRVM 188
Cdd:cd03269 74 YLPEER----------GLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
27-256 |
9.46e-35 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 126.78 E-value: 9.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFS--TPDG-DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMG-LLASNGRIGGSAKFNGREILN 102
Cdd:COG4778 2 TTLLEVENLSKTFTlhLQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVRHDGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 103 LPEKQLNRLRAEEISMIFQdpmtSLNPYMRVG--EQLMEVLqLHKKMSKSEAFEESIRMLDAVKMPEarKRMRMYPHEFS 180
Cdd:COG4778 82 ASPREILALRRRTIGYVSQ----FLRVIPRVSalDVVAEPL-LERGVDREEARARARELLARLNLPE--RLWDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 899869912 181 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
30-256 |
1.44e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPekqLN 109
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS---GEIYLDGKPLSAMP---PP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEeISMIFQDPmtSLnPYMRVGEQLMEVLQLHKKMSKSEAFEEsirMLDAVKMPEARKRMRMypHEFSGGMRQRVMI 189
Cdd:COG4619 71 EWRRQ-VAYVPQEP--AL-WGGTVRDNLPFPFQLRERKFDRERALE---LLERLGLPPDILDKPV--ERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 190 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-287 |
2.35e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 127.92 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREilnLPEKQLN 109
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS---GEVLWDGEP---LDPEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RL------RaeeismifqdpmtSLNPYMRVGEQLMEVLQLHKkMSKSEAFEESIRMLDAVKMPEARKRMRmypHEFSGGM 183
Cdd:COG4152 72 RIgylpeeR-------------GLYPKMKVGEQLVYLARLKG-LSKAEAKRRADEWLERLGLGDRANKKV---EELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 184 RQRVMIAMALLCRPKLLIADEPTTALD-VTVQAqIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG- 261
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGs 212
|
250 260
....*....|....*....|....*...
gi 899869912 262 --QARDVFyhPSHPYSIGLLNAVPRLDA 287
Cdd:COG4152 213 vdEIRRQF--GRNTLRLEADGDAGWLRA 238
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
44-271 |
3.46e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.90 E-value: 3.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNG--RIGGSaKFNGREILNlpEKQLNRLRaEEISMI 119
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDSGqlNIAGH-QFDFSQKPS--EKAIRLLR-QKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 120 FQDpmTSLNPYMRVGEQLME----VLqlhkKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLC 195
Cdd:COG4161 88 FQQ--YNLWPHLTVMENLIEapckVL----GLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 899869912 196 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICNKVLVMYAGRTMEYGQArDVFYHPS 271
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
30-256 |
1.37e-33 |
|
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: 123.63 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKqln 109
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS---GRATVAGHDVVREPRE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 rLRaEEISMIFQDPmtSLNPYMRVGEQLMevlqLHKKM---SKSEAFEESIRMLDAVKMPEARKRMRMYpheFSGGMRQR 186
Cdd:cd03265 71 -VR-RRIGIVFQDL--SVDDELTGWENLY----IHARLygvPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
53-261 |
4.44e-33 |
|
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: 122.02 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 53 NFDLRA-----GETLGIVGESGSGKSQTAFALMGLL-ASNGRI--GGSAKFNGREILNLPEKQlnrlRAeeISMIFQDpm 124
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEkPDGGTIvlNGTVLFDSRKKINLPPQQ----RK--IGLVFQQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 TSLNPYMRVGEQLMEVLQLHKKMSKSEAFEEsirMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADE 204
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRNREDRISVDE---LLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 205 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
29-266 |
1.73e-32 |
|
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: 121.25 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFStpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQL 108
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSS---GSILLEGTDITKLRGKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRAEeISMIFQD-----PMTSL-NPYM-RVGEQ--LMEVLQLHKKMSKSEAFEesirMLDAVKMPE-ARKRMRmyphE 178
Cdd:TIGR02315 75 RKLRRR-IGMIFQHynlieRLTVLeNVLHgRLGYKptWRSLLGRFSEEDKERALS----ALERVGLADkAYQRAD----Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTM 258
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
....*...
gi 899869912 259 EYGQARDV 266
Cdd:TIGR02315 226 FDGAPSEL 233
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
44-256 |
4.14e-32 |
|
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: 121.73 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKqlnrLRaEEISMIFQDP 123
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTS---GTARVAGYDVVREPRK----VR-RSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 mtslNPYMRV-GEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:TIGR01188 76 ----SVDEDLtGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADR---PVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 899869912 203 DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGR 201
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-265 |
5.41e-32 |
|
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: 125.65 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 11 QQSALLEQNAQLEQNQNVLLDVKDltVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrig 90
Cdd:COG4987 315 APPAVTEPAEPAPAPGGPSLELED--VSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS--- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 91 GSAKFNGREILNLPEKQLNRLraeeISMIFQDP---MTSL--NpyMRVG------EQLMEVL---QLHKkmskseaFEES 156
Cdd:COG4987 390 GSITLGGVDLRDLDEDDLRRR----IAVVPQRPhlfDTTLreN--LRLArpdatdEELWAALervGLGD-------WLAA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 157 IRM-LDAVkMPEARKRmrmypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMI 235
Cdd:COG4987 457 LPDgLDTW-LGEGGRR-------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLI 526
|
250 260 270
....*....|....*....|....*....|
gi 899869912 236 THDLgVVAGICNKVLVMYAGRTMEYGQARD 265
Cdd:COG4987 527 THRL-AGLERMDRILVLEDGRIVEQGTHEE 555
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-261 |
7.22e-32 |
|
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: 125.26 E-value: 7.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 14 ALLEQNAQLEQNQNVLLDVKDLTVTFstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggs 92
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSI--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 93 aKFNGREILNLPEKQLNRLraeeISMIFQDPMTslnPYMRVGEQLMevlqlhkkMSKSEAFEEsiRMLDAVKMPEARKRM 172
Cdd:COG4988 395 -LINGVDLSDLDPASWRRQ----IAWVPQNPYL---FAGTIRENLR--------LGRPDASDE--ELEAALEAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 173 RMYPHEF-----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGV 241
Cdd:COG4988 457 AALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL 534
|
250 260
....*....|....*....|
gi 899869912 242 VAgICNKVLVMYAGRTMEYG 261
Cdd:COG4988 535 LA-QADRILVLDDGRIVEQG 553
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
44-285 |
1.54e-31 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 118.75 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLPekqlnrLRAEEISMIFQD 122
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLeQPDSGRI----RLNGQDATRVH------ARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 pmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:TIGR00968 81 --YALFKHLTVRDNIAFGLEI-RKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVALARALAVEPQVLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 203 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGLLNAV 282
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
...
gi 899869912 283 PRL 285
Cdd:TIGR00968 235 NVL 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
52-270 |
2.10e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.58 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGR--IGGSaKFNGREILNlpEKQLNRLRaEEISMIFQDpmTSL 127
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRSGTlnIAGN-HFDFSKTPS--DKAIRELR-RNVGMVFQQ--YNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 128 NPYMRVGEQLME----VLqlhkKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:PRK11124 94 WPHLTVQQNLIEapcrVL----GLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICNKVLVMYAGRTMEYGQArDVFYHP 270
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQP 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-278 |
4.71e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 25 NQNVLLDVKDLTvtFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREilnLP 104
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA---GTITVGGMV---LS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 EKQLNRLRaEEISMIFQDPMTSLnpymrVGEQLME--VLQLHKK-MSKSEAFEesiRMLDAVKmpeaRKRMRMY----PH 177
Cdd:PRK13635 73 EETVWDVR-RQVGMVFQNPDNQF-----VGATVQDdvAFGLENIgVPREEMVE---RVDQALR----QVGMEDFlnrePH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCNKVLVMYAGRT 257
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
250 260
....*....|....*....|.
gi 899869912 258 MEYGQARDVFYHPSHPYSIGL 278
Cdd:PRK13635 219 LEEGTPEEIFKSGHMLQEIGL 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
30-272 |
6.07e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.79 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQL 108
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEdPTSGEI----LIGGRDVTDLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NrlraeeISMIFQDPMtsLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 188
Cdd:COG3839 76 N------IAMVFQSYA--LYPHMTVYENIAFPLKL-RKVPKAEIDRRVREAAELLGLEDLLDR---KPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD------LGvvagicNKVLVMYAGRTMEYGQ 262
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVGT 217
|
250
....*....|
gi 899869912 263 ARDVFYHPSH 272
Cdd:COG3839 218 PEELYDRPAN 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-272 |
1.12e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL--LASNGRIGGSAKFNGREILNLPEKQ 107
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRlraeEISMIFQDPmtSLNPYMRVGEQLMEVLQLHKKM-SKSEAFEESIRMLDAVKM-PEARKRMRMYPHEFSGGMRQ 185
Cdd:PRK14247 80 LRR----RVQMVFQIP--NPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwDEVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARD 265
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....*..
gi 899869912 266 VFYHPSH 272
Cdd:PRK14247 232 VFTNPRH 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
37-261 |
1.61e-30 |
|
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: 122.25 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREILNLPekqLNRLRaEE 115
Cdd:COG2274 479 VSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRI----LIDGIDLRQID---PASLR-RQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ISMIFQDPM----------TSLNPYMRVgEQLMEVLQLhkkmskSEAFEESIRM---LDAVKMPEARKrmrmypheFSGG 182
Cdd:COG2274 551 IGVVLQDVFlfsgtireniTLGDPDATD-EEIIEAARL------AGLHDFIEALpmgYDTVVGEGGSN--------LSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICNKVLVMYAGRTMEYG 261
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-267 |
1.74e-30 |
|
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: 118.66 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 34 DLTVTFSTPDGDVTAvnalnfdlragetlgIVGESGSGKSQTAFALMGLL-ASNGRI--GGSAKFNGREILNLP-EKqln 109
Cdd:COG4148 15 TLDVDFTLPGRGVTA---------------LFGPSGSGKTTLLRAIAGLErPDSGRIrlGGEVLQDSARGIFLPpHR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 rlRAeeISMIFQDPmtSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMpearkrMRMYPHEFSGGMRQRVMI 189
Cdd:COG4148 77 --RR--IGYVFQEA--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHL------LDRRPATLSGGERQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 190 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-279 |
2.68e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 115.51 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLPekqlnr 110
Cdd:cd03296 5 VRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTI----LFGGEDATDVP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 111 LRAEEISMIFQDpmTSLNPYMRVGEQL---MEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRV 187
Cdd:cd03296 71 VQERNVGFVFQH--YALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
250
....*....|..
gi 899869912 268 YHPSHPYSIGLL 279
Cdd:cd03296 226 DHPASPFVYSFL 237
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
47-297 |
2.88e-30 |
|
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: 118.17 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 47 TAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrIGGSAKFNGREILNLPEKQLNrlraeeISMIFQDpmTS 126
Cdd:TIGR03258 19 TVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAG-LTGRIAIADRDLTHAPPHKRG------LALLFQN--YA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 127 LNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 206
Cdd:TIGR03258 90 LFPHLKVEDNVAFGLRA-QKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 207 TALDVTVQAQIMTLLNELKREF-NTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGLLNAVPRL 285
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245
|
250
....*....|..
gi 899869912 286 DAEGDSLMTIPG 297
Cdd:TIGR03258 246 PAIALGITEAPG 257
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
29-272 |
6.81e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.87 E-value: 6.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFAL--MGLLASNGRIGGSAKFNGREILNlPEK 106
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYS-PRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRaEEISMIFQDPmtslNPY-MRVGEQLMEVLQL---HKKMSKSEAFEESIRmlDAVKMPEARKRMRMYPHEFSGG 182
Cdd:PRK14239 80 DTVDLR-KEIGMVFQQP----NPFpMSIYENVVYGLRLkgiKDKQVLDEAVEKSLK--GASIWDEVKDRLHDSALGLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQ 262
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
250
....*....|
gi 899869912 263 ARDVFYHPSH 272
Cdd:PRK14239 231 TKQMFMNPKH 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-256 |
8.48e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.97 E-value: 8.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 28 VLLDVKDLTVTfstpdgdvTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGREILN----- 102
Cdd:COG1129 255 VVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP---ADSGEIRLDGKPVRIrsprd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 103 --------LPEkqlNRLR---------AEEISMifqdpmTSLNPYMRVGeqlmeVLQlHKKMSksEAFEESIRMLDaVKM 165
Cdd:COG1129 324 airagiayVPE---DRKGeglvldlsiRENITL------ASLDRLSRGG-----LLD-RRRER--ALAEEYIKRLR-IKT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 166 PEARKRMRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI 245
Cdd:COG1129 386 PSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGL 460
|
250
....*....|.
gi 899869912 246 CNKVLVMYAGR 256
Cdd:COG1129 461 SDRILVMREGR 471
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
30-261 |
9.39e-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: 113.12 E-value: 9.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLPEKQL 108
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRI----YIGGRDVTDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NrlraeeISMIFQDpmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEesiRMLDAVKMPEARKRMRMYPHEFSGGMRQRVM 188
Cdd:cd03301 73 D------IAMVFQN--YALYPHMTVYDNIAFGLKL-RKVPKDEIDE---RVREVAELLQIEHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
37-256 |
1.20e-29 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 113.11 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFAL--MGLLASNGRIggsaKFNGREILNLPEKQLNRLRaE 114
Cdd:TIGR02673 7 VSKAYP-GGVAALHDVSLHIRKGEFLFLTGPSGAGKT-TLLKLlyGALTPSRGQV----RIAGEDVNRLRGRQLPLLR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 115 EISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKmsKSEAFEESI-RMLDAVKMPEarkRMRMYPHEFSGGMRQRVMIAMAL 193
Cdd:TIGR02673 80 RIGVVFQD--FRLLPDRTVYENVALPLEVRGK--KEREIQRRVgAALRQVGLEH---KADAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 194 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
30-273 |
1.50e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 113.69 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFStpdgDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIG-GSAKFNGREILNLPEK 106
Cdd:PRK11264 4 IEVKNLVKKFH----GQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRvGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRaEEISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQR 186
Cdd:PRK11264 79 LIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS---YPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
....*..
gi 899869912 267 FYHPSHP 273
Cdd:PRK11264 232 FADPQQP 238
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
44-274 |
1.58e-29 |
|
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: 115.90 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLPEKqlnrlrAEEISMIFQD 122
Cdd:TIGR03265 15 GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLeRQTAGTI----YQGGRDITRLPPQ------KRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 pmTSLNPYMRVGEQLMEVLQlHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:TIGR03265 85 --YALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 899869912 203 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPY 274
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPF 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-273 |
3.16e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.82 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 20 AQLEQNQNVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqT---AFALMGLLASNGRIGGSAKFN 96
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKS-TllrCLNRMNDLIPGARVEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 97 GREILNlPEKQLNRLRAEeISMIFQDPmtslNPY-MRVGEQLMEVLQLHKKMSKS---EAFEESIRML---DAVKmpear 169
Cdd:COG1117 77 GEDIYD-PDVDVVELRRR-VGMVFQKP----NPFpKSIYDNVAYGLRLHGIKSKSeldEIVEESLRKAalwDEVK----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 170 KRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICNKV 249
Cdd:COG1117 146 DRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYT 223
|
250 260
....*....|....*....|....
gi 899869912 250 LVMYAGRTMEYGQARDVFYHPSHP 273
Cdd:COG1117 224 AFFYLGELVEFGPTEQIFTNPKDK 247
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-256 |
5.08e-29 |
|
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: 110.21 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 28 VLLDVKDLTVTfstpdgdvTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGREILNLPEKQ 107
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP---PASGEITLDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRaeeISMIFQDPM-TSLNPYMRVGEQLMEVLQLhkkmskseafeesirmldavkmpearkrmrmyphefSGGMRQR 186
Cdd:cd03215 72 AIRAG---IAYVPEDRKrEGLVLDLSVAENIALSSLL------------------------------------SGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
30-256 |
1.01e-28 |
|
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: 110.36 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGeTLGIVGESGSGKSqtafALMGLLA-----SNGRIggsaKFNGREILNLP 104
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILAtltppSSGTI----RIDGQDVLKQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 EKqlnrLRAEeISMIFQDPMTSlnPYMRVGEQL--MEVLqlhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGG 182
Cdd:cd03264 68 QK----LRRR-IGYLPQEFGVY--PNFTVREFLdyIAWL---KGIPSKEVKARVDEVLELVNLGDRAKK---KIGSLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03264 135 MRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
37-255 |
1.37e-28 |
|
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: 110.04 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGdVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGReilNLPEKQlnrlRAEE 115
Cdd:cd03226 5 ISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSI----LLNGK---PIKAKE----RRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ISMIFQDPMTSLnpYMR-VGEQLMEVL-QLHKKMSKSEAfeesirMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMAL 193
Cdd:cd03226 73 IGYVMQDVDYQL--FTDsVREELLLGLkELDAGNEQAET------VLKDLDLYALKER---HPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 899869912 194 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAG 255
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
29-252 |
3.18e-28 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 109.40 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALN---FDLRAGETLGIVGESGSGKSQTAFALMG-LLASNGRIGGSAKFNGREILNLP 104
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQQGGVRLPVLKnvsLTVNAGECVALSGPSGAGKSTLLKSLYAnYLPDSGRILVRHEGAWVDLAQAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 EKQLNRLRAEEISMIFQdpmtslnpYMRV------GEQLMEVLqLHKKMSKSEAFEESIRMLDAVKMPEarKRMRMYPHE 178
Cdd:TIGR02324 81 PREVLEVRRKTIGYVSQ--------FLRViprvsaLEVVAEPL-LERGVPREAARARARELLARLNIPE--RLWHLPPAT 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:TIGR02324 150 FSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-266 |
4.16e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 28 VLLDVKDLTVTfstPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEK 106
Cdd:COG3845 256 VVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRpPASGSI----RLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRaeeISMIFQDPM-TSLNPYMRVGEQLmeVLQLHKK--------MSKSEAFEESIRMLDA--VKMPEARKRMRMy 175
Cdd:COG3845 329 ERRRLG---VAYIPEDRLgRGLVPDMSVAENL--ILGRYRRppfsrggfLDRKAIRAFAEELIEEfdVRTPGPDTPARS- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 176 pheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAG 255
Cdd:COG3845 403 ---LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEG 478
|
250
....*....|.
gi 899869912 256 RTMEYGQARDV 266
Cdd:COG3845 479 RIVGEVPAAEA 489
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
29-238 |
2.00e-27 |
|
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: 106.79 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGLL-ASNGRIggsaKFNGREILNLPEK 106
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKT-TLLrILAGLLpPSAGEV----LWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 qlnrlRAEEISMIFQDPMtsLNPYMRVGEQLMEVLQLHKKMSKSEAFEEsirMLDAVKMPEARKRmrmYPHEFSGGMRQR 186
Cdd:COG4133 73 -----YRRRLAYLGHADG--LKPELTVRENLRFWAALYGLRADREAIDE---ALEAVGLAGLADL---PVRQLSAGQKRR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 238
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
44-256 |
2.48e-27 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 106.72 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLASNGR-IGGSAKFNGREILNLPEKQLNRLRaEEISMIFQD 122
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELpTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 pmTSLNPYMRVGEQL---MEVLQL-HKKMSKseafeesiRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPK 198
Cdd:cd03292 87 --FRLLPDRNVYENVafaLEVTGVpPREIRK--------RVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 199 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
259-341 |
3.21e-27 |
|
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: 102.44 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 259 EYGQARDVFYHPSHPYSIGLLNAVPRLDAEGDSLMTIPGNPPNLLRLPKGCPFQPRCQYAMDRCAS-APALESFGEGRLR 337
Cdd:TIGR01727 4 ETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKePPALVEIAEGHRV 83
|
....
gi 899869912 338 ACYK 341
Cdd:TIGR01727 84 ACHL 87
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-267 |
3.44e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.86 E-value: 3.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTvtFSTPDGDVtAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREIlNLPEKQL 108
Cdd:PRK13639 1 ILETRDLK--YSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS---GEVLIKGEPI-KYDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRaEEISMIFQDPMTSLnpYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQRVM 188
Cdd:PRK13639 74 LEVR-KTVGIVFQNPDDQL--FAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
30-261 |
5.52e-27 |
|
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: 106.04 E-value: 5.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFStPDGDvTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPekqL 108
Cdd:cd03244 3 IEFKNVSLRYR-PNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSI----LIDGVDISKIG---L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRaEEISMIFQDPMT-------SLNPYMRVG-EQLMEVLqlhKKMSKSEAFEESIRMLDAVkmpearkrmrmypHE-- 178
Cdd:cd03244 74 HDLR-SRISIIPQDPVLfsgtirsNLDPFGEYSdEELWQAL---ERVGLKEFVESLPGGLDTV-------------VEeg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 ---FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGiCNKVLVMYA 254
Cdd:cd03244 137 genLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE---AFkDCTVLTIAHRLDTIID-SDRILVLDK 212
|
....*..
gi 899869912 255 GRTMEYG 261
Cdd:cd03244 213 GRVVEFD 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
44-273 |
5.72e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.98 E-value: 5.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLLASNGRigGSAKFNGREI---------LNLPEKQLNRLRAE 114
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPSE--GSIVVNGQTInlvrdkdgqLKVADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 115 EISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEaRKRMRmYPHEFSGGMRQRVMIAMALL 194
Cdd:PRK10619 93 RLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE-RAQGK-YPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 195 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHP 273
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
52-274 |
7.45e-27 |
|
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: 108.66 E-value: 7.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRI--GGSAKFNGREILNLPEKQlnrlRAeeISMIFQDpmTSLN 128
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIvlNGRTLFDSRKGIFLPPEK----RR--IGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 129 PYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMpearkrMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 208
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 899869912 209 LDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPY 274
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
258-322 |
8.68e-27 |
|
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: 100.55 E-value: 8.68e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 258 MEYGQARDVFYHPSHPYSIGLLNAVPRLDAEGDSLMTIPGNPPNLLRLPKGCPFQPRCQYAMDRC 322
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
48-285 |
8.83e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.06 E-value: 8.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 48 AVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGreiLNLPEKQ--LNRLRaEEISMIFQDPM 124
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKI----IIDG---VDITDKKvkLSDIR-KKVGLVFQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 TSLnpYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMP-EARKRMRmyPHEFSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:PRK13637 94 YQL--FEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKS--PFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGLlnAVP 283
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIGL--AVP 247
|
..
gi 899869912 284 RL 285
Cdd:PRK13637 248 QV 249
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
44-273 |
1.00e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.95 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLLASngrI-GGSAKFNGREILNlPEKQLNRLRaEEISMIFQD 122
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEE---ItSGDLIVDGLKVND-PKVDERLIR-QEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 pmTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEarkRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:PRK09493 86 --FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 203 DEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHP 273
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
64-272 |
1.92e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.31 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 64 IVGESGSGKSQTAFALMGLLASN--GRIGGSAKFNGREILNlPEKQLNRLRaEEISMIFQDPmtSLNPYMRVGEQLMEVL 141
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLELNeeARVEGEVRLFGRNIYS-PDVDPIEVR-REVGMVFQYP--NPFPHLTIYDNVAIGV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 142 QLHKKMSKSEAFEESIR--MLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT 219
Cdd:PRK14267 111 KLNGLVKSKKELDERVEwaLKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 899869912 220 LLNELKREFntAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSH 272
Cdd:PRK14267 191 LLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
37-278 |
2.43e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.04 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKFNGreiLNLPEKQLNRLRaEEI 116
Cdd:PRK13640 11 VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDG---ITLTAKTVWDIR-EKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 117 SMIFQDPMtslNPYM--RVGEQLMEVLQlHKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALL 194
Cdd:PRK13640 87 GIVFQNPD---NQFVgaTVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSE---PANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 195 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPY 274
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
....
gi 899869912 275 SIGL 278
Cdd:PRK13640 239 EIGL 242
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
30-238 |
2.49e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.10 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALM-GLLASNGRIGGSAKFNGREILNLPEKQl 108
Cdd:COG4136 2 LSLENLTITL----GGRPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIaGTLSPAFSASGEVLLNGRRLTALPAEQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nrlRAeeISMIFQDPMtsLNPYMRVGEQLMevLQLHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVM 188
Cdd:COG4136 76 ---RR--IGILFQDDL--LFPHLSVGENLA--FALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 238
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
33-270 |
2.60e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 106.33 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 33 KDLTVTFstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTafalmglL--------ASNGRIggsaKFNGREILNLP 104
Cdd:COG1125 5 ENVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT-------LrminrliePTSGRI----LIDGEDIRDLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 EKQLNRlraeEISMIFQDpmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEA--RKRmrmYPHEFSGG 182
Cdd:COG1125 71 PVELRR----RIGYVIQQ--IGLFPHMTVAENIATVPRL-LGWDKERIRARVDELLELVGLDPEeyRDR---YPHELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD------LGvvagicNKVLVMYAGR 256
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDidealkLG------DRIAVMREGR 214
|
250
....*....|....
gi 899869912 257 TMEYGQARDVFYHP 270
Cdd:COG1125 215 IVQYDTPEEILANP 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-259 |
3.62e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.09 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAS-NGRIGGSAKFNGREILNLPEKQ 107
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS----TLLAILAGlDDGSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRAEEISMIFQDPMtsLNPYMRVGEQLmEVLQLHKKMSKSEAFEESIRMLDAVKMPearKRMRMYPHEFSGGMRQRV 187
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFM--LIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLG---KRLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLgVVAGICNKVLVMYAGRTME 259
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-278 |
4.78e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.17 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFSTpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGREilnLPEK 106
Cdd:PRK13642 2 NKILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE---EFEGKVKIDGEL---LTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRaEEISMIFQDPMTSLnpymrVGEQLMEVLQL---HKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGM 183
Cdd:PRK13642 75 NVWNLR-RKIGMVFQNPDNQF-----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 184 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQA 263
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
250
....*....|....*
gi 899869912 264 RDVFYHPSHPYSIGL 278
Cdd:PRK13642 225 SELFATSEDMVEIGL 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-266 |
5.88e-26 |
|
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: 108.35 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 13 SALLEQNAQLEQNQNVLLD-----VKDLTVTFSTPD-GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASN 86
Cdd:TIGR03269 258 AVFMEGVSEVEKECEVEVGepiikVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 87 griggSAKFN---GREILNLPEKQ-LNRLRAEE-ISMIFQDpmTSLNPYMRVGEQLMEVLQLhkKMSKSEAFEESIRMLD 161
Cdd:TIGR03269 338 -----SGEVNvrvGDEWVDMTKPGpDGRGRAKRyIGILHQE--YDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 162 AVKMPE--ARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 239
Cdd:TIGR03269 409 MVGFDEekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDM 488
|
250 260
....*....|....*....|....*..
gi 899869912 240 GVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:TIGR03269 489 DFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
30-238 |
6.65e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.17 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREILNlPekql 108
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLApSSGEI----TLDGVPVTG-P---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nrlrAEEISMIFQDpmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQRVM 188
Cdd:COG4525 75 ----GADRGVVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 238
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
29-280 |
7.34e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.46 E-value: 7.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpDGDvTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLPEKQ 107
Cdd:PRK11607 19 LLEIRNLTKSF---DGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQI----MLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 lnrlraEEISMIFQDpmTSLNPYMRVgEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQRV 187
Cdd:PRK11607 91 ------RPINMMFQS--YALFPHMTV-EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---PHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
250
....*....|....*.
gi 899869912 268 YHPSHPYS---IGLLN 280
Cdd:PRK11607 239 EHPTTRYSaefIGSVN 254
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-278 |
1.07e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 23 EQNQNVLLDVKDltVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREIL 101
Cdd:PRK13648 1 MEDKNSIIVFKN--VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEI----FYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 102 NlpeKQLNRLRaEEISMIFQDP----MTSLNPYmRVGEQLMEVLQLHKKMSK--SEAFEEsIRMLDavkmpearkRMRMY 175
Cdd:PRK13648 75 D---DNFEKLR-KHIGIVFQNPdnqfVGSIVKY-DVAFGLENHAVPYDEMHRrvSEALKQ-VDMLE---------RADYE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 176 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCNKVLVMYAG 255
Cdd:PRK13648 140 PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
250 260
....*....|....*....|...
gi 899869912 256 RTMEYGQARDVFYHPSHPYSIGL 278
Cdd:PRK13648 219 TVYKEGTPTEIFDHAEELTRIGL 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
52-256 |
1.15e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 102.97 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSqTAFALMGLLASNgrIGGSAKFNGREILNLPEKQLNRLRAEEISMIFQdpMTSLNPYM 131
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTP--TSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 132 RVGEQL-MEVLQLHKKmsKSEAFEESIRMLDAVKMpEARKRMRmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 210
Cdd:PRK11629 103 TALENVaMPLLIGKKK--PAEINSRALEMLAAVGL-EHRANHR--PSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 899869912 211 VTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICNKVLVMYAGR 256
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGR 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-267 |
1.26e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTvtFSTPDGdVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREIlNLPEKQ 107
Cdd:PRK13636 5 ILKVEELN--YNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRI----LFDGKPI-DYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRaEEISMIFQDP---MTSLNPYMRVGEQLMEVlqlhkKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMR 184
Cdd:PRK13636 77 LMKLR-ESVGMVFQDPdnqLFSASVYQDVSFGAVNL-----KLPEDEVRKRVDNALKRTGIEHLKDKP---THCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 185 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQAR 264
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
...
gi 899869912 265 DVF 267
Cdd:PRK13636 228 EVF 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-256 |
2.00e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.86 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTF--STPDgDVTAVNALNFDLRAGETLGIVGESGSGKSqTafaLMGLLAsnGRI---GGSAKFNGREILNLP 104
Cdd:COG1101 2 LELKNLSKTFnpGTVN-EKRALDGLNLTIEEGDFVTVIGSNGAGKS-T---LLNAIA--GSLppdSGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 EKQlnrlRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMS--------KSEAFEESIRMLDavkMP-EARKRMRMy 175
Cdd:COG1101 75 EYK----RAKYIGRVFQDPMMGTAPSMTIEENLALAYRRGKRRGlrrgltkkRRELFRELLATLG---LGlENRLDTKV- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 176 pHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH------DLGvvagicNKV 249
Cdd:COG1101 147 -GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeqalDYG------NRL 219
|
....*..
gi 899869912 250 LVMYAGR 256
Cdd:COG1101 220 IMMHEGR 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
30-261 |
2.98e-25 |
|
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: 101.14 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKqLN 109
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS---GEITFDGKSYQKNIEA-LR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAeeismIFQDPmtSLNPYMRVGEQLmEVLQLHKKMSKSEAFEesirMLDAVKMPE-ARKRMRmyphEFSGGMRQRVM 188
Cdd:cd03268 73 RIGA-----LIEAP--GFYPNLTARENL-RLLARLLGIRKKRIDE----VLDVVGLKDsAKKKVK----GFSLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
46-261 |
4.18e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 103.24 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 46 VTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREilnlPEKQLNRLrAEEISMIFqdpm 124
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVpTSGEV----RVLGYV----PFKRRKEF-ARRIGVVF---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 tslnpymrvG--EQL------MEVLQLHKKM---SKSEaFEESIRMLdaVKMPE--------ARK-----RMRMyphEfs 180
Cdd:COG4586 102 ---------GqrSQLwwdlpaIDSFRLLKAIyriPDAE-YKKRLDEL--VELLDlgelldtpVRQlslgqRMRC---E-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 181 ggmrqrvmIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEY 260
Cdd:COG4586 165 --------LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
.
gi 899869912 261 G 261
Cdd:COG4586 237 G 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-266 |
5.72e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTafaLMGLLA-----SNGRIggsaKFNGREIl 101
Cdd:COG1129 2 EPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKS-T---LMKILSgvyqpDSGEI----LLDGEPV- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 102 nlpeKQLNRLRAEE--ISMIFQDPmtSLNPYMRVGEQLMEVLQLHKK--MSKSEAFEESIRMLDAVKMPE-ARKRMRmyp 176
Cdd:COG1129 69 ----RFRSPRDAQAagIAIIHQEL--NLVPNLSVAENIFLGREPRRGglIDWRAMRRRARELLARLGLDIdPDTPVG--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 177 hEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:COG1129 140 -DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGR 217
|
250
....*....|
gi 899869912 257 TMEYGQARDV 266
Cdd:COG1129 218 LVGTGPVAEL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-257 |
6.03e-25 |
|
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: 98.65 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLpekqlN 109
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS---GEILVDGKEVSFA-----S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEE--ISMIFQdpmtslnpymrvgeqlmevlqlhkkmskseafeesirmldavkmpearkrmrmypheFSGGMRQRV 187
Cdd:cd03216 69 PRDARRagIAMVYQ---------------------------------------------------------LSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRT 257
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
51-256 |
8.66e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.21 E-value: 8.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 51 ALNFDL--RAGETLGIVGESGSGKSqtafALMGLLA-----SNGRIggsaKFNGREILNLPEKQlnrlRAeeISMIFQDp 123
Cdd:COG3840 15 PLRFDLtiAAGERVAILGPSGAGKS----TLLNLIAgflppDSGRI----LWNGQDLTALPPAE----RP--VSMLFQE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 mTSLNPYMRVGEQLmeVLQLHKKMSKSEAFEESIR-MLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:COG3840 80 -NNLFPHLTVAQNI--GLGLRPGLKLTAEQRAQVEqALERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 899869912 203 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
37-261 |
1.10e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 104.86 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTafaLMGLLA-----SNGRIggsaKFNGREILNLPekqLNRL 111
Cdd:COG1132 345 VSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKS-T---LVNLLLrfydpTSGRI----LIDGVDIRDLT---LESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 112 RaEEISMIFQDP----MTslnpymrVGEQLmevlqlhkKMSKSEAFEESIRmlDAVKMPEARKRMRMYPH---------- 177
Cdd:COG1132 413 R-RQIGVVPQDTflfsGT-------IRENI--------RYGRPDATDEEVE--EAAKAAQAHEFIEALPDgydtvvgerg 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 -EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCNKVLVMYAGR 256
Cdd:COG1132 475 vNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGR 551
|
....*
gi 899869912 257 TMEYG 261
Cdd:COG1132 552 IVEQG 556
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
29-261 |
1.15e-24 |
|
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: 99.75 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQL 108
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA---GFATVDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRaeeismiFQDPMTSLNPYMRVGEQLMEVLQLH--KKMSKSEAFEESIRMLDavkMPEARKRMrmyPHEFSGGMRQR 186
Cdd:cd03266 78 RRLG-------FVSDSTGLYDRLTARENLEYFAGLYglKGDELTARLEELADRLG---MEELLDRR---VGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
64-287 |
1.38e-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: 101.80 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 64 IVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKqlnrLRAeeISMIFQDpmTSLNPYMRVGEQLMEVLql 143
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS---GSIMLDGEDVTNVPPH----LRH--INMVFQS--YALFPHMTVEENVAFGL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 144 hkKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNE 223
Cdd:TIGR01187 68 --KMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 224 LKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGLLNAVPRLDA 287
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEA 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-277 |
1.64e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 62 LGIVGESGSGKSQTAFALMGLLA---SNGRIGGSAKFNGREILNLPEKQLNRlraeEISMIFQDPmtSLNPYMRVGEQLM 138
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQP--NPFPHLSIYDNIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 139 EVLQLHKKMSKSEA---FEESIRMLDAVKmpEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 215
Cdd:PRK14246 113 YPLKSHGIKEKREIkkiVEECLRKVGLWK--EVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQ 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 899869912 216 QIMTLLNELKREFntAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHP----SHPYSIG 277
Cdd:PRK14246 191 AIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPknelTEKYVIG 254
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
30-266 |
2.29e-24 |
|
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: 99.05 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQL 108
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSI----RFDGRDITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLraeEISMIFQDPMtsLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKmpEARKRMrmyPHEFSGGMRQRVM 188
Cdd:cd03224 73 ARA---GIGYVPEGRR--IFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK--ERRKQL---AGTLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-278 |
2.42e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFStPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREilnLPEKQL 108
Cdd:PRK13650 4 IIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES---GQIIIDGDL---LTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRaEEISMIFQDPMTSLnpymrVGEQLMEVLQL---HKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQ 185
Cdd:PRK13650 77 WDIR-HKIGMVFQNPDNQF-----VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQDFKERE---PARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICNKVLVMYAGRTMEYGQARD 265
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
250
....*....|...
gi 899869912 266 VFYHPSHPYSIGL 278
Cdd:PRK13650 227 LFSRGNDLLQLGL 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
30-261 |
4.84e-24 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 97.87 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFStPDGDvTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPekqL 108
Cdd:cd03369 7 IEVENLSVRYA-PDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKI----EIDGIDISTIP---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRaEEISMIFQDPM-------TSLNPY-MRVGEQLMEVLQLhkkmskSEAFEEsirmldavkmpearkrmrmypheFS 180
Cdd:cd03369 78 EDLR-SSLTIIPQDPTlfsgtirSNLDPFdEYSDEEIYGALRV------SEGGLN-----------------------LS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 181 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGiCNKVLVMYAGRTME 259
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE---EFtNSTILTIAHRLRTIID-YDKILVMDAGEVKE 203
|
..
gi 899869912 260 YG 261
Cdd:cd03369 204 YD 205
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-267 |
6.26e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.65 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTafaLMGLLA-----SNGRIggsaKFNGREILNL 103
Cdd:COG4559 1 MLEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKS-T---LLKLLTgeltpSSGEV----RLNGRPLAAW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 PEKQLNRLRAeeisMIFQDpmTSLN-PYmRVgeqlMEVLQL----HkkmSKSEAFEESI--RMLDAVKMpeARKRMRMYP 176
Cdd:COG4559 69 SPWELARRRA----VLPQH--SSLAfPF-TV----EEVVALgrapH---GSSAAQDRQIvrEALALVGL--AHLAGRSYQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 177 hEFSGGMRQRVMIAMAlLC--------RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNK 248
Cdd:COG4559 133 -TLSGGEQQRVQLARV-LAqlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADR 209
|
250
....*....|....*....
gi 899869912 249 VLVMYAGRTMEYGQARDVF 267
Cdd:COG4559 210 ILLLHQGRLVAQGTPEEVL 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-267 |
9.35e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.93 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 25 NQNVLLDVKDLTVTFSTPdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNG--RIGGSAKF--NGREI 100
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTP-FEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETgqTIVGDYAIpaNLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 101 lnlpeKQLNRLRaEEISMIFQDPMTSLnpYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPeaRKRMRMYPHEFS 180
Cdd:PRK13645 83 -----KEVKRLR-KEIGLVFQFPEYQL--FQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 181 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEY 260
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
....*..
gi 899869912 261 GQARDVF 267
Cdd:PRK13645 233 GSPFEIF 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
45-258 |
1.22e-23 |
|
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: 97.40 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 45 DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGreilNLPEKQLNRLRAEeISMIFQDPm 124
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS---GEVRVAG----LVPWKRRKKFLRR-IGVVFGQK- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 tslnpymrvgEQL------MEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPK 198
Cdd:cd03267 104 ----------TQLwwdlpvIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 199 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTM 258
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
27-270 |
1.36e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTF-STPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASN------GRIGGSAKFNGRE 99
Cdd:PRK13631 19 DIILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKygtiqvGDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 100 ILNLPE----KQLNRLRaEEISMIFQDPMTSLnpYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLdaVKMPEARKRMRMY 175
Cdd:PRK13631 99 LITNPYskkiKNFKELR-RRVSMVFQFPEYQL--FKDTIEKDIMFGPVALGVKKSEAKKLAKFYL--NKMGLDDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 176 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAG 255
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|....*
gi 899869912 256 RTMEYGQARDVFYHP 270
Cdd:PRK13631 253 KILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
53-278 |
2.21e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.78 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 53 NFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILN-LPEKQLNRLRaEEISMIFQDPMtslnpym 131
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTS---GTVTIGERVITAgKKNKKLKPLR-KKVGIVFQFPE------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 132 rvgEQLME--VLQ------LHKKMSKSEAFEESIRMLDAVKMPEarKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:PRK13634 96 ---HQLFEetVEKdicfgpMNFGVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGL 278
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGL 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
48-267 |
2.62e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.54 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 48 AVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILN-LPEKQLNRLRaEEISMIFQDPMTS 126
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT---GTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 127 LnpYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 206
Cdd:PRK13646 98 L--FEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 207 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-243 |
2.95e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.95 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAS-NGRIGGSAKFNGREILNLPE 105
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGClDKPTSGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 KQLNRLRAEEISMIFQdpMTSLNPYMrVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEarkRMRMYPHEFSGGMRQ 185
Cdd:PRK10535 78 DALAQLRREHFGFIFQ--RYHLLSHL-TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVA 243
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAA 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
26-270 |
5.86e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 26 QNVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIggsaKFNGREILNL 103
Cdd:PRK09452 11 LSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIAGFetPDSGRI----MLDGQDITHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 PEKQlnrlraEEISMIFQDpmTSLNPYMRVGEQLMEVLqlhkKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGM 183
Cdd:PRK09452 82 PAEN------RHVNTVFQS--YALFPHMTVFENVAFGL----RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 184 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQA 263
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
....*..
gi 899869912 264 RDVFYHP 270
Cdd:PRK09452 230 REIYEEP 236
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
44-239 |
9.52e-23 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 97.87 E-value: 9.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSqTafaLMGLLasNGRI---GGSAKFNGREILNLPEKQLNRLRAEEISMIF 120
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKS-T---LVRCL--NRLIeptAGEVLIDGEDITKLSKKELRELRRKKMSMVF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 121 QdpmtS--LNPYMRVGEQL---MEVlqlhKKMSKSEAFEESIRMLDAV--KMPEARkrmrmYPHEFSGGMRQRVMIAMAL 193
Cdd:COG4175 112 Q----HfaLLPHRTVLENVafgLEI----QGVPKAERRERAREALELVglAGWEDS-----YPDELSGGMQQRVGLARAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 899869912 194 LCRPKLLIADEPTTALD----VTVQAQIMTLLNELKRefnTaIIMITHDL 239
Cdd:COG4175 179 ATDPDILLMDEAFSALDplirREMQDELLELQAKLKK---T-IVFITHDL 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
25-267 |
1.20e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.44 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 25 NQNVLLDVKDltVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREI--LN 102
Cdd:PRK13632 3 NKSVMIKVEN--VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS---GEIKIDGITIskEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 103 LPEkqlnrLRaEEISMIFQDPMTSLnpymrVGEQLME--VLQLHKKMSKSEAFEESIRML-DAVKMPEARKRMrmyPHEF 179
Cdd:PRK13632 78 LKE-----IR-KKIGIIFQNPDNQF-----IGATVEDdiAFGLENKKVPPKKMKDIIDDLaKKVGMEDYLDKE---PQNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICNKVLVMYAGRTME 259
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
....*...
gi 899869912 260 YGQARDVF 267
Cdd:PRK13632 223 QGKPKEIL 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-257 |
1.23e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTafaLM----GLL-ASNGRIggsaKFNGREI-LN 102
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKS-T---LMkilyGLYqPDSGEI----LIDGKPVrIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 103 LPeKQLNRLRaeeISMIFQDPMtsLNPYMRVGEQLmeVLqlhkkmskseAFEESIRMLdaVKMPEARKR----MRMYP-- 176
Cdd:COG3845 73 SP-RDAIALG---IGMVHQHFM--LVPNLTVAENI--VL----------GLEPTKGGR--LDRKAARARirelSERYGld 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 177 -------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALdvTVQ--AQIMTLLNELKREfNTAIIMITHDLGVVAGICN 247
Cdd:COG3845 133 vdpdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIAD 209
|
250
....*....|
gi 899869912 248 KVLVMYAGRT 257
Cdd:COG3845 210 RVTVLRRGKV 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
33-237 |
1.30e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 94.26 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 33 KDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKFNGREilnlPEKQLNRlr 112
Cdd:cd03234 7 WDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQP----RKPDQFQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 113 aEEISMIFQDpmTSLNPYMRVGEQL--MEVLQLHKKMSKS--EAFEESIRMLDAVKMPEARKRMRmyphEFSGGMRQRVM 188
Cdd:cd03234 81 -KCVAYVRQD--DILLPGLTVRETLtyTAILRLPRKSSDAirKKRVEDVLLRDLALTRIGGNLVK----GISGGERRRVS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 899869912 189 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 237
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-261 |
1.42e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.57 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTvtFSTPDGdVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLPE 105
Cdd:PRK13647 2 DNIIEVEDLH--FRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRV----KVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 KQLNRlraeEISMIFQDP---MTSLNPYMRV--GEQLMEvlqlhkkMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFS 180
Cdd:PRK13647 75 KWVRS----KVGLVFQDPddqVFSSTVWDDVafGPVNMG-------LDKDEVERRVEEALKAVRMWDFRDKP---PYHLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 181 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEY 260
Cdd:PRK13647 141 YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
.
gi 899869912 261 G 261
Cdd:PRK13647 220 G 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-257 |
1.44e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.46 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAS---NGRIGGSAKFNGREIlnlpe 105
Cdd:PRK13549 5 LLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKS----TLMKVLSGvypHGTYEGEIIFEGEEL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 kQLNRLRAEE---ISMIFQDPMtsLNPYMRVGEQ--LMEVLQLHKKMSKSEAFEESIRMLDAVKM---PEARKRmrmyph 177
Cdd:PRK13549 72 -QASNIRDTEragIAIIHQELA--LVKELSVLENifLGNEITPGGIMDYDAMYLRAQKLLAQLKLdinPATPVG------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRT 257
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRH 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
47-278 |
1.58e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.54 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 47 TAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNlpEKQLNRLRaEEISMIFQDP--- 123
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE---GKVYVDGLDTSD--EENLWDIR-NKAGMVFQNPdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 --MTSLNPYMRVGEQLMEVLQLHKKMSKSEAfeesirmLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALLCRPKLLI 201
Cdd:PRK13633 98 ivATIVEEDVAFGPENLGIPPEEIRERVDES-------LKKVGMYEYRRHA---PHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 202 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGL 278
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKKIGL 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
44-288 |
1.66e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREIlnlpekqlNRLRAEE--ISMIFQ 121
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS---GHIRFHGTDV--------SRLHARDrkVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 122 DpmTSLNPYMRVGEQL---MEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPK 198
Cdd:PRK10851 82 H--YALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 199 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGL 278
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF 236
|
250
....*....|
gi 899869912 279 LNAVPRLDAE 288
Cdd:PRK10851 237 MGEVNRLQGT 246
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-237 |
3.37e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.57 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 14 ALLEQNAQLEQNQNVLLDVKDLTVTfsTPDGDVTaVNALNFDLRAGETLGIVGESGSGKSqTAF-ALMGL-LASNGRIGG 91
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTLR--TPDGRPL-LEDLSLSLKPGERLLITGPSGSGKS-TLLrAIAGLwPYGSGRIAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 92 SAkfnGREILNLPEKqlnrlraeeismifqdpmtslnPYMRVGEqLMEVL---QLHKKMSKSEAfeesIRMLDAVKMPEA 168
Cdd:COG4178 423 PA---GARVLFLPQR----------------------PYLPLGT-LREALlypATAEAFSDAEL----REALEAVGLGHL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 899869912 169 RKRM---RMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkREFNTAIIMITH 237
Cdd:COG4178 473 AERLdeeADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
49-256 |
5.47e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 96.43 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 49 VNALNFDLRAGETLGIVGESGSGKSQTAFALMGllASNGRIGGSAKFNGREI-LNLPEKQLnrlrAEEISMIFQD-PMTS 126
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGKFEGNVFINGKPVdIRNPAQAI----RAGIAMVPEDrKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 127 LNPYMRVGEQL-MEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYP-HEFSGGMRQRVMIAMALLCRPKLLIADE 204
Cdd:TIGR02633 350 IVPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 899869912 205 PTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-267 |
5.93e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.30 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 28 VLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMG-LLASNGRIggsaKFNGREILNLPEK 106
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEV----RLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRA---EEISMIFqdPMT-------SLNPYMRVGEQLMEVLQlhkkmskseafeesiRMLDAVKMPEARKRMrmYP 176
Cdd:PRK13548 73 ELARRRAvlpQHSSLSF--PFTveevvamGRAPHGLSRAEDDALVA---------------AALAQVDLAHLAGRD--YP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 177 hEFSGGMRQRVMIAMALL------CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVL 250
Cdd:PRK13548 134 -QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIV 212
|
250
....*....|....*..
gi 899869912 251 VMYAGRTMEYGQARDVF 267
Cdd:PRK13548 213 LLHQGRLVADGTPAEVL 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-266 |
6.07e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.68 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLN 109
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLraeeISMIFQDpmTSLNPYMRVgEQLMEVLQlHKKMSKSEAFEESIRMldAVKMPEARKRMRMYPH----EFSGGMRQ 185
Cdd:PRK09536 77 RR----VASVPQD--TSLSFEFDV-RQVVEMGR-TPHRSRFDTWTETDRA--AVERAMERTGVAQFADrpvtSLSGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMItHDLGVVAGICNKVLVMYAGRTMEYGQARD 265
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
.
gi 899869912 266 V 266
Cdd:PRK09536 226 V 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-252 |
7.39e-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: 96.20 E-value: 7.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 14 ALLEQNAQLEQNQNVLLDVKDLT-----VTFSTPDGDVtAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGr 88
Cdd:TIGR02857 299 AVLDAAPRPLAGKAPVTAAPASSlefsgVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 89 igGSAKFNGREILNLPEKQLNRlraeEISMIFQdpmtslNPYMRVGeQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEA 168
Cdd:TIGR02857 377 --GSIAVNGVPLADADADSWRD----QIAWVPQ------HPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 169 RKRMRMYP-----HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVA 243
Cdd:TIGR02857 444 LPQGLDTPigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA 521
|
....*....
gi 899869912 244 GiCNKVLVM 252
Cdd:TIGR02857 522 L-ADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
37-256 |
9.20e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 90.74 E-value: 9.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREILNLPEKQLNRlraee 115
Cdd:cd03246 6 VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRV----RLDGADISQWDPNELGD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ismifqdpmtslnpymRVGeQLMEVLQLhkkmskseaFEESIRmlDAVkmpearkrmrmypheFSGGMRQRVMIAMALLC 195
Cdd:cd03246 77 ----------------HVG-YLPQDDEL---------FSGSIA--ENI---------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 196 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAgICNKVLVMYAGR 256
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLA-SADRILVLEDGR 172
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-256 |
1.01e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.77 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 28 VLLDVKDLTVtFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGllASNGRIGGSAKFNGREI-LNLPEK 106
Cdd:PRK13549 258 VILEVRNLTA-WDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGRWEGEIFIDGKPVkIRNPQQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLnrlrAEEISMIFQD-PMTSLNPYMRVGEQL-MEVLQLHKKMS------KSEAFEESIRMLdAVKMPEARKRMRmyphE 178
Cdd:PRK13549 335 AI----AQGIAMVPEDrKRDGIVPVMGVGKNItLAALDRFTGGSriddaaELKTILESIQRL-KVKTASPELAIA----R 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
56-274 |
1.39e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 94.71 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 56 LRAGETLGIVGESGSGKSqTAFALMGLLASNGRigGSAKFNGREILNLPEKQLNRLRAEEISMIFQDpmTSLNPYMRVge 135
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKS-TMVRLLNRLIEPTR--GQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FALMPHMTV-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 136 qlMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 215
Cdd:PRK10070 124 --LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 216 QIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPY 274
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
52-267 |
1.50e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.97 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREI-LNLPEKQLNRLRaEEISMIFQDPMTslnpy 130
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS---GTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEA----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 131 mrvgeQLME--VLQ------LHKKMSKSEAFEESIRMLDAVKMPEarKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:PRK13641 97 -----QLFEntVLKdvefgpKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 203 DEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
37-261 |
1.63e-21 |
|
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: 91.45 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPD-GDVTAVNALNFDLRAGETLGIVGESGSGKSQTafalMGLL-----ASNGRIggsaKFNGREILNLPekqLNR 110
Cdd:cd03249 6 VSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTV----VSLLerfydPTSGEI----LLDGVDIRDLN---LRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 111 LRaEEISMIFQDPMTSlnpYMRVGEQLmevlqlhkKMSKSEAFEESIRmlDAVKMPEARKRMRMYPHEF----------- 179
Cdd:cd03249 75 LR-SQIGLVSQEPVLF---DGTIAENI--------RYGKPDATDEEVE--EAAKKANIHDFIMSLPDGYdtlvgergsql 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCNKVLVMYAGRTME 259
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
|
..
gi 899869912 260 YG 261
Cdd:cd03249 218 QG 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
37-261 |
1.68e-21 |
|
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: 91.52 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGdVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLL-----ASNGRIggsaKFNGREILNLpekQLNRL 111
Cdd:cd03253 6 VTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLfrfydVSSGSI----LIDGQDIREV---TLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 112 RaEEISMIFQDpmTSL-------N-PYMRVG---EQLMEVlqlhkkmSKSEAFEESIrmldaVKMPEA-------RKRMr 173
Cdd:cd03253 74 R-RAIGVVPQD--TVLfndtigyNiRYGRPDatdEEVIEA-------AKAAQIHDKI-----MRFPDGydtivgeRGLK- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 174 mypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCNKVLVMY 253
Cdd:cd03253 138 -----LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLK 209
|
....*...
gi 899869912 254 AGRTMEYG 261
Cdd:cd03253 210 DGRIVERG 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
52-272 |
1.95e-21 |
|
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: 91.37 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSqtafALMGLLAS-NGRIGGSAKFNGREIlnlPEKQLNRLraeeisMIFQDpmTSLNPY 130
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKS----TLLNLISGlAQPTSGGVILEGKQI---TEPGPDRM------VVFQN--YSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 131 MRVGEQL-MEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 209
Cdd:TIGR01184 69 LTVRENIaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 210 DVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV-FYHPSH 272
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
37-256 |
2.19e-21 |
|
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: 90.73 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREIlnlpeKQLNR--LRA 113
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTSGSV----LLDGTDI-----RQLDPadLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 114 EeISMIFQDPMTSlnpYMRVGEQLMevlqlhkkMSKSEAFEEsiRMLDAVKMPEARKRMRMYPHEF-----------SGG 182
Cdd:cd03245 79 N-IGYVPQDVTLF---YGTLRDNIT--------LGAPLADDE--RILRAAELAGVTDFVNKHPNGLdlqigergrglSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAgICNKVLVMYAGR 256
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
37-267 |
2.26e-21 |
|
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: 94.81 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrIGGSAKFNGREILNLPEKQLNRLraeeI 116
Cdd:COG4618 336 LTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP---TAGSVRLDGADLSQWDREELGRH----I 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 117 SMIFQDPmtslnpymrvgeqlmevlqlhkkmsksEAFEESI-----RM--LDAVKMPEARKRMRMypHEF---------- 179
Cdd:COG4618 409 GYLPQDV---------------------------ELFDGTIaeniaRFgdADPEKVVAAAKLAGV--HEMilrlpdgydt 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 ---------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAgICNKVL 250
Cdd:COG4618 460 rigeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLL 537
|
250
....*....|....*..
gi 899869912 251 VMYAGRTMEYGQARDVF 267
Cdd:COG4618 538 VLRDGRVQAFGPRDEVL 554
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-256 |
2.84e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 94.30 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 15 LLEQNAQLEQNQ-NVLLDVKDLtvtfSTPDgdvtaVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSA 93
Cdd:PRK10762 242 LEDQYPRLDKAPgEVRLKVDNL----SGPG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP---RTSGYV 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 94 KFNGREILNL-PEKQLnrlrAEEISMIFQD----------------PMTSLNPYMRVGEQLmevlqlhKKMSKSEAFEES 156
Cdd:PRK10762 310 TLDGHEVVTRsPQDGL----ANGIVYISEDrkrdglvlgmsvkenmSLTALRYFSRAGGSL-------KHADEQQAVSDF 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 157 IRMLDaVKMPEARKRMRMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMIT 236
Cdd:PRK10762 379 IRLFN-IKTPSMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVS 452
|
250 260
....*....|....*....|
gi 899869912 237 HDLGVVAGICNKVLVMYAGR 256
Cdd:PRK10762 453 SEMPEVLGMSDRILVMHEGR 472
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
52-256 |
4.46e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.96 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQlnRLRA--------EEISMIFQDP 123
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG---GRIMLNGKEINALSTAQ--RLARglvylpedRQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 MTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIrmldAVKMPEARKRMRmyphEFSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAVLERYRRAL----NIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-261 |
1.29e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.72 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 26 QNVLLDVKDLTVTFSTpDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGllasngRI----GGSAKFNGREIL 101
Cdd:PRK13657 329 GRVKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQ------RVfdpqSGRILIDGTDIR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 102 NLPEKQLNRlraeEISMIFQDPM---TSLNPYMRVG------EQLMEVLqlhKKMSKSEAFEESIRMLDAVkmpeARKRM 172
Cdd:PRK13657 401 TVTRASLRR----NIAVVFQDAGlfnRSIEDNIRVGrpdatdEEMRAAA---ERAQAHDFIERKPDGYDTV----VGERG 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 173 RMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAGiCNKVLVM 252
Cdd:PRK13657 470 RQ----LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVF 542
|
....*....
gi 899869912 253 YAGRTMEYG 261
Cdd:PRK13657 543 DNGRVVESG 551
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-261 |
1.48e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.60 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 11 QQSALLEQNAQLEQNQNVLLDVKDLTVTfsTPDGDVTAVNaLNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrig 90
Cdd:PRK11174 331 PLAHPQQGEKELASNDPVTIEAEDLEIL--SPDGKTLAGP-LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 91 gSAKFNGREILNLPEKQLNRlraeEISMIFQDPmtslnpymrvgeQLME------VLqlhkkMSKSEAFEESIRMLDAvk 164
Cdd:PRK11174 405 -SLKINGIELRELDPESWRK----HLSWVGQNP------------QLPHgtlrdnVL-----LGNPDASDEQLQQALE-- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 165 mpearkrmRMYPHEF-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELK 225
Cdd:PRK11174 461 --------NAWVSEFlpllpqgldtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS 532
|
250 260 270
....*....|....*....|....*....|....*.
gi 899869912 226 REFNTaiIMITHDLGVVAGiCNKVLVMYAGRTMEYG 261
Cdd:PRK11174 533 RRQTT--LMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
26-271 |
1.57e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.93 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 26 QNVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsakF-NGREILNl 103
Cdd:PRK11432 3 QKNFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQI-----FiDGEDVTH- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 pekqlNRLRAEEISMIFQDpmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFE---ESIRMLDAVKMpEARkrmrmYPHEFS 180
Cdd:PRK11432 73 -----RSIQQRDICMVFQS--YALFPHMSLGENVGYGLKM-LGVPKEERKQrvkEALELVDLAGF-EDR-----YVDQIS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 181 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEY 260
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
|
250
....*....|.
gi 899869912 261 GQARDVFYHPS 271
Cdd:PRK11432 219 GSPQELYRQPA 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
30-256 |
1.63e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.97 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGllasNGR---IGGSAKFNGREILNL-PE 105
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG----HPKyevTSGSILLDGEDILELsPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 KqlnrlRAEE-ISMIFQDPM------------TSLNpymRVGEQLMEVLQLHKKMSKseafeesirMLDAVKMPEA-RKR 171
Cdd:COG0396 73 E-----RARAgIFLAFQYPVeipgvsvsnflrTALN---ARRGEELSAREFLKLLKE---------KMKELGLDEDfLDR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 172 mrmYPHE-FSGGMRQRVMIA-MALLcRPKLLIADEPTTALDVTVqAQIMT-LLNELKREfNTAIIMITH-----DLGVVa 243
Cdd:COG0396 136 ---YVNEgFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIDA-LRIVAeGVNKLRSP-DRGILIITHyqrilDYIKP- 208
|
250
....*....|...
gi 899869912 244 gicNKVLVMYAGR 256
Cdd:COG0396 209 ---DFVHVLVDGR 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-277 |
1.67e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 92.20 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAS---NGRIGGSAKFNGREilnLPE 105
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKS----TLMKILSGvypHGTWDGEIYWSGSP---LKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 KQLNRLRAEEISMIFQDPMtsLNPYMRVGEQLM---EVLQLHKKMSKSEAFEESIRMLDAVK---MPEARKRMrmyphEF 179
Cdd:TIGR02633 70 SNIRDTERAGIVIIHQELT--LVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQldaDNVTRPVG-----DY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR--- 256
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQhva 221
|
250 260 270
....*....|....*....|....*....|....
gi 899869912 257 -------------TMEYGQARDVFYhPSHPYSIG 277
Cdd:TIGR02633 222 tkdmstmseddiiTMMVGREITSLY-PHEPHEIG 254
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
37-237 |
1.69e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 86.82 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTaVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIGgsaKFNGREILNLPEKqlnrlraee 115
Cdd:cd03223 6 LSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWpWGSGRIG---MPEGEDLLFLPQR--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ismifqdpmtslnPYMRVGeQLMEVLqlhkkmskseafeesirmldavkmpearkrmrMYP--HEFSGGMRQRVMIAMAL 193
Cdd:cd03223 73 -------------PYLPLG-TLREQL--------------------------------IYPwdDVLSGGEQQRLAFARLL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 899869912 194 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKrefnTAIIMITH 237
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
44-256 |
1.85e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLASNGR-IGGSAKFNGREILNLPEKQLNRLRaEEISMIFQD 122
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKS----TLLKLICGIERpSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 P--MTSLNPYMRVGEQLMevlqlhkkmsKSEAFEESIR-----MLDAVKMPEarkRMRMYPHEFSGGMRQRVMIAMALLC 195
Cdd:PRK10908 88 HhlLMDRTVYDNVAIPLI----------IAGASGDDIRrrvsaALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 196 RPKLLIADEPTTALDVTVQAQIMTLLNELKReFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
30-261 |
2.15e-20 |
|
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: 87.61 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFSTPDGDVTA--VNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLaSNGRIGGSAKFNGReilNLPEKQ 107
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEVLINGR---PLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLraeeISMIFQDPMtsLNPYMRVGEQLMEVLQLhkkmskseafeesiRMLdavkmpearkrmrmyphefSGGMRQRV 187
Cdd:cd03213 80 FRKI----IGYVPQDDI--LHPTLTVRETLMFAAKL--------------RGL-------------------SGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDL-GVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-270 |
3.03e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.51 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQL 108
Cdd:PRK11300 5 LLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG---GTILLRGQHIEGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLraeEISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKM--------------SKSEAFEESIRMLDAVKMPEARKRMrm 174
Cdd:PRK11300 78 ARM---GVVRTFQH--VRLFREMTVIENLLVAQHQQLKTglfsgllktpafrrAESEALDRAATWLERVGLLEHANRQ-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 175 yPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYA 254
Cdd:PRK11300 151 -AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
250
....*....|....*.
gi 899869912 255 GRTMEYGQARDVFYHP 270
Cdd:PRK11300 230 GTPLANGTPEEIRNNP 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
33-266 |
4.53e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 33 KDLTVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTafaLMGLLA-----------SNGRIGG----SAKFN- 96
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKS-T---LLKLIAgileptsgrveVNGRVSAllelGAGFHp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 97 ---GRE-------ILNLPEKQLNRlRAEEIsmifqdpmtslnpymrvgeqlmevlqlhkkmsksEAFEEsirmL-DAVKM 165
Cdd:COG1134 102 eltGREniylngrLLGLSRKEIDE-KFDEI----------------------------------VEFAE----LgDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 166 PearkrMRMYphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI 245
Cdd:COG1134 143 P-----VKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRL 212
|
250 260
....*....|....*....|.
gi 899869912 246 CNKVLVMYAGRTMEYGQARDV 266
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDPEEV 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-270 |
6.69e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.78 E-value: 6.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFSTPdgdvTAVNALNFDLRAGETLGIVGESGSGKSQTAFAL--MGLLASNGRIGGSAKFNGREILnlpEKQ 107
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNQNIY---ERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 --LNRLRaEEISMIFQDPmtSLNPyMRVGEQL---MEVLQLHKKMSKSEAFEESIRmlDAVKMPEARKRMRMYPHEFSGG 182
Cdd:PRK14258 81 vnLNRLR-RQVSMVHPKP--NLFP-MSVYDNVaygVKIVGWRPKLEIDDIVESALK--DADLWDEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYA-----GRT 257
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQL 234
|
250
....*....|...
gi 899869912 258 MEYGQARDVFYHP 270
Cdd:PRK14258 235 VEFGLTKKIFNSP 247
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
51-267 |
8.63e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 51 ALNFDLRAGETLGIVGESGSGKSqTAFALM-GLLASNGRIggsaKFNGREILNLPEKQLNRLRAeeisMIFQDPMTSLNp 129
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLPGQGEI----LLNGRPLSDWSAAELARHRA----YLSQQQSPPFA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 130 yMRVGEqlmeVLQLHkkMSKSEAFEESIRMLDAV--KMPEARKRMRMYpHEFSGGMRQRVMIAMALL-------CRPKLL 200
Cdd:COG4138 84 -MPVFQ----YLALH--QPAGASSEAVEQLLAQLaeALGLEDKLSRPL-TQLSGGEWQRVRLAAVLLqvwptinPEGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 201 IADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCQQGIT-VVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
30-261 |
8.73e-20 |
|
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: 86.90 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDltVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLA-----SNGRIggsaKFNGREILNLp 104
Cdd:cd03251 1 VEFKN--VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPrfydvDSGRI----LIDGHDVRDY- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 ekQLNRLRaEEISMIFQDPM---TSLNPYMRVGeqlmevlqlhkkmsKSEAFEESIRmlDAVKMPEArkrmrmypHEF-- 179
Cdd:cd03251 70 --TLASLR-RQIGLVSQDVFlfnDTVAENIAYG--------------RPGATREEVE--EAARAANA--------HEFim 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 -----------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLGVV 242
Cdd:cd03251 123 elpegydtvigergvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRLSTI 200
|
250
....*....|....*....
gi 899869912 243 AGIcNKVLVMYAGRTMEYG 261
Cdd:cd03251 201 ENA-DRIVVLEDGKIVERG 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
37-261 |
1.05e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 85.06 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLpEKQLnrlrAEEI 116
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQ---GEITLDGVPVSDL-EKAL----SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 117 SMIFQDPM---TSLnpYMRVGEQlmevlqlhkkmskseafeesirmldavkmpearkrmrmypheFSGGMRQRVMIAMAL 193
Cdd:cd03247 78 SVLNQRPYlfdTTL--RNNLGRR------------------------------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 194 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGIcNKVLVMYAGRTMEYG 261
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-304 |
1.06e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 25 NQNVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAsngrigGSAKFNGREIL--N 102
Cdd:PRK11247 8 NQGTPLLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLA------GLETPSAGELLagT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 103 LPekqLNRLRaEEISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKmskseafEESIRMLDAVKMPEarkRMRMYPHEFSGG 182
Cdd:PRK11247 74 AP---LAEAR-EDTRLMFQD--ARLLPWKKVIDNVGLGLKGQWR-------DAALQALAAVGLAD---RANEWPAALSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRtmeygq 262
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK------ 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 899869912 263 ardvfyhpshpysIGLLNAV----PR---------LDAEG-DSLMTIPGNPPNLLR 304
Cdd:PRK11247 212 -------------IGLDLTVdlprPRrrgsarlaeLEAEVlQRVMSRGESEPTRLR 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-288 |
1.51e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.61 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLN 109
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS---GTVFLGDKPISMLSSRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RlraeEISMIFQDPMT------------SLNPYM----RVGEQLMEVLQlhKKMSKSEAFEESIRMLDavkmpearkrmr 173
Cdd:PRK11231 76 R----RLALLPQHHLTpegitvrelvayGRSPWLslwgRLSAEDNARVN--QAMEQTRINHLADRRLT------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 174 myphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMY 253
Cdd:PRK11231 138 ----DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLA 212
|
250 260 270
....*....|....*....|....*....|....*
gi 899869912 254 AGRTMEYGQARDVFyhpshpySIGLLNAVPRLDAE 288
Cdd:PRK11231 213 NGHVMAQGTPEEVM-------TPGLLRTVFDVEAE 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-272 |
3.03e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.30 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 47 TAVNALNFDLRAGETLGIVGESGSGKSQTAFAL--MGLLASNGRIGGSAKFNGREILNLPEKQLNRLRaeeISMIFQDPm 124
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRR---VGMLFQRP- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 tslNPY-MRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARK-RMRMYPHEFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:PRK14271 111 ---NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 203 DEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSH 272
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
30-261 |
3.24e-19 |
|
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: 84.50 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTfstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLlaSNGRI-GGSAKFNGREILNLPEKQl 108
Cdd:cd03217 1 LEIKDLHVS----VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVtEGEILFKGEDITDLPPEE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nrlRAEE-ISMIFQDPMT----SLNPYMR-VGEQlmevlqlhkkmskseafeesirmldavkmpearkrmrmypheFSGG 182
Cdd:cd03217 74 ---RARLgIFLAFQYPPEipgvKNADFLRyVNEG------------------------------------------FSGG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI-CNKVLVMYAGRTMEYG 261
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
26-239 |
3.79e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 88.19 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 26 QNVLLDVKDLTVTFstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrIGGSAKFNGREILNLPE 105
Cdd:TIGR02868 331 GKPTLELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP---LQGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 KQLNRLraeeISMIFQDPM---TSLNPYMRVG------EQLMEVLqlhkkmskseafeESIRMLDAVKMPEARKRMRMYP 176
Cdd:TIGR02868 405 DEVRRR----VSVCAQDAHlfdTTVRENLRLArpdatdEELWAAL-------------ERVGLADWLRALPDGLDTVLGE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 177 H--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDL 239
Cdd:TIGR02868 468 GgaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
42-261 |
4.18e-19 |
|
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: 84.85 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 42 PDGDVTAVNaLNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRIggsaKFNGREILNLPEKQLNRlraeEISMIF 120
Cdd:cd03252 12 PDGPVILDN-ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRV----LVDGHDLALADPAWLRR----QVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 121 QDPmTSLNPYMRvgeqlmEVLQLHKKMSKSEAFEESIRMLDA----VKMPEARKRM-RMYPHEFSGGMRQRVMIAMALLC 195
Cdd:cd03252 83 QEN-VLFNRSIR------DNIALADPGMSMERVIEAAKLAGAhdfiSELPEGYDTIvGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 899869912 196 RPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYG 261
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
47-270 |
4.47e-19 |
|
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: 84.90 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 47 TAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQLNRL----RAEEISmIFQ 121
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKI----LLDGQDITKLPMHKRARLgigyLPQEAS-IFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 122 DpmtslnpyMRVGEQLMEVLQLHKKmSKSEAFEESIRMLDAVKMPEARKRMRMYpheFSGGMRQRVMIAMALLCRPKLLI 201
Cdd:cd03218 89 K--------LTVEENILAVLEIRGL-SKKEREEKLEELLEEFHITHLRKSKASS---LSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 202 ADEPTTALDVTVQAQIMTLLNELKrefNTAI-IMIT-HDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHP 270
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILK---DRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
48-239 |
1.30e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.98 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 48 AVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLA-----SNGRIggsakfngreilNLPEKQLNRLRAEEiSMIFQD 122
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKT----TLLNLIAgfvpyQHGSI------------TLDGKPVEGPGAER-GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 pmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRmrmYPHEFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:PRK11248 79 --EGLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 899869912 203 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 239
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
29-266 |
1.36e-18 |
|
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: 83.49 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQ 107
Cdd:COG0410 3 MLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLpPRSGSI----RFDGEDITGLPPHR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 LNRLRaeeISM------IFqdpmtslnPYMRVGEQLMEVLQLHKKMSKSEAFEEsiRMLDAVkmPEARKRMRMYPHEFSG 181
Cdd:COG0410 75 IARLG---IGYvpegrrIF--------PSLTVEENLLLGAYARRDRAEVRADLE--RVYELF--PRLKERRRQRAGTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 182 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
....*
gi 899869912 262 QARDV 266
Cdd:COG0410 219 TAAEL 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
29-250 |
1.44e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.62 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIGGSAKFngrEILNLPEKq 107
Cdd:PRK09544 4 LVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNGKL---RIGYVPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 lnrlraeeismIFQDPMTSLNpymrvgeqLMEVLQLHKKMSKSEafeesirMLDAVKMPEARKRMRMYPHEFSGGMRQRV 187
Cdd:PRK09544 76 -----------LYLDTTLPLT--------VNRFLRLRPGTKKED-------ILPALKRVQAGHLIDAPMQKLSGGETQRV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVL 250
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
54-252 |
1.45e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 83.36 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 54 FDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRI---GGSAKFNGREILNLPEKQlnrlraeEISMIFqdPMTSLNP 129
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVkvaGASPGKGWRHIGYVPQRH-------EFAWDF--PISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 130 YMRVGEQLMEVLqlhkKMSKSEAFEESIRMLDAVKMPEARKRmrmyP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 208
Cdd:TIGR03771 72 VMSGRTGHIGWL----RRPCVADFAAVRDALRRVGLTELADR----PvGELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 899869912 209 LDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL 186
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
37-261 |
3.20e-18 |
|
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: 82.27 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQLNRLraee 115
Cdd:cd03254 8 VNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQI----LIDGIDIRDISRKSLRSM---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ISMIFQDpmtslnPYMRVGEqLMEVLqlhkKMSKSEAFEES-IRMLDAVKM-PEARKRMRMYPHE-------FSGGMRQR 186
Cdd:cd03254 79 IGVVLQD------TFLFSGT-IMENI----RLGRPNATDEEvIEAAKEAGAhDFIMKLPNGYDTVlgenggnLSQGERQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDV----TVQAQIMTLLNelkrefNTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYG 261
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTetekLIQEALEKLMK------GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
45-267 |
4.34e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 45 DVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGrEILNLPEKQLNRLRaEEISMIFQDPM 124
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQK---GAVLWQG-KPLDYSKRGLLALR-QQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 TSLNpYMRVGEQLMEVLqlhKKMSKSEAfEESIRMLDAVKMPEArKRMRMYPHE-FSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:PRK13638 88 QQIF-YTDIDSDIAFSL---RNLGVPEA-EITRRVDEALTLVDA-QHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
37-272 |
5.05e-18 |
|
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: 85.15 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLA-----SNGRIggsaKFNGREILNLpekQLNRL 111
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPrfyepDSGQI----LLDGHDLADY---TLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 112 RAEeISMIFQDPM----TSLN--PYMRVGEQLMEvlQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMyphefSGGMRQ 185
Cdd:TIGR02203 405 RRQ-VALVSQDVVlfndTIANniAYGRTEQADRA--EIERALAAAYAQDFVDKLPLGLDTPIGENGVLL-----SGGQRQ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCNKVLVMYAGRTMEYGQARD 265
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
....*..
gi 899869912 266 VFYHPSH 272
Cdd:TIGR02203 554 LLARNGL 560
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-267 |
6.00e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 82.05 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLasNGRI----GGSAKFNGReiln 102
Cdd:COG1119 1 DPLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLI--TGDLpptyGNDVRLFGE---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 103 lpekqlnRLRAEEI----SMI-FQDPmtSLNPYMRVGEQLMEV--------LQLHKKMSKSEAfEESIRMLDAVKMpeAR 169
Cdd:COG1119 67 -------RRGGEDVwelrKRIgLVSP--ALQLRFPRDETVLDVvlsgffdsIGLYREPTDEQR-ERARELLELLGL--AH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 170 KRMRMYpHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG-VVAGIcNK 248
Cdd:COG1119 135 LADRPF-GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-TH 212
|
250
....*....|....*....
gi 899869912 249 VLVMYAGRTMEYGQARDVF 267
Cdd:COG1119 213 VLLLKDGRVVAAGPKEEVL 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-270 |
1.45e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 34 DLTVTFSTPDGDVTAvnalnfdlragetlgIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGReILNLPEKQLNrLR 112
Cdd:PRK11144 14 CLTVNLTLPAQGITA---------------IFGRSGAGKTSLINAISGLTrPQKGRI----VLNGR-VLFDAEKGIC-LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 113 AEE--ISMIFQDpmTSLNPYMRV-GeqlmevlQLHKKMSKS--EAFEESIRMLDAVKMpearkrMRMYPHEFSGGMRQRV 187
Cdd:PRK11144 73 PEKrrIGYVFQD--ARLFPHYKVrG-------NLRYGMAKSmvAQFDKIVALLGIEPL------LDRYPGSLSGGEKQRV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK11144 138 AIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVW 217
|
...
gi 899869912 268 YHP 270
Cdd:PRK11144 218 ASS 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-266 |
1.46e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.19 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 12 QSALLEQNAQLEQNQNVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIg 90
Cdd:PRK13536 24 QGISEAKASIPGSMSTVAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 91 gsakfngrEILNLPEKQLNRLRAEEISMIFQdpMTSLNPYMRVGEQLMeVLQLHKKMSKSEaFEESIRMLDAVKMPEARK 170
Cdd:PRK13536 99 --------TVLGVPVPARARLARARIGVVPQ--FDNLDLEFTVRENLL-VFGRYFGMSTRE-IEAVIPSLLEFARLESKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 171 RMRMypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVL 250
Cdd:PRK13536 167 DARV--SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLC 243
|
250
....*....|....*.
gi 899869912 251 VMYAGRTMEYGQARDV 266
Cdd:PRK13536 244 VLEAGRKIAEGRPHAL 259
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-262 |
1.53e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 8 SAVQQSALLEQ-------NAQLEQNQNVLLDVKDltVTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALM 80
Cdd:PRK11160 310 SARRINEITEQkpevtfpTTSTAAADQVSLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 81 GLL-----ASNGRIggsaKFNGREILNLPEKQLNRLraeeISMIFQdpmtslnpymRV---GEQLMEVLQLHKKMSKSEA 152
Cdd:PRK11160 384 QLLtrawdPQQGEI----LLNGQPIADYSEAALRQA----ISVVSQ----------RVhlfSATLRDNLLLAAPNASDEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 153 FEESIRMLDAVKMPEARKRMRMYPHE----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRef 228
Cdd:PRK11160 446 LIEVLQQVGLEKLLEDDKGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-- 523
|
250 260 270
....*....|....*....|....*....|....
gi 899869912 229 NTAIIMITHDLGVVAGIcNKVLVMYAGRTMEYGQ 262
Cdd:PRK11160 524 NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
53-256 |
1.85e-17 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 79.91 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 53 NFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrIGGSAKFNGREILNLPEKQlnrlraEEISMIFQDpmTSLNPYMR 132
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP---ASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 133 VGEQLmeVLQLHKKMsKSEAFEESiRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 212
Cdd:TIGR01277 87 VRQNI--GLGLHPGL-KLNAEQQE-KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 899869912 213 VQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:TIGR01277 163 LREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
56-257 |
2.40e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 56 LRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKFNGREIlnlpEKQLNRLRAeeiSMIFQDPMtsLNPYMRVGE 135
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPI----DAKEMRAIS---AYVQQDDL--FIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 136 QLM--EVLQLHKKMSKS---EAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 210
Cdd:TIGR00955 119 HLMfqAHLRMPRRVTKKekrERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 899869912 211 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRT 257
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRV 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
37-271 |
2.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGdVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNgriGGSAKFNGREILNLPEKQLNRlraEEI 116
Cdd:PRK13644 7 VSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ---KGKVLVSGIDTGDFSKLQGIR---KLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 117 SMIFQDPMTSLnpymrVGEQLMEVLQLHKK---MSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMAL 193
Cdd:PRK13644 80 GIVFQNPETQF-----VGRTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHRS---PKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 194 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAgICNKVLVMYAGRTMEYGQARDVFYHPS 271
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
32-266 |
3.89e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFS--TPDgDVTAVNALNFDLRAGETLGIVGESGSGKsqTAF-----ALmgLLASNGRI-------------GG 91
Cdd:PRK13651 5 VKNIVKIFNkkLPT-ELKALDNVSVEINQGEFIAIIGQTGSGK--TTFiehlnAL--LLPDTGTIewifkdeknkkktKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 92 SAKFNGREILNLPE----KQLNRLRaEEISMIFQdpmtsLNPYmrvgeQLMEvlQLHKK----------MSKSEAFEESI 157
Cdd:PRK13651 80 KEKVLEKLVIQKTRfkkiKKIKEIR-RRVGVVFQ-----FAEY-----QLFE--QTIEKdiifgpvsmgVSKEEAKKRAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 158 RMLDAVKMPEARkrMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITH 237
Cdd:PRK13651 147 KYIELVGLDESY--LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTH 223
|
250 260
....*....|....*....|....*....
gi 899869912 238 DLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:PRK13651 224 DLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-256 |
4.02e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.08 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFSTPDGDVTavnalnFDLRAGETLGIVGESGSGKSQTAFALMGLlasNGRIGGSAKFNGREILN-LPE 105
Cdd:PRK10982 248 EVILEVRNLTSLRQPSIRDVS------FDLHKGEILGIAGLVGAKRTDIVETLFGI---REKSAGTITLHGKKINNhNAN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 KQLNR---LRAEE---------ISMIFQDPMTSLNPYM-RVGeqlmevLQLHKKMSKSEAFeesirMLDA--VKMPEARK 170
Cdd:PRK10982 319 EAINHgfaLVTEErrstgiyayLDIGFNSLISNIRNYKnKVG------LLDNSRMKSDTQW-----VIDSmrVKTPGHRT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 171 RMrmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVL 250
Cdd:PRK10982 388 QI----GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRIL 462
|
....*.
gi 899869912 251 VMYAGR 256
Cdd:PRK10982 463 VMSNGL 468
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
43-261 |
4.84e-17 |
|
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: 78.73 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 43 DGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLA-----SNGRIggsaKFNGReilnlpekqlnrlraeeIS 117
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLLAgiyppDSGTV----TVRGR-----------------VS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 118 MIFqDPMTSLNPYMRVGEQLMEVLQLHKkMSKSE--AFEESIRML----DAVKMPearkrMRMYphefSGGMRQRVMIAM 191
Cdd:cd03220 87 SLL-GLGGGFNPELTGRENIYLNGRLLG-LSRKEidEKIDEIIEFselgDFIDLP-----VKTY----SSGMKARLAFAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 192 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYG 261
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-285 |
6.45e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.46 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFStpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQL 108
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS---GSVLIRGEPITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLraeeISMIFQDPMTSLnpYMRVGEQLMEV----LQLHKKMSKSEAfEESIRMLDavkMPEARKRMrmyPHEFSGGMR 184
Cdd:PRK13652 77 RKF----VGLVFQNPDDQI--FSPTVEQDIAFgpinLGLDEETVAHRV-SSALHMLG---LEELRDRV---PHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 185 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQAR 264
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
250 260
....*....|....*....|..
gi 899869912 265 DVFYHPSHPYSIGL-LNAVPRL 285
Cdd:PRK13652 224 EIFLQPDLLARVHLdLPSLPKL 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
53-256 |
8.45e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.47 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 53 NFDLRAGETLGIVGESGSGKSqTAFALM-GLLASNGrigGSAKFNGREILNLPEKQlnrlraEEISMIFQDpmTSLNPYM 131
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIaGFLTPAS---GSLTLNGQDHTTTPPSR------RPVSMLFQE--NNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 132 RVGEQLmeVLQLHKKMSKSEAFEESIR-MLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 210
Cdd:PRK10771 87 TVAQNI--GLGLNPGLKLNAAQREKLHaIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 899869912 211 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-266 |
8.59e-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: 81.39 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA---SNGRI----------------- 89
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyepTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 90 ---------GGSAKFNGREILNLPEKQLNRLRaEEISMIFQDPMtSLNPYMRVGEQLMEVLQlHKKMSKSEAFEESIRML 160
Cdd:TIGR03269 77 kvgepcpvcGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 161 DAVKMPEarkRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG 240
Cdd:TIGR03269 154 EMVQLSH---RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 899869912 241 VVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
29-263 |
9.53e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.53 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNgRIGGSAKFNGREILNLPEKQL 108
Cdd:CHL00131 7 ILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYK-ILEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLraeEISMIFQDPMTSlnpymrVGEQLMEVLQL-----HKKMSKSE----AFEESIR-MLDAVKMpEARKRMRMYPHE 178
Cdd:CHL00131 82 AHL---GIFLAFQYPIEI------PGVSNADFLRLaynskRKFQGLPEldplEFLEIINeKLKLVGM-DPSFLSRNVNEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 FSGGMRQRVMI-AMALLcRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGIC-NKVLVMYAGR 256
Cdd:CHL00131 152 FSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKpDYVHVMQNGK 229
|
....*..
gi 899869912 257 TMEYGQA 263
Cdd:CHL00131 230 IIKTGDA 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-265 |
9.88e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 9.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 25 NQNVLLDVKDLTvtfstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGllaSNGRIGGSAKFNGREILnlP 104
Cdd:PRK09700 261 AHETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDKRAGGEIRLNGKDIS--P 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 EKQLNRLRaEEISMIFQD-------PMTSLNPYMRVGEQLME------VLQLHKKMSKSEAfeESIRMLDAVKMPEARKR 171
Cdd:PRK09700 330 RSPLDAVK-KGMAYITESrrdngffPNFSIAQNMAISRSLKDggykgaMGLFHEVDEQRTA--ENQRELLALKCHSVNQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 172 MRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLV 251
Cdd:PRK09700 407 IT----ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAV 481
|
250
....*....|....
gi 899869912 252 MYAGRTMEYGQARD 265
Cdd:PRK09700 482 FCEGRLTQILTNRD 495
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
37-266 |
1.10e-16 |
|
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: 80.85 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrIGGSAKFNGREILNLPEKQLNRLRAeei 116
Cdd:TIGR01842 322 VTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP---TSGSVRLDGADLKQWDRETFGKHIG--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 117 smifqdpmtslnpYMRVGEQLMEVlQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEF-----------SGGMRQ 185
Cdd:TIGR01842 396 -------------YLPQDVELFPG-TVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYdtvigpggatlSGGQRQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 186 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGIcNKVLVMYAGRTMEYGQARD 265
Cdd:TIGR01842 462 RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGCV-DKILVLQDGRIARFGERDE 539
|
.
gi 899869912 266 V 266
Cdd:TIGR01842 540 V 540
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
51-256 |
1.90e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 77.15 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 51 ALNFDLR--AGETLGIVGESGSGKSQTAFALMG-LLASNGRIggsaKFNGREILNLPEKqlnrlrAEEISMIFQDpmTSL 127
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRV----LINGVDVTAAPPA------DRPVSMLFQE--NNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 128 NPYMRVgEQ---LMEVLQLHKKMSKSEAFEESIRmldavKMPEARKRMRMyPHEFSGGMRQRVMIAMALLCRPKLLIADE 204
Cdd:cd03298 82 FAHLTV-EQnvgLGLSPGLKLTAEDRQAIEVALA-----RVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 899869912 205 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
44-243 |
1.95e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngRIGGSAKFNGREILNLPEK-QLNR---LRAEE-ISM 118
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP--TSGTVRRAGGARVAYVPQRsEVPDslpLTVRDlVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 119 IFQDPMTSLNPYMRvgeqlmevlqlhkkmsksEAFEESIRMLDAVKMPEARKRMRmypHEFSGGMRQRVMIAMALLCRPK 198
Cdd:NF040873 81 GRWARRGLWRRLTR------------------DDRAAVDDALERVGLADLAGRQL---GELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 899869912 199 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVA 243
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
52-266 |
3.98e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIggsaKFNGREILNLPEKQLNRLRA---EEISMIFqdpmtsln 128
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSI----QFAGQPLEAWSAAELARHRAylsQQQTPPF-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 129 pymrvgeqLMEV---LQLHKKMSKSEAFEESI--RMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALL-----CRP- 197
Cdd:PRK03695 83 --------AMPVfqyLTLHQPDKTRTEAVASAlnEVAEALGLDDKLGRS---VNQLSGGEWQRVRLAAVVLqvwpdINPa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 198 -KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:PRK03695 152 gQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-256 |
7.93e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.29 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVtFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGllASNGR-IGGSAKFNGREI--LNL 103
Cdd:NF040905 255 EVVFEVKNWTV-YHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGRnISGTVFKDGKEVdvSTV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 PE-------------KQLNRLRAEEISmiFQDPMTSLNPYMRVGeqlmeVLQLHKKMSKSEAFeesirmldavkmpeaRK 170
Cdd:NF040905 332 SDaidaglayvtedrKGYGLNLIDDIK--RNITLANLGKVSRRG-----VIDENEEIKVAEEY---------------RK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 171 RMRMYPH-------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVA 243
Cdd:NF040905 390 KMNIKTPsvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELL 468
|
250
....*....|...
gi 899869912 244 GICNKVLVMYAGR 256
Cdd:NF040905 469 GMCDRIYVMNEGR 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
59-286 |
8.30e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 59 GETLGIVGESGSGKSQTAFALMGLLASNGrIGGSAKFNGREilnlPEKQLNRlraeEISMIFQDPMtsLNPYMRVGEQLM 138
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNN-FTGTILANNRK----PTKQILK----RTGFVTQDDI--LYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 139 --EVLQLHKKMSKSE---AFEESIRMLDAVKMpEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTV 213
Cdd:PLN03211 163 fcSLLRLPKSLTKQEkilVAESVISELGLTKC-ENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 214 QAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARD-------VFYHPSHP-----YSIGLLNA 281
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDamayfesVGFSPSFPmnpadFLLDLANG 321
|
....*
gi 899869912 282 VPRLD 286
Cdd:PLN03211 322 VCQTD 326
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
30-270 |
9.66e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.45 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPekqLN 109
Cdd:COG1137 4 LEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS---GRIFLDGEDITHLP---MH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RlRA--------EEISmIFQDpMTslnpymrVGEQLMEVLQLHKKmSKSEAFEESIRMLDAVKMPEARKRMRMYpheFSG 181
Cdd:COG1137 74 K-RArlgigylpQEAS-IFRK-LT-------VEDNILAVLELRKL-SKKEREERLEELLEEFGITHLRKSKAYS---LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 182 GMRQRVMIAMALLCRPKLLIADEPTTALD-VTVqAQIMTLLNELKrEFNTAIImIT-HD----LgvvaGICNKVLVMYAG 255
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVL-ITdHNvretL----GICDRAYIISEG 212
|
250
....*....|....*
gi 899869912 256 RTMEYGQARDVFYHP 270
Cdd:COG1137 213 KVLAEGTPEEILNNP 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-259 |
9.79e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.91 E-value: 9.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAS---NGRIGGSAKFNGREIlnlpe 105
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKS----TLMKVLSGvypHGSYEGEILFDGEVC----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 kQLNRLRAEE---ISMIFQDpmTSLNPYMRVGEQLM---EVLQlHKKMSKSEAFEESIRMLDAVKMPEArkrmrmyPHEF 179
Cdd:NF040905 68 -RFKDIRDSEalgIVIIHQE--LALIPYLSIAENIFlgnERAK-RGVIDWNETNRRARELLAKVGLDES-------PDTL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 SG----GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICNKVLVMYAG 255
Cdd:NF040905 137 VTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDG 215
|
....
gi 899869912 256 RTME 259
Cdd:NF040905 216 RTIE 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
44-266 |
1.03e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.77 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREIlnlPEKQlnRLRAEEISMIFQdp 123
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA---GSISLCGEPV---PSRA--RHARQRVGVVPQ-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 MTSLNPYMRVGEQLMeVLQLHKKMSKSEAFEESIRMLDAVKMpEARKRMRMypHEFSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:PRK13537 88 FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKL-ENKADAKV--GELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
48-269 |
1.15e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 48 AVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPE-KQLNRLRaEEISMIFQDPMTs 126
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ---GSVRVDDTLITSTSKnKDIKQIR-KKVGLVFQFPES- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 127 lnpymrvgeQLMEVLQLHKKMSKSEAFEESIRmlDAVKMpeARKRMRMY----------PHEFSGGMRQRVMIAMALLCR 196
Cdd:PRK13649 97 ---------QLFEETVLKDVAFGPQNFGVSQE--EAEAL--AREKLALVgiseslfeknPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 197 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYH 269
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-267 |
1.23e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFSTPDgdvTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIGgsakfngreILNLPEKQLNR 110
Cdd:PRK15056 9 VNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVrLASGKIS---------ILGQPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 111 L-------RAEEISMIFQ---DPMTSLNPYMRVGeqLMEVLQLHKKMSKSEAfeesirmLDAVKMPEARKRMrmyPHEFS 180
Cdd:PRK15056 77 KnlvayvpQSEEVDWSFPvlvEDVVMMGRYGHMG--WLRRAKKRDRQIVTAA-------LARVDMVEFRHRQ---IGELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 181 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICNKVlVMYAGRTMEY 260
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYT-VMVKGTVLAS 222
|
....*..
gi 899869912 261 GQARDVF 267
Cdd:PRK15056 223 GPTETTF 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
37-261 |
1.27e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.75 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAfalmGLLAsngriggsaKF---NGREIL----NLPEKQLN 109
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA----NLLT---------RFydiDEGEILldghDLRDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRaEEISMI------FQDPMTSLNPYMRvgeqlmevlqlHKKMSKsEAFEESIRMLDAV----KMPEARKRMrmyPHE- 178
Cdd:PRK11176 414 SLR-NQVALVsqnvhlFNDTIANNIAYAR-----------TEQYSR-EQIEEAARMAYAMdfinKMDNGLDTV---IGEn 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 ---FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCNKVLVMYAG 255
Cdd:PRK11176 478 gvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDG 554
|
....*.
gi 899869912 256 RTMEYG 261
Cdd:PRK11176 555 EIVERG 560
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-272 |
2.62e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 25 NQNVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQT--AFALMGLLASNGRIGGSAKFNGREiLN 102
Cdd:PRK14243 6 GTETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrCFNRLNDLIPGFRVEGKVTFHGKN-LY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 103 LPEKQLNRLRaEEISMIFQDPmtslNPYMR-VGEQLMEVLQLHK-KMSKSEAFEESIRmlDAVKMPEARKRMRMYPHEFS 180
Cdd:PRK14243 81 APDVDPVEVR-RRIGMVFQKP----NPFPKsIYDNIAYGARINGyKGDMDELVERSLR--QAALWDEVKDKLKQSGLSLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 181 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICNKVLVMYA------ 254
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVeltegg 231
|
250 260
....*....|....*....|.
gi 899869912 255 ---GRTMEYGQARDVFYHPSH 272
Cdd:PRK14243 232 gryGYLVEFDRTEKIFNSPQQ 252
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
37-261 |
8.21e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.53 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPD-GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLNRlraeE 115
Cdd:TIGR00958 484 VSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG---GQVLLDGVPLVQYDHHYLHR----Q 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ISMIFQDPMTslnpYMR-VGEQLMEVLQlhkkmskseaFEESIRMLDAVKMPEARKRMRMYPHEF-----------SGGM 183
Cdd:TIGR00958 557 VALVGQEPVL----FSGsVRENIAYGLT----------DTPDEEIMAAAKAANAHDFIMEFPNGYdtevgekgsqlSGGQ 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 184 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAqimtLLNELKREFNTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYG 261
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
44-279 |
1.31e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.91 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLASNGRIGGSAKFNGREILN-LPEKQlnrlraEEISMIFQD 122
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGDLFIGEKRMNdVPPAE------RGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 pmTSLNPYMRVGEQLMEVLQLhKKMSKSEA---FEESIRMLDAVKMPEARkrmrmyPHEFSGGMRQRVMIAMALLCRPKL 199
Cdd:PRK11000 84 --YALYPHLSVAENMSFGLKL-AGAKKEEInqrVNQVAEVLQLAHLLDRK------PKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 200 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYHPSHPYSIGLL 279
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-238 |
2.76e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTafaLMGLLAsnGRI---GGSAKFNGREilnlpekql 108
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS-T---LLKILA--GELepdSGEVSIPKGL--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nrlraeEISMIFQDPmtSLNPYMRVGEQLM----EVLQLHKKMSK-----SEAFEESIRM-------------------- 159
Cdd:COG0488 62 ------RIGYLPQEP--PLDDDLTVLDTVLdgdaELRALEAELEEleaklAEPDEDLERLaelqeefealggweaearae 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 160 --LDAVKMPEARKRMRMypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtVQAqIMTLLNELKReFNTAIIMITH 237
Cdd:COG0488 134 eiLSGLGFPEEDLDRPV--SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLKN-YPGTVLVVSH 207
|
.
gi 899869912 238 D 238
Cdd:COG0488 208 D 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
52-267 |
2.95e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.07 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLNRLRAEEISMIFQDPMTSLnpym 131
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTE---GKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 132 rVGEQLMEVLQLHKK---MSKSEAFEESIRMLDAVKMpeARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 208
Cdd:PRK13643 98 -FEETVLKDVAFGPQnfgIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 209 LDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
27-260 |
4.05e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAsnGRI---GGSAKFnGREIlnl 103
Cdd:COG0488 313 KKVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLLA--GELepdSGTVKL-GETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 pekqlnrlraeEISMIFQDpMTSLNPYMRVGEQLMEVlqlhkkmsKSEAFEESIR-----ML---DavkmpEARKRMRmy 175
Cdd:COG0488 379 -----------KIGYFDQH-QEELDPDKTVLDELRDG--------APGGTEQEVRgylgrFLfsgD-----DAFKPVG-- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 176 phEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHDLGVVAGICNKVLVMYA 254
Cdd:COG0488 432 --VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-----LEEALDDFPGTVLLVSHDRYFLDRVATRILEFED 504
|
....*.
gi 899869912 255 GRTMEY 260
Cdd:COG0488 505 GGVREY 510
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-266 |
4.82e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 23 EQNQNVLLDVKDLTVTfstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGllasnGRI---GGSAKFNGRE 99
Cdd:PRK11831 1 EQSVANLVDMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKT-TLLRLIG-----GQIapdHGEILFDGEN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 100 ILNLPEKQLNRLRaEEISMIFQDP--MTSLNPYMRVGEQLMEVLQLHKKMSKSeafeeSIRM-LDAVKMPEARKRMrmyP 176
Cdd:PRK11831 71 IPAMSRSRLYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLREHTQLPAPLLHS-----TVMMkLEAVGLRGAAKLM---P 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 177 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKK 221
|
250
....*....|
gi 899869912 257 TMEYGQARDV 266
Cdd:PRK11831 222 IVAHGSAQAL 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
175-252 |
5.56e-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: 68.24 E-value: 5.56e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 175 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtLLNELKrEFNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:cd03221 67 YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALK-EYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
47-267 |
5.64e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 47 TAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGREILNLPekqLNRLRAEEISMIFQDPmtS 126
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP---RDAGNIIIDDEDISLLP---LHARARRGIGYLPQEA--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 127 LNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 206
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM---GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 207 TALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-266 |
8.71e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 8.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNgriGGSAKFNGREILNLPEKql 108
Cdd:PRK09700 5 YISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNINYNKLDHK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nrLRAE-EISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKMSkseafeeSIRMLDAVKMPEARKRM------RMYPHEFSG 181
Cdd:PRK09700 76 --LAAQlGIGIIYQE--LSVIDELTVLENLYIGRHLTKKVC-------GVNIIDWREMRVRAAMMllrvglKVDLDEKVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 182 GM----RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGRT 257
Cdd:PRK09700 145 NLsishKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSS 223
|
....*....
gi 899869912 258 MEYGQARDV 266
Cdd:PRK09700 224 VCSGMVSDV 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
24-238 |
1.41e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 24 QNQNVLLDVKDltVTFSTpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLLASNGRigGSAKFNGREILNL 103
Cdd:PRK10247 2 QENSPLLQLQN--VGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISPTS--GTLLFEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 104 PEKQLNrlraEEISMIFQDPMTslnpymrVGEQLMEVL----QLHKKMSKSEAFeesIRMLDAVKMPEA--RKRMrmypH 177
Cdd:PRK10247 75 KPEIYR----QQVSYCAQTPTL-------FGDTVYDNLifpwQIRNQQPDPAIF---LDDLERFALPDTilTKNI----A 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 178 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 238
Cdd:PRK10247 137 ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-256 |
1.51e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 69.04 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFSTPD-GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQLNR 110
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG---GQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 111 lraeEISMIFQDPMT---SLNPYMRVGEQLMEVLQLHKKMSKSEAfEESIRMLDAVKMPEARKRmrmyPHEFSGGMRQRV 187
Cdd:cd03248 89 ----KVSLVGQEPVLfarSLQDNIAYGLQSCSFECVKEAAQKAHA-HSFISELASGYDTEVGEK----GSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCNKVLVMYAGR 256
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
30-270 |
5.18e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.10 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLASNGRI-GGSAKFNGREILNLPEKQL 108
Cdd:PRK11650 4 LKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMVAGLERItSGEIWIGGRVVNELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NrlraeeISMIFQDpmTSLNPYMRVGEQLMEVLQLhKKMSKSEAFEesiRMLDAVKMPE-----ARKrmrmyPHEFSGGM 183
Cdd:PRK11650 77 D------IAMVFQN--YALYPHMSVRENMAYGLKI-RGMPKAEIEE---RVAEAARILElepllDRK-----PRELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 184 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQiMTL-LNELKREFNTAIIMITHD------LGvvagicNKVLVMYAGR 256
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGGV 212
|
250
....*....|....
gi 899869912 257 TMEYGQARDVFYHP 270
Cdd:PRK11650 213 AEQIGTPVEVYEKP 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
37-261 |
7.18e-13 |
|
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: 69.46 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPEKQLnrlRAEe 115
Cdd:COG5265 363 VSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRI----LIDGQDIRDVTQASL---RAA- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 116 ISMIFQDpmTSL-------N-PYMRVGeqlmevlqlhkkmskseAFEESIRmlDAVKMPEArkrmrmypHEF-------- 179
Cdd:COG5265 434 IGIVPQD--TVLfndtiayNiAYGRPD-----------------ASEEEVE--AAARAAQI--------HDFieslpdgy 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 -----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCNK 248
Cdd:COG5265 485 dtrvgerglklSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADE 561
|
250
....*....|...
gi 899869912 249 VLVMYAGRTMEYG 261
Cdd:COG5265 562 ILVLEAGRIVERG 574
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
49-261 |
8.55e-13 |
|
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: 66.52 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 49 VNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKFNGreilnLPEKQLNRLRAEEISMIFQDpmTSLN 128
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNG-----IPYKEFAEKYPGEIIYVSEE--DVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 129 PYMRVGEQLMEVLQLhkkmsKSEAFeesIRmldavkmpearkrmrmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 208
Cdd:cd03233 96 PTLTVRETLDFALRC-----KGNEF---VR-------------------GISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 899869912 209 LDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVA-GICNKVLVMYAGRTMEYG 261
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
44-266 |
8.70e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 8.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrIGGSAKFNGREILNLPEKQLNRlraeEISMIFQDP 123
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHIQHYASKEVAR----RIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 MTSLNpyMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:PRK10253 91 TTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
11-237 |
1.14e-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: 69.01 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 11 QQSALLEQNAQLEQNQNVlldVKDLTVTFSTPDGDVTaVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrig 90
Cdd:TIGR00954 434 RNSNLVPGRGIVEYQDNG---IKFENIPLVTPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV----- 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 91 gsakFNGReiLNLPEKQlnrlraeeisMIFQDPMtslNPYMRVG---EQL---MEVLQLHKK-MSKSEAfeesIRMLDAV 163
Cdd:TIGR00954 505 ----YGGR--LTKPAKG----------KLFYVPQ---RPYMTLGtlrDQIiypDSSEDMKRRgLSDKDL----EQILDNV 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 164 KMPEARKR------MRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITH 237
Cdd:TIGR00954 562 QLTHILEReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
31-266 |
1.51e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.65 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 31 DVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLL--ASNGRIggsaKFNGREILNLPEKQL 108
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISRLlpPDSGEV----LVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nrlrAEEISMIFQDPmtSLNPYMRVGEqlmevlqL--------HK-KMSKS--EAFEESIRMLDavkMPEARKRmrmYPH 177
Cdd:COG4604 74 ----AKRLAILRQEN--HINSRLTVRE-------LvafgrfpySKgRLTAEdrEIIDEAIAYLD---LEDLADR---YLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRT 257
Cdd:COG4604 135 ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
....*....
gi 899869912 258 MEYGQARDV 266
Cdd:COG4604 215 VAQGTPEEI 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
49-287 |
2.12e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.27 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 49 VNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrIGGSAKFNGREILNLPEKQLNRlraeEISMIFQDPM---- 124
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV---CGGEIRVNGREIGAYGLRELRR----QFSMIPQDPVlfdg 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 ---TSLNPYMRVGEQ----LMEVLQLHKKM-SKSEAFEEsiRMLDAvkmpearkrmrmyPHEFSGGMRQRVMIAMALLCR 196
Cdd:PTZ00243 1399 tvrQNVDPFLEASSAevwaALELVGLRERVaSESEGIDS--RVLEG-------------GSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 197 PKLLI-ADEPTT----ALDVTVQAQIMTLLNelkrefNTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQARDVFYHPS 271
Cdd:PTZ00243 1464 GSGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
250
....*....|....*.
gi 899869912 272 HPYSiGLLNAVPRLDA 287
Cdd:PTZ00243 1537 SIFH-SMVEALGRSEA 1551
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-256 |
2.74e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.12 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFStPDGDvTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREIlnlpEKQLNRL 111
Cdd:TIGR01257 931 VKNLVKIFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS---GTVLVGGKDI----ETNLDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 112 RaEEISMIFQDPMtsLNPYMRVGEQLMEVLQLhKKMSKSEAFEESIRMLDAVKMPEARKRMrmyPHEFSGGMRQRVMIAM 191
Cdd:TIGR01257 1002 R-QSLGMCPQHNI--LFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEE---AQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 192 ALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
52-268 |
5.53e-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: 67.28 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAfalMGLLASNGRIGGSAKFNGreiLNLPEKQLNRLRAEeISMIFQDPM------- 124
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG---LNIAKIGLHDLRFK-ITIIPQDPVlfsgslr 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 TSLNPYMRVGEQ----LMEVLQLHKKMSKSEAfeesirMLDAvKMPEARKRMrmyphefSGGMRQRVMIAMALLCRPKLL 200
Cdd:TIGR00957 1378 MNLDPFSQYSDEevwwALELAHLKTFVSALPD------KLDH-ECAEGGENL-------SVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 201 IADEPTTALDVT----VQAQIMTllnelkrEFNTAIIM-ITHDLGVVAGIcNKVLVMYAGRTMEYG------QARDVFY 268
Cdd:TIGR00957 1444 VLDEATAAVDLEtdnlIQSTIRT-------QFEDCTVLtIAHRLNTIMDY-TRVIVLDKGEVAEFGapsnllQQRGIFY 1514
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
37-266 |
5.96e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 37 VTFSTPDGdvTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGL--LASNGRI--------GGSAKFNGREILNLPEK 106
Cdd:PRK10575 17 VSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRhqPPSEGEIlldaqpleSWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 --QLNRLRAEEISMIFQDPMTSlnPYMRVGEQlmevlqlhkkmsKSEAFEESIRMLDAvkMPEARKRMrmypHEFSGGMR 184
Cdd:PRK10575 94 lpAAEGMTVRELVAIGRYPWHG--ALGRFGAA------------DREKVEEAISLVGL--KPLAHRLV----DSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 185 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQAR 264
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
..
gi 899869912 265 DV 266
Cdd:PRK10575 234 EL 235
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-261 |
6.85e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.81 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFStpdgDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLlASNGRIGGSAKFNGREILNL-PEKq 107
Cdd:PRK09580 1 MLSIKDLHVSVE----DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVTGGTVEFKGKDLLELsPED- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 lnrlRAEE-ISMIFQDPM------------TSLNPYMRVGEQlmEVLQlhkKMSKSEAFEESIRMLdavKMPEARkRMRM 174
Cdd:PRK09580 75 ----RAGEgIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPLD---RFDFQDLMEEKIALL---KMPEDL-LTRS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 175 YPHEFSGGMRQRVMI-AMALLcRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGI-CNKVLVM 252
Cdd:PRK09580 142 VNVGFSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVL 219
|
....*....
gi 899869912 253 YAGRTMEYG 261
Cdd:PRK09580 220 YQGRIVKSG 228
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
49-272 |
9.26e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 9.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 49 VNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL----ASNG-RIGGSAKFNGREILNLPEKQLNRLRA-----EEISM 118
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGaRVTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 119 IFQ-DPMTSLNPYMrvgeqlmevlqlHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEFSGGMRQRVMIAMAL---- 193
Cdd:PRK13547 97 AFSaREIVLLGRYP------------HARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 194 -----LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFy 268
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL- 243
|
....
gi 899869912 269 HPSH 272
Cdd:PRK13547 244 TPAH 247
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
38-262 |
9.32e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.89 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 38 TFSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLASNGRIG-GSAKFNGreiLNLPEKQLNRLRAEeI 116
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSeGDIRFHD---IPLTKLQLDSWRSR-L 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 117 SMIFQDPMTslnpymrVGEQLMEVLQLHKKMSKSEAFEESIRML----DAVKMP-----EARKRMRMypheFSGGMRQRV 187
Cdd:PRK10789 392 AVVSQTPFL-------FSDTVANNIALGRPDATQQEIEHVARLAsvhdDILRLPqgydtEVGERGVM----LSGGQKQRI 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQ 262
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
49-260 |
1.36e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 49 VNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREILNLPEKQLNRLraeeISMIFQDPMT-- 125
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRI----MIDDCDVAKFGLTDLRRV----LSIIPQSPVLfs 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 126 -----SLNPYMRVGE-QLMEVLQ-LHKKmsksEAFEESIRMLDAvKMPEARKrmrmyphEFSGGMRQRVMIAMALLCRPK 198
Cdd:PLN03232 1324 gtvrfNIDPFSEHNDaDLWEALErAHIK----DVIDRNPFGLDA-EVSEGGE-------NFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 199 LLIADEPTTALDVTVQAQIMTLLNElkrEFNT-AIIMITHDLGVVAGiCNKVLVMYAGRTMEY 260
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIRE---EFKScTMLVIAHRLNTIID-CDKILVLSSGQVLEY 1450
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
52-261 |
3.94e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREILNLpekQLNRLRaEEISMIFQDPMT----- 125
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRI----LIDGCDISKF---GLMDLR-KVLGIIPQAPVLfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 126 --SLNPYMRVGE-QLMEVLQ-LHKKmsksEAFEESIRMLDAvKMPEARKrmrmyphEFSGGMRQRVMIAMALLCRPKLLI 201
Cdd:PLN03130 1330 rfNLDPFNEHNDaDLWESLErAHLK----DVIRRNSLGLDA-EVSEAGE-------NFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 202 ADEPTTALDVTVQAQIMTLLNElkrEFNT-AIIMITHDLGVVAGiCNKVLVMYAGRTMEYG 261
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIRE---EFKScTMLIIAHRLNTIID-CDRILVLDAGRVVEFD 1454
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-256 |
4.54e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 33 KDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASngriGGSAKFNGREIlnlpekqlnrl 111
Cdd:NF033858 270 RGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLpAS----EGEAWLFGQPV----------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 112 raeeismifqDPmTSLNPYMRVGeqLMevlqlhkkmskSEAF----EESIR---MLDA--VKMPEARKRMRM-------- 174
Cdd:NF033858 331 ----------DA-GDIATRRRVG--YM-----------SQAFslygELTVRqnlELHArlFHLPAAEIAARVaemlerfd 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 175 ---YPHEFSG----GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICN 247
Cdd:NF033858 387 ladVADALPDslplGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMN-EAERCD 465
|
....*....
gi 899869912 248 KVLVMYAGR 256
Cdd:NF033858 466 RISLMHAGR 474
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
29-255 |
4.91e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTPDgdvtAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIGGSAKFNGREILNLPE--K 106
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRlaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLRAEeISMIFQdpmtSLNPYMRvgeqlMEVLQ--LHKKMSKSEAFEESIRMLDAVKMPEA-----RKRMRMYPHE- 178
Cdd:PRK09984 80 DIRKSRAN-TGYIFQ----QFNLVNR-----LSVLEnvLIGALGSTPFWRTCFSWFTREQKQRAlqaltRVGMVHFAHQr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 ---FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAG 255
Cdd:PRK09984 150 vstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
32-269 |
6.69e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.37 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTvtFSTPDGDV-TAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNG---RIGGSAKFNGreilnlpekq 107
Cdd:PRK13545 24 LKDLF--FRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKgtvDIKGSAALIA---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 108 lnrlraeeISMIFQDPMTslnpymrvGEQLMEVLQLHKKMSKSEAFEESIRMLDavkMPEARKRMRMYPHEFSGGMRQRV 187
Cdd:PRK13545 92 --------ISSGLNGQLT--------GIENIELKGLMMGLTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVF 267
Cdd:PRK13545 153 GFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV 231
|
..
gi 899869912 268 YH 269
Cdd:PRK13545 232 DH 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
46-256 |
8.56e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 46 VTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGL-LASNGRI---GGSAKF-NGREILNlpekqlnrlraEEISMIF 120
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSIlidGQEMRFaSTTAALA-----------AGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 121 QDpmTSLNPYMRVGEQLMeVLQLHKKM---SKSEAFEESIRMLDAVKM---PEARKRmrmyphEFSGGMRQRVMIAMALL 194
Cdd:PRK11288 86 QE--LHLVPEMTVAENLY-LGQLPHKGgivNRRLLNYEAREQLEHLGVdidPDTPLK------YLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 195 cRPKLLIA-DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:PRK11288 157 -RNARVIAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
52-237 |
9.09e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 52 LNFDLRAGETLGIVGESGSGKSQTAFALMGLlASNGRIGGSAKfngreilnLPEKQLNRlraeEISMIfqdpmtslnpym 131
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-LKGTPVAGCVD--------VPDNQFGR----EASLI------------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 132 rvgEQLmevlqlhkkmSKSEAFEESIRMLDAVKMPEA---RKRmrmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 208
Cdd:COG2401 104 ---DAI----------GRKGDFKDAVELLNAVGLSDAvlwLRR----FKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|
gi 899869912 209 LDVTVqAQIMTL-LNELKREFNTAIIMITH 237
Cdd:COG2401 167 LDRQT-AKRVARnLQKLARRAGITLVVATH 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
57-261 |
9.33e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 61.23 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 57 RAGETLGIVGESGSGKSQTAFALMGLLASN-GRIGGSAK-------FNGREILNLPEKqlnrLRAEEISMIFQDPMTSLN 128
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNlGKFDDPPDwdeildeFRGSELQNYFTK----LLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 129 PYMRVGEqlmeVLQLHKKMSKSEAFEESIRMLdavkmpEARKRMRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 208
Cdd:cd03236 100 PKAVKGK----VGELLKKKDERGKLDELVDQL------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 899869912 209 LDVTVQAQIMTLLNELKREFNtAIIMITHDLGVVAGICNKVLVMYaGRTMEYG 261
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY-GEPGAYG 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-242 |
1.83e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 24 QNQNVL---LDVKDLTVTF-STPDgdVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMG---------LLASNGRIG 90
Cdd:PTZ00265 1157 KNKNDIkgkIEIMDVNFRYiSRPN--VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhIVFKNEHTN 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 91 GSAKF---NGREILNLPEKQLNRLRAEE-----------------------------------ISMIFQDPM---TSLNP 129
Cdd:PTZ00265 1235 DMTNEqdyQGDEEQNVGMKNVNEFSLTKeggsgedstvfknsgkilldgvdicdynlkdlrnlFSIVSQEPMlfnMSIYE 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 130 YMRVGEQlMEVLQLHKKMSKSEAFEESIRML----DAVKMPearkrmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 205
Cdd:PTZ00265 1315 NIKFGKE-DATREDVKRACKFAAIDEFIESLpnkyDTNVGP--------YGKSLSGGQKQRIAIARALLREPKILLLDEA 1385
|
250 260 270
....*....|....*....|....*....|....*..
gi 899869912 206 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVV 242
Cdd:PTZ00265 1386 TSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
44-266 |
2.24e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.29 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFAlmgllasnGRIGGSAKfnGREILNLPEKQLNRlRAEEISMIFQDP 123
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP--------AHV*GPDA--GRRPWRF*TWCANR-RALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 MTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMyphEFSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDV 266
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
30-242 |
2.89e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 58.91 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTfstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngrIGGSAKFNGREIlnlpeKQLN 109
Cdd:TIGR01189 1 LAARNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP---DSGEVRWNGTPL-----AEQR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEEISMIFQDPmtSLNPYMRVGEQL---MEVLQLHKKMSkSEAFEEsIRMLDAVKMPearkrmrmyPHEFSGGMRQR 186
Cdd:TIGR01189 69 DEPHENILYLGHLP--GLKPELSALENLhfwAAIHGGAQRTI-EDALAA-VGLTGFEDLP---------AAQLSAGQQRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNE-LKRefNTAIIMITH-DLGVV 242
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLAR--GGIVLLTTHqDLGLV 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-242 |
2.98e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 10 VQQSALLEQNAQLEQNQNVL-LDVKDLTVTFSTPDgDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMGLLASNGR 88
Cdd:PTZ00265 362 INRKPLVENNDDGKKLKDIKkIQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDPTE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 89 igGSAKFNGREilNLPEKQLNRLRAEeISMIFQDPMTSLNP------YMRVGEQLMEVLQLHKKMSKSEAFEES------ 156
Cdd:PTZ00265 440 --GDIIINDSH--NLKDINLKWWRSK-IGVVSQDPLLFSNSiknnikYSLYSLKDLEALSNYYNEDGNDSQENKnkrnsc 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 157 -----------IRMLDAVKMPEARKRM-------------RMYPHEF-------------------SGGMRQRVMIAMAL 193
Cdd:PTZ00265 515 rakcagdlndmSNTTDSNELIEMRKNYqtikdsevvdvskKVLIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAI 594
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 899869912 194 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVV 242
Cdd:PTZ00265 595 IRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
53-256 |
1.03e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 53 NFDLRAGETLGIVGESGSGKSQtafaLMGLL-ASNGRIGGSAKFNGRE-------------ILNLPEKQlnrlRAEEISm 118
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSE----LMKLLyGATRRTAGQVYLDGKPidirsprdairagIMLCPEDR----KAEGII- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 119 ifqdPMTS----LNPYMRvGEQLMEVLQLHKKMSKSEAfEESIRMLdAVKMPEARKRMRmyphEFSGGMRQRVMIAMALL 194
Cdd:PRK11288 344 ----PVHSvadnINISAR-RHHLRAGCLINNRWEAENA-DRFIRSL-NIKTPSREQLIM----NLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 899869912 195 CRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-255 |
1.33e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 46 VTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGREIlnlpekQLNRLRAEE---ISMIFQD 122
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT---RDAGSILYLGKEV------TFNGPKSSQeagIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 pmtsLN--PYMRVGEQLM---EVLQ-----LHKKMskseaFEESIRMLDAVKMPEARKRMRmypHEFSGGMRQRVMIAMA 192
Cdd:PRK10762 88 ----LNliPQLTIAENIFlgrEFVNrfgriDWKKM-----YAEADKLLARLNLRFSSDKLV---GELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899869912 193 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAG 255
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
30-256 |
1.85e-09 |
|
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: 56.71 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFSTPDGDVTAV-NALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGRE--------I 100
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPGSIayvsqepwI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 101 LNlpekqlNRLRaEEIsmIFQDPMtslNPymrvgEQLMEVLqlhkkmsKSEAFEESIRMLDAVKMPEArkrmrmypHE-- 178
Cdd:cd03250 78 QN------GTIR-ENI--LFGKPF---DE-----ERYEKVI-------KACALEPDLEILPDGDLTEI--------GEkg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 --FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT--LLNELKRefNTAIIMITHDLGVVAgICNKVLVMYA 254
Cdd:cd03250 126 inLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLP-HADQIVVLDN 202
|
..
gi 899869912 255 GR 256
Cdd:cd03250 203 GR 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
49-276 |
3.29e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 56.84 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 49 VNALnfdLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREILNLPekqLNRLRAEeISMIFQDPMT-- 125
Cdd:cd03288 40 VKAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVdIFDGKI----VIDGIDISKLP---LHTLRSR-LSIILQDPILfs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 126 -----SLNPYMRVGE----QLMEVLQLhKKMSKSEAfeesiRMLDAVKMPEARKrmrmypheFSGGMRQRVMIAMALLCR 196
Cdd:cd03288 109 gsirfNLDPECKCTDdrlwEALEIAQL-KNMVKSLP-----GGLDAVVTEGGEN--------FSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 197 PKLLIADEPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQARDVFYHPSH 272
Cdd:cd03288 175 SSILIMDEATASIDMAteniLQKVVMTAFAD------RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDG 247
|
....
gi 899869912 273 PYSI 276
Cdd:cd03288 248 VFAS 251
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-242 |
3.43e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.96 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTfstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLAsngriGGSAKFNGREILN-LPEKQL 108
Cdd:cd03231 1 LEADELTCE----RDGRALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILA-----GLSPPLAGRVLLNgGPLDFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLRAEEISMIFQDP--MTSLNPymrvgeqlMEVLQLHKKMSKSEAFEESIrmldavkmpeARKRMRMYPH----EFSGG 182
Cdd:cd03231 68 RDSIARGLLYLGHAPgiKTTLSV--------LENLRFWHADHSDEQVEEAL----------ARVGLNGFEDrpvaQLSAG 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITH-DLGVV 242
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-HCARGGMVVLTTHqDLGLS 189
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
44-238 |
3.72e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 44 GDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAS-NGRIGGSakfNGREILNLPEKQLNRLRAEEismifqd 122
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPvSGEIGLA---KGIKLGYFAQHQLEFLRADE------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 123 pmTSLNPYMRVGEQLMEvlQLHKKMSKSEAFEEsirmlDAVKMPEARkrmrmypheFSGGMRQRVMIAMALLCRPKLLIA 202
Cdd:PRK10636 393 --SPLQHLARLAPQELE--QKLRDYLGGFGFQG-----DKVTEETRR---------FSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190
....*....|....*....|....*....|....*..
gi 899869912 203 DEPTTALDVTV-QAqimtlLNELKREFNTAIIMITHD 238
Cdd:PRK10636 455 DEPTNHLDLDMrQA-----LTEALIDFEGALVVVSHD 486
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
30-272 |
1.19e-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: 55.25 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFStpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIggsaKFNGREILNLPEKQLN 109
Cdd:cd03289 3 MTVKDLTAKYT--EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDI----QIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRA--EEISMIFQDPM-TSLNPYMRVGEQlmEVLQLHKKMSKSEAFEESIRMLDAVKMPEArkrmrmypHEFSGGMRQR 186
Cdd:cd03289 77 KAFGviPQKVFIFSGTFrKNLDPYGKWSDE--EIWKVAEEVGLKSVIEQFPGQLDFVLVDGG--------CVLSHGHKQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALD-VTVQaqimTLLNELKREFNT-AIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQAR 264
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDpITYQ----VIRKTLKQAFADcTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQ 221
|
....*...
gi 899869912 265 DVFYHPSH 272
Cdd:cd03289 222 KLLNEKSH 229
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
53-227 |
1.93e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 53 NFDLRAGETLGIVGESGSGKSQTAFALMGLLAsngRIGGSAKFNGREILNLPEKQLNRLRAEEismiFQDPMTSLnpyMR 132
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELP---LLSGERQSQFSHITRLSFEQLQKLVSDE----WQRNNTDM---LS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 133 VGEQ-----LMEVLQL-HKKMSKSEAFEESIR---MLDavkmpearkRMRMYpheFSGGMRQRVMIAMALLCRPKLLIAD 203
Cdd:PRK10938 93 PGEDdtgrtTAEIIQDeVKDPARCEQLAQQFGitaLLD---------RRFKY---LSTGETRKTLLCQALMSEPDLLILD 160
|
170 180
....*....|....*....|....
gi 899869912 204 EPTTALDVTVQAQIMTLLNELKRE 227
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQS 184
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
40-227 |
2.16e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 40 STPDGDVTAVNALNFDLRAGETLGIVGESGSGKSqtafALMGLLASNGRIG-GSAKFNGREILNLPEKQLNRlraEEISM 118
Cdd:PRK11614 12 SAHYGKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATsGRIVFDGKDITDWQTAKIMR---EAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 119 IFQDpmtslnpyMRVGEQLM--EVLQLHKKMSKSEAFEESIRMLDAVkMPEARKRMRMYPHEFSGGMRQRVMIAMALLCR 196
Cdd:PRK11614 85 VPEG--------RRVFSRMTveENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190
....*....|....*....|....*....|.
gi 899869912 197 PKLLIADEPTTALDVTVQAQIMTLLNELKRE 227
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
59-241 |
2.17e-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: 52.76 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 59 GETLGIVGESGSGKSQTAFALMGLLASNGriGGSAKFNGREILNLPEKQLNRLRAEEismifqdpmtslnpymrvgeqlm 138
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG--GGVIYIDGEDILEEVLDQLLLIIVGG----------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 139 evlqlhkkmskseafeesirmldavkmpearkrmrmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM 218
Cdd:smart00382 57 ------------------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180
....*....|....*....|....*...
gi 899869912 219 -----TLLNELKREFNTAIIMITHDLGV 241
Cdd:smart00382 101 lleelRLLLLLKSEKNLTVILTTNDEKD 128
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-255 |
2.22e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.79 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 25 NQNVLLDVKDLTVTFstPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNlp 104
Cdd:TIGR01257 1933 NKTDILRLNELTKVY--SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS---GDATVAGKSILT-- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 105 ekqlnrlraeEISMIFQDpMTSLNPYMRVGEQLM--EVLQLHKKMS--KSEAFEE----SIRMLDavkmpearkrMRMYP 176
Cdd:TIGR01257 2006 ----------NISDVHQN-MGYCPQFDAIDDLLTgrEHLYLYARLRgvPAEEIEKvanwSIQSLG----------LSLYA 2064
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 177 HE----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:TIGR01257 2065 DRlagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
|
...
gi 899869912 253 YAG 255
Cdd:TIGR01257 2144 VKG 2146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
54-238 |
3.41e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 54 FDLRAGETLGIVGESGSGKSqtafALMGLLAsngriggsakfngREILnLPEKQLNRLRAEEISMIFQDPMTSL--NPYM 131
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKS----TLMKILN-------------GEVL-LDDGRIIYEQDLIVARLQQDPPRNVegTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 132 RVGEQLMEVLQLHKK---MSKSEAFEESIRMLDAV-----------------KMPEARKRMRMYPH----EFSGGMRQRV 187
Cdd:PRK11147 86 FVAEGIEEQAEYLKRyhdISHLVETDPSEKNLNELaklqeqldhhnlwqlenRINEVLAQLGLDPDaalsSLSGGWLRKA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKrEFNTAIIMITHD 238
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLK-TFQGSIIFISHD 212
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
59-244 |
4.60e-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: 54.56 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 59 GETLGIVGESGSGKSqTAFALMGLLASNgrIGGSAKFN-GREILNLP-EKQLNRL-------------------RAEEIS 117
Cdd:TIGR03719 31 GAKIGVLGLNGAGKS-TLLRIMAGVDKD--FNGEARPQpGIKVGYLPqEPQLDPTktvrenveegvaeikdaldRFNEIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 118 MIFQDPMTSLNPYMRVGEQLMEVLQ---LHKKMSKSEafeesiRMLDAVKMPEARKRMRmyphEFSGGMRQRVMIAMALL 194
Cdd:TIGR03719 108 AKYAEPDADFDKLAAEQAELQEIIDaadAWDLDSQLE------IAMDALRCPPWDADVT----KLSGGERRRVALCRLLL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 899869912 195 CRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 244
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHDryfLDNVAG 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
179-260 |
8.42e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 179 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtVQAQIMtlLNELKREFNTAIIMITHDLGVVAGICNKVLVMYAGRTM 258
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIW--LEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLF 225
|
..
gi 899869912 259 EY 260
Cdd:PRK10636 226 EY 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-272 |
1.01e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.76 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFsTPDGDVTAVNaLNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGRIggsaKFNGREILNLPEKQLN 109
Cdd:TIGR01271 1218 MDVQGLTAKY-TEAGRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEI----QIDGVSWNSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 110 RLRAEEISMIFQDPMT---SLNPYMRVGEQlmEVLQLHKKMSKSEAFEESIRMLDAVKMPEArkrmrmypHEFSGGMRQR 186
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSGTfrkNLDPYEQWSDE--EIWKVAEEVGLKSVIEQFPDKLDFVLVDGG--------YVLSNGHKQL 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 187 VMIAMALLCRPKLLIADEPTTALD-VTVQaqimTLLNELKREF-NTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQAR 264
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDpVTLQ----IIRKTLKQSFsNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQ 1436
|
....*...
gi 899869912 265 DVFYHPSH 272
Cdd:TIGR01271 1437 KLLNETSL 1444
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-262 |
1.46e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.80 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDltVTFSTPDGDVTAVNaLNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREILNLPEKQL 108
Cdd:PRK10790 341 IDIDN--VSFAYRDDNLVLQN-INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPlTEGEI----RLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRlraeEISMIFQDPMTslnpymrVGEQLMEVLQLHKKMSKSEAFE--ESIRMLDAVK-MPEA-RKRMRMYPHEFSGGMR 184
Cdd:PRK10790 414 RQ----GVAMVQQDPVV-------LADTFLANVTLGRDISEEQVWQalETVQLAELARsLPDGlYTPLGEQGNNLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 185 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCNKVLVMYAGRTMEYGQ 262
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-269 |
2.89e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 32 VKDLTVTFSTpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTafalmgllaSNgRIGGSakfngreilnLPEKQLNRL 111
Cdd:PRK13546 24 MKDALIPKHK-NKTFFALDDISLKAYEGDVIGLVGINGSGKSTL---------SN-IIGGS----------LSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 112 RAEEISMIFQDpmTSLNPymrvgeQLMEVLQLHKKMSKSEAFEESIRML--DAVKMPEARKRMRMYPHEFSGGMRQRVMI 189
Cdd:PRK13546 83 RNGEVSVIAIS--AGLSG------QLTGIENIEFKMLCMGFKRKEIKAMtpKIIEFSELGEFIYQPVKKYSSGMRAKLGF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 190 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICNKVLVMYAGRTMEYGQARDVFYH 269
Cdd:PRK13546 155 SINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
49-263 |
8.04e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 49 VNALnfdLRAGETLGIVGESGSGKSqtafALMGLLASN-----GRIGGSAKFNGREilnlPEKQLNRLRAEEISMIFQDP 123
Cdd:TIGR00956 80 MDGL---IKPGELTVVLGRPGSGCS----TLLKTIASNtdgfhIGVEGVITYDGIT----PEEIKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 MTslnPYMRVGEQL-----MEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYPHEF----SGGMRQRVMIAMALL 194
Cdd:TIGR00956 149 HF---PHLTVGETLdfaarCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFvrgvSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 899869912 195 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFN-TAIIMI------THDLgvvagiCNKVLVMYAGRTMEYGQA 263
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIyqcsqdAYEL------FDKVIVLYEGYQIYFGPA 295
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-255 |
8.35e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFSTpdgdVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQL 108
Cdd:PRK15439 11 LLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS---GTLEIGGNPCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NRLraeEISMIFQDPMtsLNPYMRVGEQLMevLQLHKKMSKSEAFEESIRMLDAvkmpearkrmRMYPHEFSGGM----R 184
Cdd:PRK15439 84 HQL---GIYLVPQEPL--LFPNLSVKENIL--FGLPKRQASMQKMKQLLAALGC----------QLDLDSSAGSLevadR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 185 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYAG 255
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
55-251 |
9.10e-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: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 55 DLRAGETLGIVGESGSGKsqTAFALMglLAsnGRI---GGSAKFNgreiLNLPEKqlnrlrAEEISMIFQdpmtslnpyM 131
Cdd:COG1245 362 EIREGEVLGIVGPNGIGK--TTFAKI--LA--GVLkpdEGEVDED----LKISYK------PQYISPDYD---------G 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 132 RVGEQLMEVLQlhKKMSKSEAFEESIRMLDAVKMPEarKRMRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 211
Cdd:COG1245 417 TVEEFLRSANT--DDFGSSYYKTEIIKPLGLEKLLD--KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 899869912 212 TVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLV 251
Cdd:COG1245 489 EQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-251 |
9.67e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 23 EQNQNVLLDVKDLTVTFStpdgdvtavnalNFDL-------RAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIGGSAK 94
Cdd:PRK13409 334 ESERETLVEYPDLTKKLG------------DFSLeveggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLkPDEGEVDPELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 95 fngreilnlpekqlnrlraeeISM----IFQDPMtslnpyMRVGEQLMEVlqlHKKMSKSEAFEESIRMLDAVKMPEarK 170
Cdd:PRK13409 402 ---------------------ISYkpqyIKPDYD------GTVEDLLRSI---TDDLGSSYYKSEIIKPLQLERLLD--K 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 171 RMRmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVL 250
Cdd:PRK13409 450 NVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
.
gi 899869912 251 V 251
Cdd:PRK13409 526 V 526
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-238 |
1.29e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.93 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 27 NVLLDVKDLTVTFstpdGDVTAVNALNFDLRAGETLGIVGESGSGKSqTAFALMgllasngriggsakfNGREilnLPEK 106
Cdd:TIGR03719 320 DKVIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKS-TLFRMI---------------TGQE---QPDS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 107 QLNRLrAEEISMIFQDPM-TSLNPYMRVGEQL---MEVLQLHKKMSKSEAFEESIRMldavKMPEARKRMRmyphEFSGG 182
Cdd:TIGR03719 377 GTIEI-GETVKLAYVDQSrDALDPNKTVWEEIsggLDIIKLGKREIPSRAYVGRFNF----KGSDQQKKVG----QLSGG 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 899869912 183 MRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 238
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD 499
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
56-275 |
1.93e-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: 49.40 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 56 LRAGETLGIVGESGSGKSQTAFALMGLLASN-GRIGGSA-------KFNGREILNlpekQLNRLRAEEISmifqdpmTSL 127
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNlGDYDEEPswdevlkRFRGTELQD----YFKKLANGEIK-------VAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 128 NP-YMrvgEQLMEVL-----QLHKKMSKSEAFEESIRMLDAVKMPEarKRMRmyphEFSGGMRQRVMIAMALLCRPKLLI 201
Cdd:COG1245 165 KPqYV---DLIPKVFkgtvrELLEKVDERGKLDELAEKLGLENILD--RDIS----ELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 202 ADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICNKVLVMYaGRTMEYGqardVFyhpSHPYS 275
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY-GEPGVYG----VV---SKPKS 300
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
56-275 |
1.98e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 56 LRAGETLGIVGESGSGKSQTAFALMGLLASN-GRIGGSA-------KFNGREILNLpekqLNRLRAEEISmifqdpmTSL 127
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlGDYEEEPswdevlkRFRGTELQNY----FKKLYNGEIK-------VVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 128 NP-YMrvgEQLMEVL-----QLHKKMSKSEAFEESIRMLDAVKMPEarKRMRmyphEFSGGMRQRVMIAMALLCRPKLLI 201
Cdd:PRK13409 165 KPqYV---DLIPKVFkgkvrELLKKVDERGKLDEVVERLGLENILD--RDIS----ELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 202 ADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICNKVLVMYaGRTMEYGqardVFyhpSHPYS 275
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY-GEPGAYG----VV---SKPKG 299
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
39-239 |
2.18e-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: 48.10 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 39 FSTPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLAS-NGRIGGSAKFNGREILNLPEKQlNR------- 110
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTlEGKVHWSNKNESEPSFEATRSR-NRysvayaa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 111 -----LRAE-EISMIFQDPMTSlnpymrvgeqlmevlQLHKKMSKSEAFEESIRMLDAVKMPEARKRmrmyPHEFSGGMR 184
Cdd:cd03290 86 qkpwlLNATvEENITFGSPFNK---------------QRYKAVTDACSLQPDIDLLPFGDQTEIGER----GINLSGGQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 185 QRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 239
Cdd:cd03290 147 QRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
55-263 |
2.47e-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: 48.17 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 55 DLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPE----KQLNRLRAEeISMIFQDPMTSlnPY 130
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDE---GDIEIELDTVSYKPQyikaDYEGTVRDL-LSSITKDFYTH--PY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 131 MRVgeQLMEVLQLhkkmskseafeesIRMLDavkmpearkrmRMYPhEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 210
Cdd:cd03237 95 FKT--EIAKPLQI-------------EQILD-----------REVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 899869912 211 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICNKVLVmYAGRTMEYGQA 263
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEGEPSVNGVA 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
51-244 |
2.77e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.49 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 51 ALNFDLRAGETLGIVGESGSGKSqtafALMGLLASNGR-IGGSAKFNGREIlnlpekqlNRLRAEeismIFQDPM----- 124
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKT----SLLRILAGLARpDAGEVLWQGEPI--------RRQRDE----YHQDLLylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 125 ----TSLNPYmrvgEQLMEVLQLHkkmskSEAFEESIR-MLDAVKMpeaRKRMRMYPHEFSGGMRQRVMIAMALLCRPKL 199
Cdd:PRK13538 83 pgikTELTAL----ENLRFYQRLH-----GPGDDEALWeALAQVGL---AGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 899869912 200 LIADEPTTALDVTVQAQIMTLLNE-LKRefNTAIIMITH-DLGVVAG 244
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQ--GGMVILTTHqDLPVASD 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-241 |
4.77e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 46.79 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTfstpDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLL-ASNGRIggsaKFNGREIlnlpekql 108
Cdd:PRK13539 3 LEGEDLACV----RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLpPAAGTI----KLDGGDI-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 nrlraeEISMIF--------QDPMtslNPYMRVGEQLmevlqlhkkmskseAFEESIRMLDAVKMPEARKRMRMYP---- 176
Cdd:PRK13539 67 ------DDPDVAeachylghRNAM---KPALTVAENL--------------EFWAAFLGGEELDIAAALEAVGLAPlahl 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 177 --HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITH-DLGV 241
Cdd:PRK13539 124 pfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
30-122 |
1.15e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.10 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 30 LDVKDLTVTFSTPDGDVT-AVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLA-SNGRIggsaKFNGREIlnlPEKQ 107
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRpESGEI----LLDGQPV---TADN 400
|
90
....*....|....*
gi 899869912 108 LNRLRaEEISMIFQD 122
Cdd:COG4615 401 REAYR-QLFSAVFSD 414
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
40-241 |
1.47e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.01 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 40 STPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFAlmgllasngriGGSAKFNGREILNLPekqlnrlRAEEISMI 119
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-----------GLYASGKARLISFLP-------KFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 120 FQDPMTSLnpyMRVGeqlMEVLQLHKKMSKseafeesirmldavkmpearkrmrmypheFSGGMRQRVMIAMALLCRPK- 198
Cdd:cd03238 64 FIDQLQFL---IDVG---LGYLTLGQKLST-----------------------------LSGGELQRVKLASELFSEPPg 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 899869912 199 -LLIADEPTTALDvtvQAQIMTLLNELKR---EFNTaIIMITHDLGV 241
Cdd:cd03238 109 tLFILDEPSTGLH---QQDINQLLEVIKGlidLGNT-VILIEHNLDV 151
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
180-243 |
2.58e-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: 2.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 180 SGGMRQRVMIAMAL-LCRPK---LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVA 243
Cdd:cd03227 79 SGGEKELSALALILaLASLKprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAE 145
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
180-242 |
2.72e-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: 2.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899869912 180 SGGMRQRVMIAMALLCR---PKLLIADEPTTAL---DVtvqAQIMTLLNELKREFNTaIIMITHDLGVV 242
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGNT-VVVIEHNLDVI 895
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
54-238 |
3.16e-05 |
|
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: 44.14 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 54 FDLRAGETLgIVGESGSGKSQT----AFALMGLLASNGRIG-GSAKFNGReilnlpekqlNRLRAEeISMIFQDpmtsln 128
Cdd:cd03240 18 IEFFSPLTL-IVGQNGAGKTTIiealKYALTGELPPNSKGGaHDPKLIRE----------GEVRAQ-VKLAFEN------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 129 pymRVGEQlMEVLQlhkkmsKSEAFEESI--RMLDAVK-MPEARKRMrmyphefSGGMRQ------RVMIAMALLCRPKL 199
Cdd:cd03240 80 ---ANGKK-YTITR------SLAILENVIfcHQGESNWpLLDMRGRC-------SGGEKVlasliiRLALAETFGSNCGI 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 899869912 200 LIADEPTTALDV-TVQAQIMTLLNELKREFNTAIIMITHD 238
Cdd:cd03240 143 LALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
57-218 |
6.02e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 57 RAGETLGIVGESGSGKSqtafALMGLLA---SNGRIGGSAKFNGreilnLPEKQLNRLRaeeIS-MIFQDPMTSlnPYMR 132
Cdd:PLN03140 904 RPGVLTALMGVSGAGKT----TLMDVLAgrkTGGYIEGDIRISG-----FPKKQETFAR---ISgYCEQNDIHS--PQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 133 VGEQLM--EVLQLHKKMSKSEAFEESIRMLDAVKMPEARKRMRMYP--HEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 208
Cdd:PLN03140 970 VRESLIysAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170
....*....|
gi 899869912 209 LDVTVQAQIM 218
Cdd:PLN03140 1050 LDARAAAIVM 1059
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
180-244 |
6.93e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 6.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899869912 180 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 244
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHDryfLDNVAG 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-263 |
8.56e-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: 42.56 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 157 IRMLDAVKMPEA------RKRMRMYPH--EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREF 228
Cdd:cd03222 42 VKILAGQLIPNGdndewdGITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
90 100 110
....*....|....*....|....*....|....*
gi 899869912 229 NTAIIMITHDLGVVAGICNKVLVMYaGRTMEYGQA 263
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGIA 155
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
46-256 |
8.95e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 46 VTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREILNLPEKQlnrlrAEE--ISMIFQDp 123
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS---GSILFQGKEIDFKSSKE-----ALEngISMVHQE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 124 mtsLNPYMRvgEQLMEVLQL-----------HKKMskseaFEESIRMLDAVKMP-EARKRMRmyphEFSGGMRQRVMIAM 191
Cdd:PRK10982 82 ---LNLVLQ--RSVMDNMWLgryptkgmfvdQDKM-----YRDTKAIFDELDIDiDPRAKVA----TLSVSQMQMIEIAK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899869912 192 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICNKVLVMYAGR 256
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
174-256 |
1.66e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 174 MYphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLnelkrEFNTAIIMITHDLGVVAGICNKVLVM 252
Cdd:PLN03073 625 MY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVV 697
|
....
gi 899869912 253 YAGR 256
Cdd:PLN03073 698 SEGK 701
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
180-238 |
1.97e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 1.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 180 SGGMRQRVMIAmALLCRP-KLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 238
Cdd:PRK11147 442 SGGERNRLLLA-RLFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-211 |
2.34e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 24 QNQNVLLDVKDLTVtfstpDGDVTavnalnfdLRAGETLGIVGESGSGKSqTAFALMGLLASNG------------RIGG 91
Cdd:PLN03073 181 ENFSISVGGRDLIV-----DASVT--------LAFGRHYGLVGRNGTGKT-TFLRYMAMHAIDGipkncqilhveqEVVG 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 92 SAKFNGREILNlPEKQLNRLRAEEISMIFQDpmTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEESIRMLDAVKMPEARKR 171
Cdd:PLN03073 247 DDTTALQCVLN-TDIERTQLLEEEAQLVAQQ--RELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEAR 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 899869912 172 --------------MRMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 211
Cdd:PLN03073 324 aasilaglsftpemQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
106-239 |
4.67e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 41.57 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 106 KQLNRLRAEEISMIFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKS-EAFEESIRMLDAVKMP--EARKRMRMYPH----- 177
Cdd:COG1106 117 AQLNVPLLSPLYDWFDNNISLDTSSDGLTLLLKEDESLKEELLELlKIADPGIEDIEVEEEEieDLVERKLIFKHkggnv 196
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 178 -----EFSGGMRQRVMIAMAL---LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 239
Cdd:COG1106 197 plplsEESDGTKRLLALAGALldaLAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHST 266
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
180-227 |
5.27e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 5.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 899869912 180 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRE 227
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
29-237 |
6.08e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.32 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 29 LLDVKDLTVTFStpdgDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASNGrigGSAKFNGREIlnlpEKQL 108
Cdd:PRK13540 1 MLDVIELDFDYH----DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK---GEILFERQSI----KKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 109 NrlrAEEISMIFQDPMTSLNPYMRVGEQLMevLQLHKKmSKSEAFEESIRMLDAVKMPEarkrmrmYP-HEFSGGMRQRV 187
Cdd:PRK13540 70 C---TYQKQLCFVGHRSGINPYLTLRENCL--YDIHFS-PGAVGITELCRLFSLEHLID-------YPcGLLSSGQKRQV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 899869912 188 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITH 237
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
57-224 |
7.46e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 57 RAGETLGIVGESGSGKSqtafALMGLLAsnGRIGGSAKFNGREILNLPEKQLNRLRAeeISMIFQDPMTSLNPYMRVGEQ 136
Cdd:TIGR00956 787 KPGTLTALMGASGAGKT----TLLNVLA--ERVTTGVITGGDRLVNGRPLDSSFQRS--IGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 137 LMEVLQLHKKMSKSEAF---EESIRMLDavkmpearkrMRMYPHEFSG----GM----RQRVMIAMALLCRPKLLI-ADE 204
Cdd:TIGR00956 859 FSAYLRQPKSVSKSEKMeyvEEVIKLLE----------MESYADAVVGvpgeGLnveqRKRLTIGVELVAKPKLLLfLDE 928
|
170 180
....*....|....*....|
gi 899869912 205 PTTALDVTVQAQIMTLLNEL 224
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKL 948
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
119-238 |
2.44e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 119 IFQDPMTSLNPYMRVGEQLMEVLQLHKKMSKSEAFEesirMLDAVKMPEARKRMRMypHEFSGGMRQRVMIAMALLCRPK 198
Cdd:PRK15064 102 IYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGE----LLLGVGIPEEQHYGLM--SEVAPGWKLRVLLAQALFSNPD 175
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 899869912 199 LLIADEPTTALDVTVqaqIMTLLNELkREFNTAIIMITHD 238
Cdd:PRK15064 176 ILLLDEPTNNLDINT---IRWLEDVL-NERNSTMIIISHD 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
180-250 |
4.76e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 4.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899869912 180 SGGMRQRVMIAMALLC---RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAgICNKVL 250
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI-IEHNMHVVK-VADYVL 882
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-261 |
5.20e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.95 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 38 TFS-TPDGDVTAVNALNFDLRAGETLGIVGESGSGKSQTAFALMGLLASngRIGGSAKFNGReILNLPEkqlnrlraeeI 116
Cdd:PLN03130 621 YFSwDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP--RSDASVVIRGT-VAYVPQ----------V 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899869912 117 SMIF----QDPMTSLNPYMRVG-EQLMEVLQLHKKMSkseafeesirMLDAVKMPEARKRMRmyphEFSGGMRQRVMIAM 191
Cdd:PLN03130 688 SWIFnatvRDNILFGSPFDPERyERAIDVTALQHDLD----------LLPGGDLTEIGERGV----NISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899869912 192 ALLCRPKLLIADEPTTALDVTVQAQIMTllNELKREF-NTAIIMITHDLGVVAGIcNKVLVMYAGRTMEYG 261
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| |
