|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-247 |
9.71e-83 |
|
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: 250.74 E-value: 9.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLS----LQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVDLGKLTVKQWQ 79
Cdd:COG0444 2 LEVRNLKvyfpTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 KLRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKYPFELSGGMLQRIML 159
Cdd:COG0444 82 KIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 160 ATILSLDPQVIILDEPTSAVDchncSTISA----ILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQA 234
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD----VTIQAqilnLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
250
....*....|...
gi 446358294 235 ILSNPQHNYTKAL 247
Cdd:COG0444 238 LFENPRHPYTRAL 250
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-247 |
1.36e-67 |
|
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: 217.46 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLS-----LQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQW 78
Cdd:COG1123 261 LEVRNLSkrypvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR---PTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 QKLRgRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIM 158
Cdd:COG1123 338 RELR-RRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPP--DLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
250
....*....|
gi 446358294 238 NPQHNYTKAL 247
Cdd:COG1123 495 NPQHPYTRAL 504
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-247 |
4.47e-66 |
|
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: 214.16 E-value: 4.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIG----EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGM-TVRGNIFFKGVDLGKLTVKQW 78
Cdd:COG4172 7 LSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAaHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 QKLRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKYPFELSGGMLQRIM 158
Cdd:COG4172 87 RRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 159 LATILSLDPQVIILDEPTSAVDChncsTISA----ILQELQN-NGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQ 233
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDV----TVQAqildLLKDLQReLGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
250
....*....|....
gi 446358294 234 AILSNPQHNYTKAL 247
Cdd:COG4172 243 ELFAAPQHPYTRKL 256
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-230 |
2.05e-65 |
|
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: 203.12 E-value: 2.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSL----QIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKLTvKQWQ 79
Cdd:cd03257 2 LEVKNLSVsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP---TSGSIIFDGKDLLKLS-RRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 KLRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKA-LEWMKRLNLDDAIslLKKYPFELSGGMLQRIM 158
Cdd:cd03257 78 KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvLLLLVGVGLPEEV--LNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQN-NGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-240 |
2.29e-61 |
|
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: 201.29 E-value: 2.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQI--GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVDLGKLTVKqwqkL 81
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEA----L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRDIAYLVQNPMSMFNPfQKIEAHILETILSHeKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLAT 161
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNP-VTVGDQIAEALENL-GLSRAEARARVLELLEAVGLER---RLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 162 ILSLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-247 |
1.49e-58 |
|
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: 186.04 E-value: 1.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 21 DFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMT-VRGNIFFKGVDLGKLtvkqwqKLRGRDIAYLVQNPMSMFNP 99
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTqTSGEILLDGRPLLPL------SIRGRHIATIMQNPRTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 100 FQKIEAHILETILSHEKCSKrVALSKALEWMKRLNLDDAISLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAV 179
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 180 DCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYTKAL 247
Cdd:TIGR02770 157 DVVNQARVLKLLRELrQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKL 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-247 |
2.12e-54 |
|
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: 175.76 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGE----VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKltvkQWQ 79
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP---WSGEVTFDGRPVTR----RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 KLRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEwmkRLNLDDaiSLLKKYPFELSGGMLQRIML 159
Cdd:COG1124 75 KAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELLE---QVGLPP--SFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQN-NGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSN 238
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
....*....
gi 446358294 239 PQHNYTKAL 247
Cdd:COG1124 230 PKHPYTREL 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-240 |
3.31e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 164.43 E-value: 3.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQI-GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQwqkL 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT----SGEVLVDGKDITKKNLRE---L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RgRDIAYLVQNPMSMFnpfqkIEAHILETI--------LSHEKCSKRVAlskalEWMKRLNLDDaisLLKKYPFELSGGM 153
Cdd:COG1122 74 R-RKVGLVFQNPDDQL-----FAPTVEEDVafgpenlgLPREEIRERVE-----EALELVGLEH---LADRPPHELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQ 233
Cdd:COG1122 140 KQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
....*..
gi 446358294 234 AILSNPQ 240
Cdd:COG1122 220 EVFSDYE 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-247 |
1.13e-46 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 158.53 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQI----GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIF-FKGVDLGKLTV 75
Cdd:COG4170 1 MPLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFrWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 76 KQWQKLRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHE-KCS--KRVALSK--ALEWMKRLNLDDAISLLKKYPFELS 150
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTfKGKwwQRFKWRKkrAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 151 GGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQ 229
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250
....*....|....*...
gi 446358294 230 GQTQAILSNPQHNYTKAL 247
Cdd:COG4170 241 GPTEQILKSPHHPYTKAL 258
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-247 |
1.17e-46 |
|
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: 162.93 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvrGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQNP 93
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE----GEIRFDGQDLDGLSRRALRPLR-RRMQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMFNPFQKIEAHILETILSHekcskRVALSKA------LEWMKRLNLDDAisLLKKYPFELSGGMLQRIMLATILSLDP 167
Cdd:COG4172 372 FGSLSPRMTVGQIIAEGLRVH-----GPGLSAAerrarvAEALEEVGLDPA--ARHRYPHEFSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 168 QVIILDEPTSAVDchncSTISA----ILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHN 242
Cdd:COG4172 445 KLLVLDEPTSALD----VSVQAqildLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
....*
gi 446358294 243 YTKAL 247
Cdd:COG4172 521 YTRAL 525
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-247 |
1.18e-46 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 156.01 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 2 EQLEIRKLSLQiGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMT-VRGNIFFKGVDLGKltvkqwQK 80
Cdd:PRK10418 3 QQIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGRVLLDGKPVAP------CA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEwmkRLNLDDAISLLKKYPFELSGGMLQRIMLA 160
Cdd:PRK10418 76 LRGRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALE---AVGLENAARVLKLYPFEMSGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNP 239
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
....*...
gi 446358294 240 QHNYTKAL 247
Cdd:PRK10418 233 KHAVTRSL 240
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-225 |
3.84e-46 |
|
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: 153.39 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 5 EIRKLSLQI--GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQwqklR 82
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG---PTSGEVLVDGKDLTKLSLKE----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLVQNPMSMFnpfqkIEAHILETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIML 159
Cdd:cd03225 74 RRKVGLVFQNPDDQF-----FGPTVEEEVafgLENLGLPEEEIEERVEEALELVGLEG---LRDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGE 225
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-247 |
9.06e-45 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 153.36 E-value: 9.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPV----LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIP-QGMTVRGNIFFKGVDLGKLTV 75
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 76 KQWQKLRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKYPFELSGGMLQ 155
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 156 RIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQA 234
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|...
gi 446358294 235 ILSNPQHNYTKAL 247
Cdd:PRK11022 241 IFRAPRHPYTQAL 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-247 |
1.67e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 158.48 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQ-GMTVRGNIFF------KGVDLGKLTVKQWQKLRGRDI 86
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQaGGLVQCDKMLlrrrsrQVIELSEQSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 87 AYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKYPFELSGGMLQRIMLATILSLD 166
Cdd:PRK10261 107 AMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 167 PQVIILDEPTSAVDChncsTISA-ILQEL----QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQH 241
Cdd:PRK10261 187 PAVLIADEPTTALDV----TIQAqILQLIkvlqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
....*.
gi 446358294 242 NYTKAL 247
Cdd:PRK10261 263 PYTRAL 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-256 |
4.65e-42 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 150.63 E-value: 4.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSL---QIGEV-PVLRDFSCKIDMGESLTIIGESGSGK--TLLAKLLVGHIPQGMTVRGNIFFKGVDLGKLTVKQ 77
Cdd:PRK15134 6 LAIENLSVafrQQQTVrTVVNDVSLQIEAGETLALVGESGSGKsvTALSILRLLPSPPVVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 78 WQKLRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKYPFELSGGMLQRI 157
Cdd:PRK15134 86 LRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAIL 236
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
250 260
....*....|....*....|
gi 446358294 237 SNPQHNYTKALtVQMEYEGD 256
Cdd:PRK15134 246 SAPTHPYTQKL-LNSEPSGD 264
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-247 |
5.68e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.03 E-value: 5.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 21 DFSckIDMGESLTIIGESGSGKTLLAKLLVGHIPqgMTvRGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQNPMSMFNPF 100
Cdd:COG4608 38 SFD--IRRGETLGLVGESGCGKSTLGRLLLRLEE--PT-SGEILFDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 101 QKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVD 180
Cdd:COG4608 112 MTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRP--EHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 181 ChncsTISA----ILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYTKAL 247
Cdd:COG4608 190 V----SIQAqvlnLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQAL 257
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-247 |
9.30e-42 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 145.64 E-value: 9.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVDLGKLTVKQWQKLRGRDIAYLVQNP 93
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKYPFELSGGMLQRIMLATILSLDPQVIILD 173
Cdd:PRK09473 107 MTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446358294 174 EPTSAVDCHNCSTISAILQELQNNGKT-LITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYTKAL 247
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGL 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-236 |
1.49e-41 |
|
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: 142.43 E-value: 1.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQWQKLR 82
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD----SGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNPM---SMfNPFQKIEAHILEtilsHEKCSKRVALSKALEWMKRLNLDDAIsllKKYPFELSGGMLQRIML 159
Cdd:COG1127 82 -RRIGMLFQGGAlfdSL-TVFENVAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAA---DKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAIL 236
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-237 |
2.06e-41 |
|
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: 143.02 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQN 92
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlEKPA----QGTVSFRGQDLYQLDRKQRRAFR-RDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 PMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAIslLKKYPFELSGGMLQRIMLATILSLDPQVIIL 172
Cdd:TIGR02769 97 SPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSED--ADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 173 DEPTSAVDCHNCSTISAILQELQNNGKT-LITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-240 |
8.44e-41 |
|
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: 140.33 E-value: 8.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKLTVKQWQKLRg 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP---DSGEVLIDGEDISGLSEAELYRLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPM---SMfNPFQKIEAHILEtilsHEKCSKRVALSKALEWMKRLNLDDAIsllKKYPFELSGGMLQRIMLA 160
Cdd:cd03261 77 RRMGMLFQSGAlfdSL-TVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQELQN-NGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS-- 237
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsd 228
|
...
gi 446358294 238 NPQ 240
Cdd:cd03261 229 DPL 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-226 |
8.69e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.57 E-value: 8.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKLTVKQWqklRg 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP---TSGEIYLDGKPLSAMPPPEW---R- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPmSMFnpFQKIEAHILETILSHEKcskRVALSKALEWMKRLNLDDAIslLKKYPFELSGGMLQRIMLATIL 163
Cdd:COG4619 74 RQVAYVPQEP-ALW--GGTVRDNLPFPFQLRER---KFDRERALELLERLGLPPDI--LDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-247 |
1.46e-39 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 139.84 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 29 GESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQNPMSMFNPFQKIEAHIL 108
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVK---ATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 109 ETILS-HEKCSKRVALSKALEWMKRLNLddAISLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTI 187
Cdd:PRK15079 123 EPLRTyHPKLSRQEVKDRVKAMMLKVGL--LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 188 SAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYTKAL 247
Cdd:PRK15079 201 VNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKAL 261
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-246 |
3.47e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 136.28 E-value: 3.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGkLTVKQWQKLR 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPDS----GTITVDGEDLT-DSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNpmsmFNPFqkieAH--ILETI----LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQR 156
Cdd:COG1126 77 -RKVGMVFQQ----FNLF----PHltVLENVtlapIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAIL 236
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
250
....*....|
gi 446358294 237 SNPQHNYTKA 246
Cdd:COG1126 225 ENPQHERTRA 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-247 |
7.15e-38 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 139.07 E-value: 7.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 13 IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtvRGNIFFKGVDLGKLTVKQWQKLRGRdIAYLVQN 92
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS----QGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 PMSMFNPFQKIEAHILETILSHEKC-SKRVALSKALEWMKRLNLDDAISllKKYPFELSGGMLQRIMLATILSLDPQVII 171
Cdd:PRK15134 371 PNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLDPETR--HRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 172 LDEPTSAVDCHNCSTISAILQELQNNGK-TLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYTKAL 247
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQL 525
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-251 |
1.94e-37 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 134.16 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQI----GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIF-FKGVDLGKLTV 75
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMrFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 76 KQWQKLRGRDIAYLVQNPMSMFNPFQKIEAHILETI---LSHEKCSKRVALSK--ALEWMKRLNLDDAISLLKKYPFELS 150
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwTYKGRWWQRFGWRKrrAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 151 GGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQ 229
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260
....*....|....*....|..
gi 446358294 230 GQTQAILSNPQHNYTKALTVQM 251
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAI 262
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-237 |
3.97e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.98 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKltvkqwqklRG 83
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP---PTSGTVRLFGKPPRR---------AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQN-------PMSmfnpfqkieahILETILSH-------EKCSKRVALSKALEWMKRLNLDDaislLKKYPF-E 148
Cdd:COG1121 75 RRIGYVPQRaevdwdfPIT-----------VRDVVLMGrygrrglFRRPSRADREAVDEALERVGLED----LADRPIgE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISeGEVVE 228
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVA 218
|
....*....
gi 446358294 229 QGQTQAILS 237
Cdd:COG1121 219 HGPPEEVLT 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-226 |
1.81e-36 |
|
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: 128.76 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIG----EVPVLRDFSCKIDMGESLTIIGESGSGKT----LLAKLLVghiPQgmtvRGNIFFKGVDLGKLTV 75
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKStllnILGGLDR---PT----SGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 76 KQWQKLRGRDIAYLVQNpmsmFN--PFQKIEAHIlETILSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGM 153
Cdd:cd03255 74 KELAAFRRRHIGFVFQS----FNllPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARdLGGQLLVISEGEV 226
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-238 |
4.57e-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: 128.44 E-value: 4.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLgkltVKQWQKLR 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkPD----SGSILIDGEDV----RKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNPMsmFNPFQKIEAHILETILSHEKcSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATI 162
Cdd:COG4555 74 -RQIGVLPDERG--LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGLEE---FLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 163 LSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSN 238
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-229 |
8.25e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 127.08 E-value: 8.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIG----EVPVLRDFSCKIDMGESLTIIGESGSGK-TLLakllvgHIPQGMTV--RGNIFFKGVDLGKLTVK 76
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKsTLL------NILGGLDRptSGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 77 QWQKLRGRDIAYLVQNP--MSMFNPFQKIEahiLETILSHEkcSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGML 154
Cdd:COG1136 79 ELARLRRRHIGFVFQFFnlLPELTALENVA---LPLLLAGV--SRKERRERARELLERVGLGD---RLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 155 QRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARdLGGQLLVISEGEVVEQ 229
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-230 |
5.38e-35 |
|
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: 124.55 E-value: 5.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgMTvRGNIFFKGVDLGKLTVKQwqklrg 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER--PD-SGEILIDGRDVTGVPPER------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPmSMFnPfqkieaH--ILETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIM 158
Cdd:cd03259 72 RNIGMVFQDY-ALF-P------HltVAENIafgLKLRGVPKAEIRARVRELLELVGLEG---LLNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-228 |
1.07e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 125.57 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQNPMSM 96
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESPSQ----GNVSWRGEPLAKLNRAQRKAFR-RDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPT 176
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446358294 177 SAVDCHNCSTISAILQELQNNGKT-LITVTHDYQLARDLGGQLLVISEGEVVE 228
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-211 |
2.57e-34 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 122.72 E-value: 2.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 6 IRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLvGHIPQgmTVRGNIFFKGVDLGKLTVKQWQKLRGRD 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNII-GLLEK--FDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 86 IAYLVQNPMSMFNpfQKIEAHiLETILSHEKCSKRVALSKALEWMKRLNLDdaiSLLKKYPFELSGGMLQRIMLATILSL 165
Cdd:TIGR03608 78 LGYLFQNFALIEN--ETVEEN-LDLGLKYKKLSKKEKREKKKEALEKVGLN---LKLKQKIYELSGGEQQRVALARAILK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446358294 166 DPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLA 211
Cdd:TIGR03608 152 PPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-239 |
5.03e-34 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 123.18 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEV-PVLRDFSCKIDMGESLTIIGESGSGKTLLAKL---LVGHipqgmtVRGNIFFKGVDlgkltVKQWQ 79
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMinrLIEP------TSGEIFIDGED-----IREQD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 --KLRgRDIAYLVQNpMSMFnPFQKIEAHIlETILSHEKCSKRVALSKALEWMKRLNLDDAiSLLKKYPFELSGGMLQRI 157
Cdd:cd03295 70 pvELR-RKIGYVIQQ-IGLF-PHMTVEENI-ALVPKLLKWPKEKIRERADELLALVGLDPA-EFADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDchncSTISAILQEL-----QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQT 232
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALD----PITRDQLQEEfkrlqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
....*..
gi 446358294 233 QAILSNP 239
Cdd:cd03295 221 DEILRSP 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-230 |
7.12e-34 |
|
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: 121.87 E-value: 7.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 5 EIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKltvkqwqklRGR 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP---TSGSIRVFGKPLEK---------ERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 85 DIAYLVQN-------PMS-----MFNPFQKIEAHileTILSHEKCskrvalSKALEWMKRLNLDDaislLKKYPF-ELSG 151
Cdd:cd03235 69 RIGYVPQRrsidrdfPISvrdvvLMGLYGHKGLF---RRLSKADK------AKVDEALERVGLSE----LADRQIgELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 152 GMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVIsEGEVVEQG 230
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
4-247 |
8.31e-34 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 123.00 E-value: 8.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGE----VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKG-----VDLGKLT 74
Cdd:COG4107 9 LSVRGLSKRYGPgcgtVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPT---SGSVYYRDrdggpRDLFALS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 75 VKQWQKLRGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDdaISLLKKYPFELSGGML 154
Cdd:COG4107 86 EAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHYGDIRARALEWLERVEIP--LERIDDLPRTFSGGMQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 155 QRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQ 233
Cdd:COG4107 164 QRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQrELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLTD 243
|
250
....*....|....
gi 446358294 234 AILSNPQHNYTKAL 247
Cdd:COG4107 244 QVLEDPQHPYTQLL 257
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-240 |
1.30e-33 |
|
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: 121.67 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVpVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQwqklrg 83
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK---PDSGKILLNGKDITNLPPEK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNpMSMFnPFQKIEAHIlETILSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATIL 163
Cdd:cd03299 71 RDISYVPQN-YALF-PHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDH---LLNRKPETLSGGEQQRVAIARAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-247 |
1.67e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 123.92 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 16 VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLL-VGHIPQGmtvrGNIFFKGVDLGKLTvKQWQKLRGRDIAYLVQNPM 94
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLtMIETPTG----GELYYQGQDLLKAD-PEAQKLLRQKIQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 95 SMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISllKKYPFELSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:PRK11308 103 GSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHY--DRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 175 PTSAVDChncsTISA----ILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYTKAL 247
Cdd:PRK11308 181 PVSALDV----SVQAqvlnLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQAL 254
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-237 |
5.05e-33 |
|
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: 120.53 E-value: 5.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQwqklRG 83
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLASLSRRE----LA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMSMFNpfqkieAHILETIL----SHEKCSKRVA---LSKALEWMKRLNLDDaislLKKYPF-ELSGGMLQ 155
Cdd:COG1120 75 RRIAYVPQEPPAPFG------LTVRELVAlgryPHLGLFGRPSaedREAVEEALERTGLEH----LADRPVdELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 156 RIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQA 234
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
...
gi 446358294 235 ILS 237
Cdd:COG1120 225 VLT 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-237 |
8.82e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.40 E-value: 8.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLgkltVKQWQKLR 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTS----GEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRdIAYLVQNPMsmFNPFQKIEAHiLETILSHEKCSKRVALSKALEWMKRLNLDDAislLKKYPFELSGGMLQRIMLATI 162
Cdd:COG1131 73 RR-IGYVPQEPA--LYPDLTVREN-LRFFARLYGLPRKEARERIDELLELFGLTDA---ADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446358294 163 LSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-240 |
1.16e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.10 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLGKLTVKQWQKlrgrDIAYLVQNP 93
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQS----GEIKIDGITISKENLKEIRK----KIGIIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMFnpfqkIEAHILETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQVI 170
Cdd:PRK13632 93 DNQF-----IGATVEDDIafgLENKKVPPKKMKDIIDDLAKKVGMED---YLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 171 ILDEPTSAVDCHNCSTISAILQELQNNG-KTLITVTHDYQLARdLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-240 |
1.87e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 121.36 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKLTVKQwqk 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP---DSGRILLDGRDVTGLPPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 lrgRDIAYLVQNP-----MSmfnpfqkieahILETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGG 152
Cdd:COG3842 77 ---RNVGMVFQDYalfphLT-----------VAENVafgLRMRGVPKAEIRARVAELLELVGLEG---LADRYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHN----CSTISAILQELqnnGKTLITVTHDyQ---LArdLGGQLLVISEGE 225
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLreemREELRRLQREL---GITFIYVTHD-QeeaLA--LADRIAVMNDGR 213
|
250
....*....|....*
gi 446358294 226 VVEQGQTQAILSNPQ 240
Cdd:COG3842 214 IEQVGTPEEIYERPA 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-235 |
5.32e-32 |
|
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: 117.28 E-value: 5.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKL---LVGHIPqGMTVRGNIFFKGVDLGKLTVKQwQK 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIP-GAPDEGEVLLDGKDIYDLDVDV-LE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRgRDIAYLVQNPmsmfNPFQK-IEAHI-----LETILSHEKCSKRV--ALSKALEW---MKRLNlddaisllkkyPFEL 149
Cdd:cd03260 79 LR-RRVGMVFQKP----NPFPGsIYDNVayglrLHGIKLKEELDERVeeALRKAALWdevKDRLH-----------ALGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 150 SGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVVEQ 229
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
....*.
gi 446358294 230 GQTQAI 235
Cdd:cd03260 222 GPTEQI 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-245 |
8.42e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 117.54 E-value: 8.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKT-LLAKLLVGHIPQGMTVR-GNIffkGVDLGKLTVKQW 78
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTtLLRCINLLEQPEAGTIRvGDI---TIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 QKLRG--RDIAYLVQNpmsmFN--PFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNL---DDAisllkkYPFELSG 151
Cdd:PRK11264 78 GLIRQlrQHVGFVFQN----FNlfPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLagkETS------YPRRLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 152 GMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQ 231
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
250
....*....|....
gi 446358294 232 TQAILSNPQHNYTK 245
Cdd:PRK11264 228 AKALFADPQQPRTR 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-230 |
1.12e-31 |
|
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: 115.23 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 5 EIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQwqklRGR 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---SGEILLDGKDLASLSPKE----LAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 85 DIAYLVQnpmsmfnpfqkieahiletilshekcskrvalskaleWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILS 164
Cdd:cd03214 74 KIAYVPQ-------------------------------------ALELLGLAH---LADRPFNELSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 165 LDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-238 |
1.79e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.88 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKT-----LLAKLL--VGHI--------PQGMTVRGNIFFKGVDLGKLTVKQWQ 79
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTtfiehLNALLLpdTGTIewifkdekNKKKTKEKEKVLEKLVIQKTRFKKIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 KLRG--RDIAYLVQnpmsmFNPFQKIEAHILETI----LSHeKCSKRVALSKALEWMKRLNLDdaISLLKKYPFELSGGM 153
Cdd:PRK13651 99 KIKEirRRVGVVFQ-----FAEYQLFEQTIEKDIifgpVSM-GVSKEEAKKRAAKYIELVGLD--ESYLQRSPFELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQ 233
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
....*
gi 446358294 234 AILSN 238
Cdd:PRK13651 251 DILSD 255
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-240 |
7.44e-31 |
|
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: 114.60 E-value: 7.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGhipQGMTVRGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQNp 93
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING---LERPTSGSVLVDGTDLTLLSGKELRKAR-RRIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 msmFNPFQkiEAHILETI---LSHEKCSKRVALSKALEWMKRLNLDDAIsllKKYPFELSGGMLQRIMLATILSLDPQVI 170
Cdd:cd03258 91 ---FNLLS--SRTVFENValpLEIAGVPKAEIEERVLELLELVGLEDKA---DAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 171 ILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-243 |
2.16e-30 |
|
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: 114.28 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 5 EIRKlslQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLRGR 84
Cdd:cd03294 29 EILK---KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE---PTSGKVLIDGQDIAAMSRKELRELRRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 85 DIAYLVQNpMSMFnpfqkieAH--ILETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIML 159
Cdd:cd03294 103 KISMVFQS-FALL-------PHrtVLENVafgLEVQGVPRAEREERAAEALELVGLEG---WEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 160 ATILSLDPQVIILDEPTSAVDchncSTISAILQE----LQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQA 234
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALD----PLIRREMQDellrLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
....*....
gi 446358294 235 ILSNPQHNY 243
Cdd:cd03294 248 ILTNPANDY 256
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-207 |
2.17e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.03 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQ----IGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLaKLLVGHIPQgmtVRGNIFFKGVDLGKLtvkqw 78
Cdd:COG1116 8 LELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKsTLL-RLIAGLEKP---TSGEVLVDGKPVTGP----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 qklrGRDIAYLVQNPMSMfnPFQKIEAHIlETILSHEKCSKRVALSKALEWMKRLNLDDAislLKKYPFELSGGMLQRIM 158
Cdd:COG1116 79 ----GPDRGVVFQEPALL--PWLTVLDNV-ALGLELRGVPKAERRERARELLELVGLAGF---EDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 159 LATILSLDPQVIILDEPTSAVDchncstisAI----LQEL-----QNNGKTLITVTHD 207
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALD--------ALtrerLQDEllrlwQETGKTVLFVTHD 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-225 |
2.80e-30 |
|
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: 110.80 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 5 EIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQWQklrgR 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDIAKLPLEELR----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 85 DIAYLVQnpmsmfnpfqkieahiletilshekcskrvalskalewmkrlnlddaisllkkypfeLSGGMLQRIMLATILS 164
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------------LSGGQRQRVALARALL 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 165 LDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGE 225
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-247 |
6.07e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 117.65 E-value: 6.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQNPM 94
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE---SQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDPY 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 95 SMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISLlkKYPFELSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:PRK10261 412 ASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAW--RYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 175 PTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYTKAL 247
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKL 563
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-240 |
1.06e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.98 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLAKLLVGHIPQgmtvRGNIFFKGVDL-------GKLT 74
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKsTFLRCINFLEKPS----EGSIVVNGQTInlvrdkdGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 75 V---KQWQKLRGRdIAYLVQNpmsmFN--PFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISllKKYPFEL 149
Cdd:PRK10619 81 VadkNQLRLLRTR-LTMVFQH----FNlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 150 SGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQ 229
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250
....*....|.
gi 446358294 230 GQTQAILSNPQ 240
Cdd:PRK10619 234 GAPEQLFGNPQ 244
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-239 |
1.08e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 111.72 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLL-----------AKLLVGhipqGMTVRGniffkgvdlG 71
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKsTLLrcinkleeitsGDLIVD----GLKVND---------P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 72 KLTVKQWqklrgRDIAYLVqnpMSMFNPFQKIEAhiLETI----LSHEKCSKRVALSKALEWMKRLNLDDAISllkKYPF 147
Cdd:PRK09493 69 KVDERLI-----RQEAGMV---FQQFYLFPHLTA--LENVmfgpLRVRGASKEEAEKQARELLAKVGLAERAH---HYPS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 148 ELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
250
....*....|..
gi 446358294 228 EQGQTQAILSNP 239
Cdd:PRK09493 216 EDGDPQVLIKNP 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-240 |
1.17e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLL-VGHIPQG--MTVRGNIFfkgvDLG-KLTVKQWQKLRgRDIAYL 89
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDSgqLNIAGHQF----DFSqKPSEKAIRLLR-QKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 90 VQNpmsmFN--PFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDP 167
Cdd:COG4161 88 FQQ----YNlwPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTD---KADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 168 QVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGqTQAILSNPQ 240
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQ 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-227 |
1.54e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.42 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 5 EIRKLSLQIGEVP-VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGkltvkqwQKLRG 83
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE---SSGSILLNGKPIK-------AKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMSMFnpFQkiEAHILETILSHEKCSKRVAlsKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATIL 163
Cdd:cd03226 71 KSIGYVMQDVDYQL--FT--DSVREELLLGLKELDAGNE--QAETVLKDLDLYA---LKERHPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-243 |
3.68e-29 |
|
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: 115.70 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQ--IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQWQk 80
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlYEPT----SGRILIDGIDLRQIDPASLR- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 lrgRDIAYLVQNPMsMFNpfqkieAHILETI-LSHEKCSkrvaLSKALEWMKRLNLDDAISLLkkyP--FE--------- 148
Cdd:COG2274 549 ---RQIGVVLQDVF-LFS------GTIRENItLGDPDAT----DEEIIEAARLAGLHDFIEAL---PmgYDtvvgeggsn 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELqNNGKTLITVTHDYQLARDLgGQLLVISEGEVVE 228
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVE 689
|
250
....*....|....*
gi 446358294 229 QGQTQAILSNPQHNY 243
Cdd:COG2274 690 DGTHEELLARKGLYA 704
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-240 |
5.27e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.16 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLG-KLTVKQwqkl 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD----SGRIVLNGRDLFtNLPPRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 rgRDIAYLVQNP-----MSMFnpfqkieahilETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGM 153
Cdd:COG1118 75 --RRVGFVFQHYalfphMTVA-----------ENIafgLRVRPPSKAEIRARVEELLELVQLEG---LADRYPSQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQT 232
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTP 218
|
....*...
gi 446358294 233 QAILSNPQ 240
Cdd:COG1118 219 DEVYDRPA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-225 |
3.45e-28 |
|
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: 105.73 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTvKQWQKLRg 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE---PDSGSILIDGEDLTDLE-DELPPLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPmsmfnpfqkieahileTILSHekcskrvalskalewmkrLNLDDAISLLkkypfeLSGGMLQRIMLATIL 163
Cdd:cd03229 76 RRIGMVFQDF----------------ALFPH------------------LTVLENIALG------LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGE 225
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-247 |
4.83e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 107.70 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKG-----VDLGKLTVKQW 78
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD---AGEVHYRMrdgqlRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 QKLRGRDIAYLVQNPMSMFNPFQKIEAHILETILshekcskrvAL---------SKALEWMKRLNLDdaISLLKKYPFEL 149
Cdd:PRK11701 84 RRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLM---------AVgarhygdirATAGDWLERVEID--AARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 150 SGGMLQRIMLATILSLDPQVIILDEPTSAVDChncsTISAILQELQNN-----GKTLITVTHDYQLARDLGGQLLVISEG 224
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGlvrelGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250 260
....*....|....*....|...
gi 446358294 225 EVVEQGQTQAILSNPQHNYTKAL 247
Cdd:PRK11701 229 RVVESGLTDQVLDDPQHPYTQLL 251
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-226 |
1.04e-27 |
|
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: 105.69 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLAKLLVGHIPQGmtvrGNIFFKGVDLGKlTVKQWQKLR 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKsTLLRCINLLEEPDS----GTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNpmsmFNPFqkieAH--ILETI----LSHEKCSKRVALSKALEWMKRLNLDDAISllkKYPFELSGGMLQR 156
Cdd:cd03262 76 -QKVGMVFQQ----FNLF----PHltVLENItlapIKVKGMSKAEAEERALELLEKVGLADKAD---AYPAQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-238 |
1.19e-27 |
|
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: 111.00 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQ-IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQWQKL 81
Cdd:COG4988 336 SIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY---SGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 rgrdIAYLVQNPMsMFNpfqkieAHILETILSHEKCSKRVALSKALEwmkRLNLDDAISLLkkyP-----------FELS 150
Cdd:COG4988 413 ----IAWVPQNPY-LFA------GTIRENLRLGRPDASDEELEAALE---AAGLDEFVAAL---PdgldtplgeggRGLS 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 151 GGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQnNGKTLITVTHDYQLARDlGGQLLVISEGEVVEQG 230
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
....*...
gi 446358294 231 QTQAILSN 238
Cdd:COG4988 554 THEELLAK 561
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-229 |
1.46e-27 |
|
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: 105.63 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQ----IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKltvkqwq 79
Cdd:cd03293 1 LEVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT---SGEVLVDGEPVTG------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 klRGRDIAYLVQNPMSMfnPFQKIeahiLETI---LSHEKCSKRVALSKALEWMKRLNLDDAislLKKYPFELSGGMLQR 156
Cdd:cd03293 71 --PGPDRGYVFQQDALL--PWLTV----LDNValgLELQGVPKAEARERAEELLELVGLSGF---ENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVDCHncstISAILQEL-----QNNGKTLITVTHDYQLARDLGGQLLVISE--GEVVEQ 229
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDAL----TREQLQEElldiwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-231 |
1.63e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.52 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQN 92
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEErPT----SGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 pmsmfnpFQKIE--------AHILETI-LSHEKCSKRVAlskalEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATIL 163
Cdd:COG2884 88 -------FRLLPdrtvyenvALPLRVTgKSRKEIRRRVR-----EVLDLVGLSD---KAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQ 231
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-245 |
2.38e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKL---LVGHIPQGmTVRGNIFFKGVDLGKLTVKQ 77
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEA-RVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 78 wqkLRGR-DIAYLVQNPMSMFNPFQKIE--AHILETILSHEKCSKRV--ALSKALEWmkrlnlDDAISLLKKYPFELSGG 152
Cdd:PRK14247 80 ---LRRRvQMVFQIPNPIPNLSIFENVAlgLKLNRLVKSKKELQERVrwALEKAQLW------DEVKDRLDAPAGKLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQT 232
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
250
....*....|...
gi 446358294 233 QAILSNPQHNYTK 245
Cdd:PRK14247 230 REVFTNPRHELTE 242
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-247 |
2.44e-27 |
|
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: 105.68 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIP--QGMTVRGNIFFKGVDLGKLTVKQWQKL 81
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLApdHGTATYIMRSGAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRDIAYLVQNPMSMFNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAisLLKKYPFELSGGMLQRIMLAT 161
Cdd:TIGR02323 84 MRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPT--RIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 162 ILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241
|
....*..
gi 446358294 241 HNYTKAL 247
Cdd:TIGR02323 242 HPYTQLL 248
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-240 |
3.23e-27 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 105.65 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLL--AKLLVghIPQgmtvRGNIFFKGVDL-------GKL 73
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKsTFLrcINLLE--TPD----SGEIRVGGEEIrlkpdrdGEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 74 TV---KQWQKLRGRdIAYLVQNpmsmFNPFQK-------IEA--HILetilsheKCSKRVALSKALEWMKRLNLDDAisl 141
Cdd:COG4598 83 VPadrRQLQRIRTR-LGMVFQS----FNLWSHmtvlenvIEApvHVL-------GRPKAEAIERAEALLAKVGLADK--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 142 LKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVI 221
Cdd:COG4598 148 RDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFL 227
|
250
....*....|....*....
gi 446358294 222 SEGEVVEQGQTQAILSNPQ 240
Cdd:COG4598 228 HQGRIEEQGPPAEVFGNPK 246
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-177 |
6.79e-27 |
|
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: 101.57 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWqklrGRDIAYLVQNPMsmFN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS---PTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQ--LF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 99 PFQKIEAHILETILSHEKcSKRVALSKALEWMKRLNL-DDAISLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTS 177
Cdd:pfam00005 72 PRLTVRENLRLGLLLKGL-SKREKDARAEEALEKLGLgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-240 |
1.49e-26 |
|
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: 103.19 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQwqklr 82
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPD----SGTILFGGEDATDVPVQE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQN-----PMSMFNPFqkieAHILETILSHEKCSKRVALSKALEWMKRLNLDdaiSLLKKYPFELSGGMLQRI 157
Cdd:cd03296 74 -RNVGFVFQHyalfrHMTVFDNV----AFGLRVKPRSERPPEAEIRAKVHELLKLVQLD---WLADRYPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAIL 236
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
....
gi 446358294 237 SNPQ 240
Cdd:cd03296 226 DHPA 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-234 |
2.18e-26 |
|
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: 102.51 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQI----GEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLAkLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQ 77
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKsTLLG-LLAGlDRPTS----GTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 78 WQKLRGRDIAYLVQNpmsmfnpFQKIeAHI--LETI-LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGML 154
Cdd:COG4181 84 RARLRARHVGFVFQS-------FQLL-PTLtaLENVmLPLELAGRRDARARARALLERVGLGH---RLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 155 QRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQlLVISEGEVVEQGQTQ 233
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAARCDRV-LRLRAGRLVEDTAAT 231
|
.
gi 446358294 234 A 234
Cdd:COG4181 232 A 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-240 |
2.54e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.79 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLAKLLVGHIPQG--MTVRGNIFfkgvDLGKLT-VKQWQKLRgRDIAYL 89
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKsSLLRVLNLLEMPRSgtLNIAGNHF----DFSKTPsDKAIRELR-RNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 90 VQNpmsmFN--PFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDP 167
Cdd:PRK11124 88 FQQ----YNlwPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKP---YADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 168 QVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAiLSNPQ 240
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-247 |
3.27e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.39 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQN 92
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlERPT----SGSVLVDGVDLTALSERELRAAR-RKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 pmsmFN------PFQKIeAHILEtilsHEKCSKRVALSKALEWMKRLNLDDAIsllKKYPFELSGGMLQRIMLATILSLD 166
Cdd:COG1135 91 ----FNllssrtVAENV-ALPLE----IAGVPKAEIRKRVAELLELVGLSDKA---DAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 167 PQVIILDEPTSAVDchnCSTISAILQELQN-NGKTLITV---THDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHN 242
Cdd:COG1135 159 PKVLLCDEATSALD---PETTRSILDLLKDiNRELGLTIvliTHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
....*
gi 446358294 243 YTKAL 247
Cdd:COG1135 236 LTRRF 240
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-247 |
4.70e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 102.56 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLS---------LQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFfkgVDLGKLT 74
Cdd:PRK15112 5 LEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE---PTSGELL---IDDHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 75 VKQWqKLRGRDIAYLVQNPMSMFNPFQKIeAHILE------TILSHEKCSKRVALSkalewMKRLNL--DDAisllKKYP 146
Cdd:PRK15112 79 FGDY-SYRSQRIRMIFQDPSTSLNPRQRI-SQILDfplrlnTDLEPEQREKQIIET-----LRQVGLlpDHA----SYYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 147 FELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGE 225
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
250 260
....*....|....*....|..
gi 446358294 226 VVEQGQTQAILSNPQHNYTKAL 247
Cdd:PRK15112 228 VVERGSTADVLASPLHELTKRL 249
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-230 |
6.04e-26 |
|
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: 101.18 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQwqklrg 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE---PTSGRIYIGGRDVTDLPPKD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQN----P-MSMFnpfQKIeAHILETilshEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIM 158
Cdd:cd03301 72 RDIAMVFQNyalyPhMTVY---DNI-AFGLKL----RKVPKDEIDERVREVAELLQIEH---LLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-226 |
2.16e-25 |
|
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: 98.24 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKltvkQWQKLRG 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP---DSGEIKVLGKDIKK----EPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RdIAYLVQNPMsmfnpfqkieahiletilshekcskrvalskALEWMK-RLNLDdaisllkkypfeLSGGMLQRIMLATI 162
Cdd:cd03230 74 R-IGYLPEEPS-------------------------------LYENLTvRENLK------------LSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 163 LSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-213 |
2.76e-25 |
|
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: 98.22 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIG--EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLGKLTVKQWQK 80
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPT----SGEILIDGVDLRDLDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LrgrdIAYLVQNPMsMFNpfqkieahilETIlshekcskrvalskalewmkRLNLddaisllkkypfeLSGGMLQRIMLA 160
Cdd:cd03228 77 N----IAYVPQDPF-LFS----------GTI--------------------RENI-------------LSGGQRQRIAIA 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQELQnNGKTLITVTHDYQLARD 213
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRD 160
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-246 |
2.96e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.11 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLAKL--LVGHIPqGMTVRGNIFFKGVDLGKLTVKQWQk 80
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKsTLLRCLnrMNDLIP-GARVEGEILLDGEDIYDPDVDVVE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRgRDIAYLVQNPmsmfNPFQKieaHILETILS----HEKCSKRVaLSKALEW-MKRLNL-----DDaislLKKYPFELS 150
Cdd:COG1117 90 LR-RRVGMVFQKP----NPFPK---SIYDNVAYglrlHGIKSKSE-LDEIVEEsLRKAALwdevkDR----LKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 151 GGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
250
....*....|....*.
gi 446358294 231 QTQAILSNPQHNYTKA 246
Cdd:COG1117 236 PTEQIFTNPKDKRTED 251
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-235 |
3.13e-25 |
|
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: 99.95 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGE-VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLR 82
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE---PTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNP-----------------------MSMFNPFQKIEahiletilshekcsKRVALSkALEwmkRLNLDDai 139
Cdd:cd03256 78 -RQIGMIFQQFnlierlsvlenvlsgrlgrrstwRSLFGLFPKEE--------------KQRALA-ALE---RVGLLD-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 140 sLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQL 218
Cdd:cd03256 137 -KAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRI 215
|
250
....*....|....*..
gi 446358294 219 LVISEGEVVEQGQTQAI 235
Cdd:cd03256 216 VGLKDGRIVFDGPPAEL 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-239 |
4.07e-25 |
|
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: 101.65 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQwqk 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT---AGTIYQGGRDITRLPPQK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 lrgRDIAYLVQNpMSMFnPFQKIEAHIlETILSHEKCSKRVALSKALEWMKRLNLDDAislLKKYPFELSGGMLQRIMLA 160
Cdd:TIGR03265 76 ---RDYGIVFQS-YALF-PNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPGS---ERKYPGQLSGGQQQRVALA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 161 TILSLDPQVIILDEPTSAVDC----HNCSTISAILQELqnnGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAIL 236
Cdd:TIGR03265 147 RALATSPGLLLLDEPLSALDArvreHLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY 223
|
...
gi 446358294 237 SNP 239
Cdd:TIGR03265 224 RHP 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-241 |
5.61e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.30 E-value: 5.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQwq 79
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPTS----GEILIGGRDVTDLPPKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 klrgRDIAYLVQNP-----MSMFnpfqkieahilETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSG 151
Cdd:COG3839 75 ----RNIAMVFQSYalyphMTVY-----------ENIafpLKLRKVPKAEIDRRVREAAELLGLED---LLDRKPKQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 152 GMLQRIMLATILSLDPQVIILDEPTSAVDCH----NCSTISAILQELqnnGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKlrveMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
250
....*....|....
gi 446358294 228 EQGQTQAILSNPQH 241
Cdd:COG3839 214 QVGTPEELYDRPAN 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-230 |
1.77e-24 |
|
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: 96.97 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGvdlgkltvKQWQKLRG 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD---SGEVLFDG--------KPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNpmSMFNPFQKIeAHILETILSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATIL 163
Cdd:cd03269 70 NRIGYLPEE--RGLYPKMKV-IDQLVYLAQLKGLKKEEARRRIDEWLERLELSE---YANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-236 |
2.93e-24 |
|
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: 97.46 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQ--GMTVRgnIFfkGVDLGKLTVkqWQkL 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtyGNDVR--LF--GERRGGEDV--WE-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRdIAYlVQNpmSMFNPFQKiEAHILETILS--------HEKCSKRvALSKALEWMKRLNLDDaislLKKYPF-ELSGG 152
Cdd:COG1119 77 RKR-IGL-VSP--ALQLRFPR-DETVLDVVLSgffdsiglYREPTDE-QRERARELLELLGLAH----LADRPFgTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQ 231
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGP 226
|
....*
gi 446358294 232 TQAIL 236
Cdd:COG1119 227 KEEVL 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-240 |
3.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVdlgKLTVKQWQKLRgRDIAYLVQNPMSMF 97
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGiEKVK----SGEIFYNNQ---AITDDNFEKLR-KHIGIVFQNPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 98 --NPFQKIEAHILET-ILSHEKCSKRValSKALEWMKRLNLDDAisllkkYPFELSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:PRK13648 97 vgSIVKYDVAFGLENhAVPYDEMHRRV--SEALKQVDMLERADY------EPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 175 PTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-214 |
4.05e-24 |
|
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: 100.82 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSL-QIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQWQKL 81
Cdd:TIGR02857 321 SLEFSGVSVaYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 rgrdIAYLVQNPMsMFnpfqkiEAHILETILSHEKCSKRVALSKALEwmkRLNLDDAIS--------LLKKYPFELSGGM 153
Cdd:TIGR02857 398 ----IAWVPQHPF-LF------AGTIAENIRLARPDASDAEIREALE---RAGLDEFVAalpqgldtPIGEGGAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQnNGKTLITVTHDYQLARDL 214
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA 523
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-218 |
5.48e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 5.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQWQKLRGRDIAYLVQNpMSM 96
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTS----GDVIFNGQPMSKLSSAAKAELRNQKLGFIYQF-HHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNPFQKIEAHILETILSHEKCSKrvALSKALEWMKRLNLDDAIsllKKYPFELSGGMLQRIMLATILSLDPQVIILDEPT 176
Cdd:PRK11629 99 LPDFTALENVAMPLLIGKKKPAE--INSRALEMLAAVGLEHRA---NHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446358294 177 SAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQL 218
Cdd:PRK11629 174 GNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-241 |
8.65e-24 |
|
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: 99.84 E-value: 8.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQI--GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKL 81
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD---PQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 rgrdIAYLVQNPmSMFNpfqkieAHILETIL------SHEkcskrvALSKALEwmkRLNLDDaisLLKKYP--------- 146
Cdd:COG4987 411 ----IAVVPQRP-HLFD------TTLRENLRlarpdaTDE------ELWAALE---RVGLGD---WLAALPdgldtwlge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 147 --FELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHncsTISAILQELQN--NGKTLITVTHDyQLARDLGGQLLVIS 222
Cdd:COG4987 468 ggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAA---TEQALLADLLEalAGRTVLLITHR-LAGLERMDRILVLE 543
|
250
....*....|....*....
gi 446358294 223 EGEVVEQGQTQAILSNPQH 241
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGR 562
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-247 |
1.17e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.57 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 2 EQLEIRKLSLQIGevpvLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKL 81
Cdd:PRK10070 31 KEQILEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE---PTRGQVLIDGVDIAKISDAELREV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRDIAYLVQNpMSMFNPFQKIEAHILETILSHEKCSKRvaLSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLAT 161
Cdd:PRK10070 104 RRKKIAMVFQS-FALMPHMTVLDNTAFGMELAGINAEER--REKALDALRQVGLEN---YAHSYPDELSGGMRQRVGLAR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 162 ILSLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK10070 178 ALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
....*..
gi 446358294 241 HNYTKAL 247
Cdd:PRK10070 258 NDYVRTF 264
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-230 |
2.33e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.75 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHiPQGMTVRGNIFFKGVDLGKLTVKQwqklRG 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEVTSGSILLDGEDILELSPDE----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RD-IAYLVQNP-----MSMFNpfqkieahILETILSH---EKCSKRVALSKALEWMKRLNLDDaiSLLKKYPFE-LSGGM 153
Cdd:COG0396 76 RAgIFLAFQYPveipgVSVSN--------FLRTALNArrgEELSAREFLKLLKEKMKELGLDE--DFLDRYVNEgFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHdYQlardlggQLL---------VISEG 224
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH-YQ-------RILdyikpdfvhVLVDG 217
|
....*.
gi 446358294 225 EVVEQG 230
Cdd:COG0396 218 RIVKSG 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-237 |
5.14e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLL---AKLLvghipqgMTVRGNIFFKGVDLGKLTVKQW 78
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKsTLLkcfARLL-------TPQSGTVFLGDKPISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 qklrGRDIAYLVQNPMSmfnP----FQKIEAHILETILSH-----EKCSKRVALSkalewMKRLNLDDaisLLKKYPFEL 149
Cdd:PRK11231 75 ----ARRLALLPQHHLT---PegitVRELVAYGRSPWLSLwgrlsAEDNARVNQA-----MEQTRINH---LADRRLTDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 150 SGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQ 229
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
....*...
gi 446358294 230 GQTQAILS 237
Cdd:PRK11231 220 GTPEEVMT 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-239 |
7.38e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.54 E-value: 7.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVkqwqklRG 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT---SGHIRFHGTDVSRLHA------RD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQN-----PMSMFNPFqkieAHILETILSHEKCSKRVALSKALEWMKRLNLDdaiSLLKKYPFELSGGMLQRIM 158
Cdd:PRK10851 74 RKVGFVFQHyalfrHMTVFDNI----AFGLTVLPRRERPNAAAIKAKVTQLLEMVQLA---HLADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGK-TLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
..
gi 446358294 238 NP 239
Cdd:PRK10851 227 EP 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-240 |
1.30e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.71 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVDLGKLTVkqWQkLRGRdIAYLVQNPM 94
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTV--WD-IREK-VGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 95 SMF--NPFQKIEAHILET-ILSHEKCSKRVAlsKALEWMKRLNLDDAisllkkYPFELSGGMLQRIMLATILSLDPQVII 171
Cdd:PRK13640 95 NQFvgATVGDDVAFGLENrAVPRPEMIKIVR--DVLADVGMLDYIDS------EPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 172 LDEPTSAVDCHNCSTISAILQELQN-NGKTLITVTHDYQLArDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-225 |
1.33e-22 |
|
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: 92.31 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQI-GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGhipQGMTVRGNIFFKGVDLgkltvkqwQKLR 82
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYG---ALTPSRGQVRIAGEDV--------NRLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLVQNPMSMFNPFQkieahiletILSHEKCSKRVALS------KALEWMKRLN-LDDAISLLKK---YPFELSGG 152
Cdd:TIGR02673 71 GRQLPLLRRRIGVVFQDFR---------LLPDRTVYENVALPlevrgkKEREIQRRVGaALRQVGLEHKadaFPEQLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGE 225
Cdd:TIGR02673 142 EQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-249 |
2.04e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIP---QGMTVRGNIFFKGVDLGKLTVKqwqK 80
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQIDAI---K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRgRDIAYLVQNPmsmfNPFQKIEAH--ILETILSHEKCSKRVALSKALEWMKRLNL-DDAISLLKKYPFELSGGMLQRI 157
Cdd:PRK14246 88 LR-KEVGMVFQQP----NPFPHLSIYdnIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
250
....*....|..
gi 446358294 238 NPQHNYTKALTV 249
Cdd:PRK14246 242 SPKNELTEKYVI 253
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-240 |
2.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.36 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIpqgMTVRGNIFFKGVDLGKLTV-KQWQKLRgRDIAYLVQNPMSmf 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALL---KPSSGTITIAGYHITPETGnKNLKKLR-KKVSLVFQFPEA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 98 npfQKIEAHILETILSHEK---CSKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:PRK13641 97 ---QLFENTVLKDVEFGPKnfgFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 175 PTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-240 |
2.27e-22 |
|
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: 92.11 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVkqwQKLRG 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDITGLPP---HEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPmsmfNPFQK--------IEAHILE---TILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKypfELSGG 152
Cdd:cd03219 75 LGIGRTFQIP----RLFPEltvlenvmVAAQARTgsgLLLARARREEREARERAEELLERVGLADLADRPAG---ELSYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQT 232
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
....*...
gi 446358294 233 QAILSNPQ 240
Cdd:cd03219 228 DEVRNNPR 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-207 |
3.42e-22 |
|
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: 91.00 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKLTVKqwqklR 82
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP---SAGEVLWNGEPIRDARED-----Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLVQNPMsmFNPFQKIeahiLETILSHEKCSK-RVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLAT 161
Cdd:COG4133 74 RRRLAYLGHADG--LKPELTV----RENLRFWAALYGlRADREAIDEALEAVGLAG---LADLPVRQLSAGQKRRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446358294 162 ILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD 207
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-230 |
4.80e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 90.73 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVkqwQKLRgRDIAYLVQNP 93
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPT----SGSVLLDGTDIRQLDP---ADLR-RNIGYVPQDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MsMFnpFQKIEAHILETILSHEkcSKRValskaLEWMKRLNLDDaisLLKKYP-----------FELSGGMLQRIMLATI 162
Cdd:cd03245 88 T-LF--YGTLRDNITLGAPLAD--DERI-----LRAAELAGVTD---FVNKHPngldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 163 LSLDPQVIILDEPTSAVDchnCSTISAILQELQN--NGKTLITVTHDYQLArDLGGQLLVISEGEVVEQG 230
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD---MNSEERLKERLRQllGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-239 |
5.04e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 12 QIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVRGNIFFKGVDLGKLT---------VKQWQKL 81
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGTIQVGDIYIGDKKNNHElitnpyskkIKNFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RgRDIAYLVQnpmsmFNPFQKIEAHILETILSHE---KCSKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIM 158
Cdd:PRK13631 115 R-RRVSMVFQ-----FPEYQLFKDTIEKDIMFGPvalGVKKSEAKKLAKFYLNKMGLDD--SYLERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSN 238
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD 266
|
.
gi 446358294 239 P 239
Cdd:PRK13631 267 Q 267
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-237 |
5.79e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.00 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLGKLTVkqWQkLRgRDIAYLVQNP 93
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPE----AGTITVGGMVLSEETV--WD-VR-RQVGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMF--NPFQKIEAHILETI-LSHEKCSKRVAlskalEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQVI 170
Cdd:PRK13635 91 DNQFvgATVQDDVAFGLENIgVPREEMVERVD-----QALRQVGMED---FLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 171 ILDEPTSAVDCHNCSTISAILQELQNNGK-TLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-244 |
7.66e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.99 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLL--VGHIPQGMTVRGNIFFKGVDLGKLTVKQWQkL 81
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYSPRTDTVD-L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RgRDIAYLVQNPmsmfNPFqkiEAHILETIL-------SHEKCSKRVALSKAL-------EWMKRLNlDDAISllkkypf 147
Cdd:PRK14239 85 R-KEIGMVFQQP----NPF---PMSIYENVVyglrlkgIKDKQVLDEAVEKSLkgasiwdEVKDRLH-DSALG------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 148 eLSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:PRK14239 149 -LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
250
....*....|....*..
gi 446358294 228 EQGQTQAILSNPQHNYT 244
Cdd:PRK14239 227 EYNDTKQMFMNPKHKET 243
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-230 |
9.86e-22 |
|
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: 90.36 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQWQKLrgrdIAYLVQN 92
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfYDPQ----KGQILIDGIDIRDISRKSLRSM----IGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 PMsMFNpfqkieAHILETI-LSHEKCSKRVALSKAlewmKRLNLDDAISLLKK----YPFE----LSGGMLQRIMLATIL 163
Cdd:cd03254 86 TF-LFS------GTIMENIrLGRPNATDEEVIEAA----KEAGAHDFIMKLPNgydtVLGEnggnLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELqNNGKTLITVTHDYQLARDlGGQLLVISEGEVVEQG 230
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-206 |
1.08e-21 |
|
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: 88.81 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIG--EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIpqgMTVRGNIFFKGVDLGKLTVKQWqkl 81
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL---RPTSGRVRLDGADISQWDPNEL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 rGRDIAYLVQNpMSMFnpfqkiEAHILETIlshekcskrvalskalewmkrlnlddaisllkkypfeLSGGMLQRIMLAT 161
Cdd:cd03246 75 -GDHVGYLPQD-DELF------SGSIAENI-------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446358294 162 ILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTH 206
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-237 |
1.19e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 90.24 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGkLTVKQWqkLRgRDIAYLVQNPMsM 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfYVPE----NGRVLVDGHDLA-LADPAW--LR-RQVGVVLQENV-L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNPFQKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPT 176
Cdd:cd03252 88 FNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYD-TIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 177 SAVDCHncsTISAILQELQN--NGKTLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAILS 237
Cdd:cd03252 167 SALDYE---SEHAIMRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-243 |
1.50e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLGKLTvkqwqKLRG-RDIAYLV-QNP 93
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQ----KGKVLVSGIDTGDFS-----KLQGiRKLVGIVfQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMFnpfqkieahILETILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKY----PFELSGGMLQRIMLATILSLDPQV 169
Cdd:PRK13644 87 ETQF---------VGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 170 IILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAILSNPQHNY 243
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-240 |
1.56e-21 |
|
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: 89.60 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGhipqgmtvrgnifFKGVDLGKLTvkqwqkLRG 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-------------FETPTSGEIL------LDG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMSMFNPFQK--IEAH--ILETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQR 156
Cdd:cd03300 62 KDITNLPPHKRPVNTVFQNyaLFPHltVFENIafgLRLKKLPKAEIKERVAEALDLVQLEG---YANRKPSQLSGGQQQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAI 235
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
....*
gi 446358294 236 LSNPQ 240
Cdd:cd03300 219 YEEPA 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-230 |
1.56e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.31 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQWQKLrgrdIAYLVQN 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfYDPTS----GRILIDGVDIRDLTLESLRRQ----IGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 PMsMFNpfqkieahilETILSHekcskrVALSKA-------LEWMKRLNLDDAISLL-KKYPFE-------LSGGMLQRI 157
Cdd:COG1132 423 TF-LFS----------GTIREN------IRYGRPdatdeevEEAAKAAQAHEFIEALpDGYDTVvgergvnLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDchncsTIS--AILQELQNN--GKTLITVTH--------DyqlardlggQLLVISEGE 225
Cdd:COG1132 486 AIARALLKDPPILILDEATSALD-----TETeaLIQEALERLmkGRTTIVIAHrlstirnaD---------RILVLDDGR 551
|
....*
gi 446358294 226 VVEQG 230
Cdd:COG1132 552 IVEQG 556
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-227 |
1.87e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.25 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKlSLQIGE--VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLvGHIPQGMTvrGNIFFKGVDLGKLTVKQW 78
Cdd:PRK10535 5 LELKDIRR-SYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKPTS--GTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 QKLRGRDIAYLVQ--NPMSMFNPFQKIEAHILetilsHEKCSKRVALSKALEWMKRLNLDDAISLlkkYPFELSGGMLQR 156
Cdd:PRK10535 81 AQLRREHFGFIFQryHLLSHLTAAQNVEVPAV-----YAGLERKQRLLRAQELLQRLGLEDRVEY---QPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDlGGQLLVISEGEVV 227
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-230 |
3.10e-21 |
|
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: 88.40 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGeSLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDlgklTVKQWQKLRG 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP---SSGTIRIDGQD----VLKQPQKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RdIAYLVQNPMsmFNPFQKIEAHiLETILSHEKCSKRVALSKALEWMKRLNLDDAislLKKYPFELSGGMLQRIMLATIL 163
Cdd:cd03264 73 R-IGYLPQEFG--VYPNFTVREF-LDYIAWLKGIPSKEVKARVDEVLELVNLGDR---AKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-211 |
3.56e-21 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 87.86 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKG--VDLGKLTVKQWQklrgRDIAYLV 90
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLrPQS----GAVLIDGepLDYSRKGLLERR----QRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 91 QNP-MSMFNP--FQKIEAHILETILSHEKCSKRValSKALEwmkrlnLDDAISLLKKYPFELSGGMLQRIMLATILSLDP 167
Cdd:TIGR01166 75 QDPdDQLFAAdvDQDVAFGPLNLGLSEAEVERRV--REALT------AVGASGLRERPTHCLSGGEKKRVAIAGAVAMRP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446358294 168 QVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLA 211
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-240 |
3.64e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGK-TLLAKLLVGHIPQgmtvRGNIFFKGVDLGKLTVKqWqkLRGRdIAYLVQNPMSmf 97
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKsTLLLHLNGIYLPQ----RGRVKVMGREVNAENEK-W--VRSK-VGLVFQDPDD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 98 npfQKIEAHILETI--------LSHEKCSKRVAlskalEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQV 169
Cdd:PRK13647 91 ---QVFSSTVWDDVafgpvnmgLDKDEVERRVE-----EALKAVRMWD---FRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 170 IILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQaILSNPQ 240
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDED 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-226 |
6.25e-21 |
|
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: 87.85 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQI-GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIpqgMTVRGNIFFKGVDLGKLtvkqwqklR 82
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE---LPTSGTIRVNGQDVSDL--------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLVQNPMSMFNPFQkieahiletILSHEKCSKRVALS------KALEWMKR----LNLDDAISLLKKYPFELSGG 152
Cdd:cd03292 70 GRAIPYLRRKIGVVFQDFR---------LLPDRNVYENVAFAlevtgvPPREIRKRvpaaLELVGLSHKHRALPAELSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:cd03292 141 EQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-240 |
6.62e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.98 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLgKLTVKQWQKLRgRDIAYLVQNP-MS 95
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPT----SGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNPdDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 96 MFNPF--QKIEAHILETILSHEKCSKRVAlskalEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQVIILD 173
Cdd:PRK13639 91 LFAPTveEDVAFGPLNLGLSKEEVEKRVK-----EALKAVGMEG---FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 174 EPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-229 |
6.94e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 6.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQ----IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIP--------QGMTVRGniffKGV 68
Cdd:COG4525 1 MSMLTVRHVSVRypggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLApssgeitlDGVPVTG----PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 69 DLGklTVKQ------WQ----------KLRGRDiaylvqnpmsmfnpfqKIEAHiletilshekcskrvalSKALEWMKR 132
Cdd:COG4525 77 DRG--VVFQkdallpWLnvldnvafglRLRGVP----------------KAERR-----------------ARAEELLAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 133 LNLDDAIsllKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLA 211
Cdd:COG4525 122 VGLADFA---RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA 198
|
250 260
....*....|....*....|
gi 446358294 212 RDLGGQLLVIS--EGEVVEQ 229
Cdd:COG4525 199 LFLATRLVVMSpgPGRIVER 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-243 |
9.35e-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: 87.98 E-value: 9.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLvghipqgmtVR------GNIFFKGVDLGKLTVKQWQKLrgrdIAY 88
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---------ERfydptsGEILLDGVDIRDLNLRWLRSQ----IGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 89 LVQNPMsMFNpfqkieAHILETILShekCSKRVALSKALEWMKRLNLDDAI-SLLKKYP-------FELSGGMLQRIMLA 160
Cdd:cd03249 82 VSQEPV-LFD------GTIAENIRY---GKPDATDEEVEEAAKKANIHDFImSLPDGYDtlvgergSQLSGGQKQRIAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNcstiSAILQELQNN---GKTLITVTHDYQLAR--DLggqLLVISEGEVVEQGQTQAI 235
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAES----EKLVQEALDRamkGRTTIVIAHRLSTIRnaDL---IAVLQNGQVVEQGTHDEL 224
|
....*...
gi 446358294 236 LSNPQHNY 243
Cdd:cd03249 225 MAQKGVYA 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-241 |
2.48e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.51 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTvkqwqklrg 83
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD---HGEILFDGENIPAMS--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMSMF----------NPFQKIEAHILEtilsHEKCSKRVALSKALEWMKRLNLDDAISLLkkyPFELSGGM 153
Cdd:PRK11831 76 RSRLYTVRKRMSMLfqsgalftdmNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQT 232
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
....*....
gi 446358294 233 QAILSNPQH 241
Cdd:PRK11831 229 QALQANPDP 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-240 |
3.06e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.38 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVRgniffkgvdLGKLTV------KQWQKLRGRdiAYLVq 91
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSGTVT---------IGERVItagkknKKLKPLRKK--VGIV- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 92 npmsmfnpFQKIEAHILETILSHEKC--------SKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIMLATIL 163
Cdd:PRK13634 91 --------FQFPEHQLFEETVEKDICfgpmnfgvSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-237 |
3.14e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.48 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFK----GVDLGKLTVK 76
Cdd:TIGR03269 282 VRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE---PTSGEVNVRvgdeWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 77 qwqkLRGRDIAYL--VQNPMSMFnPFQKIEAHILETIlSHEkCSKRVALSKALEWMKRLNLDD--AISLLKKYPFELSGG 152
Cdd:TIGR03269 359 ----GRGRAKRYIgiLHQEYDLY-PHRTVLDNLTEAI-GLE-LPDELARMKAVITLKMVGFDEekAEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTIS-AILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQ 231
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 446358294 232 TQAILS 237
Cdd:TIGR03269 512 PEEIVE 517
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-211 |
3.76e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.99 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGE----VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGhIPQGMTvrGNIFFKGVDLGKLTVKQWQ 79
Cdd:PRK10584 7 VEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAG-LDDGSS--GEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 KLRGRDIAYLVQNPM--SMFNPFQKIEahiLETILSHEkcSKRVALSKALEWMKRLNLDDAislLKKYPFELSGGMLQRI 157
Cdd:PRK10584 84 KLRAKHVGFVFQSFMliPTLNALENVE---LPALLRGE--SSRQSRNGAKALLEQLGLGKR---LDHLPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLA 211
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLA 210
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-237 |
3.88e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 89.33 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 13 IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLgkltvKQW-QKLRGRDIAYLVQ 91
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP---PTSGSVRLDGADL-----KQWdRETFGKHIGYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 92 NpmsmfnpFQKIEAHILETI------LSHEKCSKRVALSKALEWMKRL--NLDDAISLLKKypfELSGGMLQRIMLATIL 163
Cdd:TIGR01842 400 D-------VELFPGTVAENIarfgenADPEKIIEAAKLAGVHELILRLpdGYDTVIGPGGA---TLSGGQRQRIALARAL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLArDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLA 542
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-213 |
4.01e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVRgniffkgvdlgkltvkqwqKLRGRDIAYLVQN 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLrPTSGTVR-------------------RAGGARVAYVPQR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 ---PMSMfnPFQKIEAHILET-----ILSHEKCSKRVALSKALEwmkRLNLDDaislLKKYPF-ELSGGMLQRIMLATIL 163
Cdd:NF040873 64 sevPDSL--PLTVRDLVAMGRwarrgLWRRLTRDDRAAVDDALE---RVGLAD----LAGRQLgELSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARD 213
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-257 |
4.33e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.09 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLGKLTVkqwqklr 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDS----GEVLWDGEPLDPEDR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLvqnP--------MsmfnpfqKIEAHI-----LETIlshekcSKRVALSKALEWMKRLNL----DDAISllkky 145
Cdd:COG4152 71 -RRIGYL---PeerglypkM-------KVGEQLvylarLKGL------SKAEAKRRADEWLERLGLgdraNKKVE----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 146 pfELSGGMLQRI-MLATILSlDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEG 224
Cdd:COG4152 129 --ELSKGNQQKVqLIAALLH-DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKG 205
|
250 260 270
....*....|....*....|....*....|...
gi 446358294 225 EVVEQGQTQAILSnpQHnytKALTVQMEYEGDI 257
Cdd:COG4152 206 RKVLSGSVDEIRR--QF---GRNTLRLEADGDA 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-223 |
4.74e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.23 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLAkLLVGHIPQGMTVRGNIFFKGVDLGKLTVKQwqklr 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKsTLLA-AIAGTLSPAFSASGEVLLNGRRLTALPAEQ----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNPMsmFNPFQKIEAHIL----ETILSHEKcskRVALSKALEwmkRLNLDDaisLLKKYPFELSGGMLQRIM 158
Cdd:COG4136 76 -RRIGILFQDDL--LFPHLSVGENLAfalpPTIGRAQR---RARVEQALE---EAGLAG---FADRDPATLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISA-ILQELQNNGKTLITVTHDYQLARDlGGQLLVISE 223
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-245 |
4.76e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.43 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLL--VGHIPQGMTVRGNIFFKGVDLGKLTVKQWQKL 81
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRDIAYLVQNPMSMFNPFQK--IEAHILETILSHEKCSKRV--ALSKALEWmkrlnlDDAISLLKKYPFELSGGMLQRI 157
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNvaIGVKLNGLVKSKKELDERVewALKKAALW------DEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
....*...
gi 446358294 238 NPQHNYTK 245
Cdd:PRK14267 238 NPEHELTE 245
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-230 |
4.80e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.79 E-value: 4.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVdlgKLTVKQWQKlrgrDIAYLVQNpmSMF 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQ---PRKPDQFQK----CVAYVRQD--DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 98 NPFQKIEAHILET-ILSHEKCSKRVALSK--ALEWMKRLNLDDAISLLKKYpfeLSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:cd03234 93 LPGLTVRETLTYTaILRLPRKSSDAIRKKrvEDVLLRDLALTRIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 175 PTSAVDCHNCSTISAILQELQNNGKTLITVTHD-----YQLARDlggqLLVISEGEVVEQG 230
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQprsdlFRLFDR----ILLLSSGEIVYSG 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-237 |
6.31e-20 |
|
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: 88.65 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQI--GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLgkltvKQWQK 80
Cdd:COG4618 330 RLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP---PTAGSVRLDGADL-----SQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 -LRGRDIAYLVQNP-------------MSMFNPFQKIEA------HilETILShekcskrvaLSKALEwmKRLNLDDAIs 140
Cdd:COG4618 402 eELGRHIGYLPQDVelfdgtiaeniarFGDADPEKVVAAaklagvH--EMILR---------LPDGYD--TRIGEGGAR- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 141 llkkypfeLSGGMLQRIMLATILSLDPQVIILDEPTSAVDchncSTISAIL----QELQNNGKTLITVTHDYQLAR--Dl 214
Cdd:COG4618 468 --------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLD----DEGEAALaaaiRALKARGATVVVITHRPSLLAavD- 534
|
250 260
....*....|....*....|...
gi 446358294 215 ggQLLVISEGEVVEQGQTQAILS 237
Cdd:COG4618 535 --KLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-230 |
7.65e-20 |
|
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: 84.85 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVlrDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQwqklr 82
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQS----GRVLINGVDVTAAPPAD----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQ--NPMSMFNPFQKIEAHILETIlsHEKCSKRVALSKALewmKRLNLDDaisLLKKYPFELSGGMLQRIMLA 160
Cdd:cd03298 70 -RPVSMLFQenNLFAHLTVEQNVGLGLSPGL--KLTAEDRQAIEVAL---ARVGLAG---LEKRLPGELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-238 |
8.50e-20 |
|
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: 84.79 E-value: 8.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLtvKQWQKLRg 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---PRSGSIRFDGRDITGL--PPHERAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQN-----PMSmfnpfqkieahILETILSHEKCSKRVALSKALEWMKRL--NLDDaisLLKKYPFELSGGmlQR 156
Cdd:cd03224 75 AGIGYVPEGrrifpELT-----------VEENLLLGAYARRRAKRKARLERVYELfpRLKE---RRKQLAGTLSGG--EQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLAtI---LSLDPQVIILDEPT-----SAVDchncsTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVE 228
Cdd:cd03224 139 QMLA-IaraLMSRPKLLLLDEPSeglapKIVE-----EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVL 212
|
250
....*....|
gi 446358294 229 QGQTQAILSN 238
Cdd:cd03224 213 EGTAAELLAD 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-240 |
8.93e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 85.48 E-value: 8.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLGKLTVkqwQKLR 82
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYrPTS----GRILFDGRDITGLPP---HRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLVQNP-----MS-----MFNPFQKIEAHILETILSHEKCSK--RVALSKALEWMKRLNLDDaisLLKKYPFELS 150
Cdd:COG0411 78 RLGIARTFQNPrlfpeLTvlenvLVAAHARLGRGLLAALLRLPRARReeREARERAEELLERVGLAD---RADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 151 GGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQ 229
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
250
....*....|.
gi 446358294 230 GQTQAILSNPQ 240
Cdd:COG0411 235 GTPAEVRADPR 245
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-247 |
9.25e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.78 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQ- 91
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlERPTS----GRVLVDGQDLTALSEKELRKAR-RQIGMIFQh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 92 -NPMSMFNPFQKIeAHILETI-LSHEKCSKRVAlskalEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQV 169
Cdd:PRK11153 91 fNLLSSRTVFDNV-ALPLELAgTPKAEIKARVT-----ELLELVGLSD---KADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 170 IILDEPTSAVDchnCSTISAILQELQNNGKTL-ITV---THDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYTK 245
Cdd:PRK11153 162 LLCDEATSALD---PATTRSILELLKDINRELgLTIvliTHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
..
gi 446358294 246 AL 247
Cdd:PRK11153 239 EF 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-238 |
1.61e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI--PQGMTVRGNIffkGVDLGKLTVKQWQKLRgRDIAYLVQN 92
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisETGQTIVGDY---AIPANLKKIKEVKRLR-KEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 PMsmFNPFQK-IEAHILETILsHEKCSKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIMLATILSLDPQVII 171
Cdd:PRK13645 99 PE--YQLFQEtIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 172 LDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSN 238
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-230 |
1.63e-19 |
|
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: 84.59 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVkqwQKLRgRDIAYLVQNp 93
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfYDVSS----GSILIDGQDIREVTL---DSLR-RAIGVVPQD- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMFNpfqkieahilETILsHEKCSKRVALSKA--LEWMKRLNLDDAIsllKKYPF-----------ELSGGMLQRIMLA 160
Cdd:cd03253 84 TVLFN----------DTIG-YNIRYGRPDATDEevIEAAKAAQIHDKI---MRFPDgydtivgerglKLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 161 -TILSlDPQVIILDEPTSAVDCHNCSTISAILQELqNNGKTLITVTHDYQLARDlGGQLLVISEGEVVEQG 230
Cdd:cd03253 150 rAILK-NPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-244 |
1.94e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 33 TIIGESGSGKTLLAKLL--VGHIPQGMTVRGNIFFKGVDLgkLTVKQWQKLRgRDIAYLVQNPmsmfNPF-QKIEAHILE 109
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLnrMNDKVSGYRYSGDVLLGGRSI--FNYRDVLEFR-RRVGMLFQRP----NPFpMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 110 TILSHEKCSKRVALSKALEWMKRLNLDDAIS-LLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTIS 188
Cdd:PRK14271 124 GVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 189 AILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNYT 244
Cdd:PRK14271 204 EFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-237 |
3.19e-19 |
|
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: 83.43 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLlvghIPQGMTV-RGNIFFKGVDLGKLTVKQwqkLRgRDIAYLVQNP 93
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNL----IPRFYDVdSGRILIDGHDVRDYTLAS---LR-RQIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MsMFNpfqkieAHILETIL------SHEKCSKRVALSKALEWMKRL--NLDDAISllkKYPFELSGGMLQRIMLATILSL 165
Cdd:cd03251 86 F-LFN------DTVAENIAygrpgaTREEVEEAARAANAHEFIMELpeGYDTVIG---ERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 166 DPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAILS 237
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKN-RTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-230 |
3.76e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 86.72 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIG-EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQwqkLR 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR---SGEILLNGFSLKDIDRHT---LR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNPMsMFNpfqkieAHILETILSHEKcsKRVALSKALEWMKRLNLDDAI--------SLLKKYPFELSGGML 154
Cdd:TIGR01193 548 -QFINYLPQEPY-IFS------GSILENLLLGAK--ENVSQDEIWAACEIAEIKDDIenmplgyqTELSEEGSSISGGQK 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 155 QRIMLATILSLDPQVIILDEPTSAVDchnCSTISAILQELQN-NGKTLITVTHDYQLARdLGGQLLVISEGEVVEQG 230
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLD---TITEKKIVNNLLNlQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQG 690
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-230 |
4.31e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 84.33 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKqWQKLRGRdIAYLVQNPmsmfn 98
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK---PTSGKIIIDGVDITDKKVK-LSDIRKK-VGLVFQYP----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 99 PFQKIEAHILETI--------LSHEKCSKRValSKALEwMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQVI 170
Cdd:PRK13637 93 EYQLFEETIEKDIafgpinlgLSEEEIENRV--KRAMN-IVGLDYED---YKDKSPFELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 171 ILDEPTSAVDCHNCSTISAILQELQNNGK-TLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-239 |
7.52e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.67 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 26 IDMGESLTIIGESGSGKTLLAKLLVGHIPqgmtVRGNIFFKGVDLGKLTVKQWQKlrgrDIAYLVQNPmsmfnpfQKIEA 105
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFLP----YQGSLKINGIELRELDPESWRK----HLSWVGQNP-------QLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 106 HILETIL------SHEKCSKRVALSKALEWMKRLN--LDDAISllkkypfE----LSGGMLQRIMLATILSLDPQVIILD 173
Cdd:PRK11174 438 TLRDNVLlgnpdaSDEQLQQALENAWVSEFLPLLPqgLDTPIG-------DqaagLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 174 EPTSAVDCHNcstISAILQELQNN--GKTLITVTHdyQLArDLGG--QLLVISEGEVVEQGQTQAILSNP 239
Cdd:PRK11174 511 EPTASLDAHS---EQLVMQALNAAsrRQTTLMVTH--QLE-DLAQwdQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-230 |
8.45e-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: 81.80 E-value: 8.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHiPQGMTVRGNIFFKGVDLGKLTVKQwqklRG 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVTEGEILFKGEDITDLPPEE----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RdiaylvqnpMSMFNPFQKIEahiletilshekcskRVALSKALEWMKRLNLDdaisllkkypfeLSGGMLQRIMLATIL 163
Cdd:cd03217 76 R---------LGIFLAFQYPP---------------EIPGVKNADFLRYVNEG------------FSGGEKKRNEILQLL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLL-VISEGEVVEQG 230
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSG 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-228 |
9.92e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 9.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVRgniffkgvdLGKlTVKqwqklr 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePDSGTVK---------LGE-TVK------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 grdIAYLVQNpMSMFNPfqkieahiletilshekcSKRValskaLEWMKRLNLDD----AISLLKKYPF----------E 148
Cdd:COG0488 380 ---IGYFDQH-QEELDP------------------DKTV-----LDELRDGAPGGteqeVRGYLGRFLFsgddafkpvgV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHncsTISAILQELQN-NGkTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE---TLEALEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
.
gi 446358294 228 E 228
Cdd:COG0488 509 E 509
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-244 |
1.01e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.50 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPqgmtVRGNIFFKGVDLGKLTVKQwqklr 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP----TAGQIMLDGVDLSHVPPYQ----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNpMSMFnPFQKIEAHIL----ETILSHEKCSKRVALSKALEWMKRLnlddaislLKKYPFELSGGMLQRIM 158
Cdd:PRK11607 91 -RPINMMFQS-YALF-PHMTVEQNIAfglkQDKLPKAEIASRVNEMLGLVHMQEF--------AKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTIS-AILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
....*..
gi 446358294 238 NPQHNYT 244
Cdd:PRK11607 240 HPTTRYS 246
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-228 |
1.13e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLgkltvkqwqKLRG 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPV---------EGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMSMfnPFQKIEAHIlETILSHEKCSKRVALSKALEWMKRLNLDDAislLKKYPFELSGGMLQRIMLATIL 163
Cdd:PRK11248 70 AERGVVFQNEGLL--PWRNVQDNV-AFGLQLAGVEKMQRLEIAHQMLKKVGLEGA---EKRYIWQLSGGQRQRVGIARAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVIS--EGEVVE 228
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-207 |
2.45e-18 |
|
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: 80.94 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLS------LQIG-EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFK----GVDLG 71
Cdd:COG4778 5 LEVENLSktftlhLQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDS----GSILVRhdggWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 72 KLTVKQWQKLRGRDIAYLVQnpmsmF---NPFQKIEAHILETILSHEkCSKRVALSKALEWMKRLNLDDAisLLKKYPFE 148
Cdd:COG4778 81 QASPREILALRRRTIGYVSQ-----FlrvIPRVSALDVVAEPLLERG-VDREEARARARELLARLNLPER--LWDLPPAT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD 207
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHD 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-235 |
2.66e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.10 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIP-QGMTVRGNIFFKGVDLGKlTVKQWQKLRGrdiayLVqn 92
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGlHVPtQGSVRVDDTLITSTSKNK-DIKQIRKKVG-----LV-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 pmsmfnpFQKIEAHIL-ETIL-------SHEKCSKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIMLATILS 164
Cdd:PRK13649 91 -------FQFPESQLFeETVLkdvafgpQNFGVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 165 LDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAI 235
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-237 |
3.21e-18 |
|
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: 83.70 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGhIPQGMTVRGNIFFK----------------- 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG-MDQYEPTSGRIIYHvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 67 -------------GVDLGKLTVKQWQKLRGRdIAYLVQNPMSMFNPFQKIEaHILETiLSHEKCSKRVALSKALEWMKRL 133
Cdd:TIGR03269 80 epcpvcggtlepeEVDFWNLSDKLRRRIRKR-IAIMLQRTFALYGDDTVLD-NVLEA-LEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 134 NLDDAISLLKKypfELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTI-SAILQELQNNGKTLITVTHDYQLAR 212
Cdd:TIGR03269 157 QLSHRITHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhNALEEAVKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*
gi 446358294 213 DLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-233 |
3.33e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVDLGKltvkqwQKLRGRDiAYLVQNpmSMFN 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDA------KEMRAIS-AYVQQD--DLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 99 PFQKIEAHIleTILSHEKCSKRVALSKALEWMK----RLNLDDAISLLKKYPFE---LSGGMLQRIMLATILSLDPQVII 171
Cdd:TIGR00955 112 PTLTVREHL--MFQAHLRMPRRVTKKEKRERVDevlqALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 172 LDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD--YQLArDLGGQLLVISEGEVVEQGQTQ 233
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELF-ELFDKIILMAEGRVAYLGSPD 252
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-239 |
3.57e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMtvrGNIFFKGVDLGKLTVKQwqk 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEALSARA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 lRGRDIAYLVQNPMSMFNpF---QKIEA--HILETILSHEKCSKRVALSKALEWMkrlnldDAISLLKKYPFELSGGMLQ 155
Cdd:PRK09536 75 -ASRRVASVPQDTSLSFE-FdvrQVVEMgrTPHRSRFDTWTETDRAAVERAMERT------GVAQFADRPVTSLSGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 156 RIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAI 235
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
....
gi 446358294 236 LSNP 239
Cdd:PRK09536 227 LTAD 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-237 |
6.69e-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: 82.84 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIG--EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLGKLTVkqwQK 80
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYePDS----GQILLDGHDLADYTL---AS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRgRDIAYLVQNPMsMFNP--FQKIEAHILETIlSHEKCSKRVALSKALEWMKRL--NLDDAISllkKYPFELSGGMLQR 156
Cdd:TIGR02203 404 LR-RQVALVSQDVV-LFNDtiANNIAYGRTEQA-DRAEIERALAAAYAQDFVDKLplGLDTPIG---ENGVLLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLI------TVTHdyqlardlGGQLLVISEGEVVEQG 230
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLViahrlsTIEK--------ADRIVVMDDGRIVERG 549
|
....*..
gi 446358294 231 QTQAILS 237
Cdd:TIGR02203 550 THNELLA 556
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-237 |
1.61e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.43 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLRg 83
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS---PDSGEVRLNGRPLADWSPAELARRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 rdiAYLVQNPmSMFNPFQKIEahILE---TILSHEKCSKRVALSKALEwmkrlnLDDAISLL-KKYPfELSGGMLQRIML 159
Cdd:PRK13548 79 ---AVLPQHS-SLSFPFTVEE--VVAmgrAPHGLSRAEDDALVAAALA------QVDLAHLAgRDYP-QLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 160 ATIL------SLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQT 232
Cdd:PRK13548 146 ARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
....*
gi 446358294 233 QAILS 237
Cdd:PRK13548 226 AEVLT 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-207 |
1.94e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLGKLTVKQWQKlr 82
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPT----SGTLLFEGEDISTLKPEIYRQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 grDIAYLVQNPMsMFNpfqkieahilET-----ILSHEKCSKRVALSKALEWMKRLNLDDAIslLKKYPFELSGGMLQRI 157
Cdd:PRK10247 82 --QVSYCAQTPT-LFG----------DTvydnlIFPWQIRNQQPDPAIFLDDLERFALPDTI--LTKNIAELSGGEKQRI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHD 207
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHD 197
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-236 |
3.45e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.83 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG--HIPQGmtvrgNIFFKGVDLGKLTVKQwqkLRgRDIAYLVQN 92
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfyDIDEG-----EILLDGHDLRDYTLAS---LR-NQVALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 pMSMFNpfQKIE---AHILETILSHEKCSKRVALSKALEWMKRLN--LDDAISllkkypfE----LSGGMLQRIMLATIL 163
Cdd:PRK11176 426 -VHLFN--DTIAnniAYARTEQYSREQIEEAARMAYAMDFINKMDngLDTVIG-------EngvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHdyQLAR-DLGGQLLVISEGEVVEQGQTQAIL 236
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAH--RLSTiEKADEILVVEDGEIVERGTHAELL 566
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-237 |
3.51e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.05 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLRGRDIAYLVQNPM 94
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK---PTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 95 SmfnpfQKIEAHILETILSHEKCSKrVALSKALEWMKRLNLDDAIS--LLKKYPFELSGGMLQRIMLATILSLDPQVIIL 172
Cdd:PRK13646 96 S-----QLFEDTVEREIIFGPKNFK-MNLDEVKNYAHRLLMDLGFSrdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 173 DEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-236 |
3.64e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.49 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDL---------GKLTVKQWQKLrgr 84
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD---AGKITVLGVPVpararlaraRIGVVPQFDNL--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 85 DIAYLVQNPMSMFNPFQKIEAHILETILShekcskrvalsKALEWMKRLNLDDA-ISllkkypfELSGGMLQRIMLATIL 163
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMSTREIEAVIP-----------SLLEFARLESKADArVS-------DLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAIL 236
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-207 |
4.71e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 80.10 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQI-GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTvkqwQKL 81
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD---PLQGEVTLDGVPVSSLD----QDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRDIAYLVQNPmsmfnpfqkieaHILETILSHekcSKRVA--------LSKALE------WMKRLNlDDAISLLKKYPF 147
Cdd:TIGR02868 407 VRRRVSVCAQDA------------HLFDTTVRE---NLRLArpdatdeeLWAALErvgladWLRALP-DGLDTVLGEGGA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 148 ELSGGMLQRIMLATILSLDPQVIILDEPTSAVDchnCSTISAILQEL--QNNGKTLITVTHD 207
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLD---AETADELLEDLlaALSGRTVVLITHH 529
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-230 |
6.20e-17 |
|
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: 76.95 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDM---GESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLGKLTVKQWQKLRGRDIAYLVQNpM 94
Cdd:cd03297 10 LPDFTLKIDFdlnEEVTGIFGASGAGKSTLLRCIAGLEkPDG----GTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ-Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 95 SMFnPFQKIEAHILETILSHEKCSKRVALSKALEwmkRLNLDdaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:cd03297 85 ALF-PHLNVRENLAFGLKRKRNREDRISVDELLD---LLGLD---HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 175 PTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-233 |
6.80e-17 |
|
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: 78.59 E-value: 6.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVRGNiffkGVDLgkltVKQWQKLRgRDIAYLVQn 92
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLrPTSGTARVA----GYDV----VREPRKVR-RSIGIVPQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 pmsMFNPFQKIEAHilETILSHEKC---SKRVALSKALEWMKRLNLDDAISLLKKYpfeLSGGMLQRIMLATILSLDPQV 169
Cdd:TIGR01188 74 ---YASVDEDLTGR--ENLEMMGRLyglPKDEAEERAEELLELFELGEAADRPVGT---YSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 170 IILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQ 233
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-240 |
9.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQI---GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtvrgnifFKGV---DLGKLTVKQ 77
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE---------FEGKvkiDGELLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 78 WQKLRgRDIAYLVQNPMSMFnpfqkIEAHILETI---LSHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGML 154
Cdd:PRK13642 76 VWNLR-RKIGMVFQNPDNQF-----VGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLD---FKTREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 155 QRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGK-TLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQ 233
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
....*..
gi 446358294 234 AILSNPQ 240
Cdd:PRK13642 226 ELFATSE 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-239 |
9.81e-17 |
|
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: 76.81 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQwqklRG 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGKILLDGQDITKLPMHK----RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RD-IAYLVQNPmSMFNPF---QKIEAhILETIlsheKCSKRVALSKALEWMKRLNLDdaiSLLKKYPFELSGGMLQRIML 159
Cdd:cd03218 74 RLgIGYLPQEA-SIFRKLtveENILA-VLEIR----GLSKKEREEKLEELLEEFHIT---HLRKSKASSLSGGERRRVEI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNG-----------KTLITVTHDYqlardlggqllVISEGEVVE 228
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGigvlitdhnvrETLSITDRAY-----------IIYEGKVLA 213
|
250
....*....|.
gi 446358294 229 QGQTQAILSNP 239
Cdd:cd03218 214 EGTPEEIAANE 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-228 |
1.06e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 9 LSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmtvrgniFFKGVDLGKLTVKQWqklrGRDIAy 88
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---------GTPVAGCVDVPDNQF----GREAS- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 89 LVQNPMSMFNPFQKIEahiletILShekcskRVALSkalewmkrlnldDAISLLKKYPfELSGGMLQRIMLATILSLDPQ 168
Cdd:COG2401 102 LIDAIGRKGDFKDAVE------LLN------AVGLS------------DAVLWLRRFK-ELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 169 VIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVI-SEGEVVE 228
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDVIDDLQPDLLIFvGYGGVPE 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-239 |
1.91e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.75 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 6 IRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFfkgvdLGKLTVKQWQ-KLRGR 84
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS---EGEIL-----LDAQPLESWSsKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 85 DIAYLVQNpmsmfnpFQKIEAHILETILSHEKCSKRVALSKaLEWMKRLNLDDAISLLKKYPF------ELSGGMLQRIM 158
Cdd:PRK10575 86 KVAYLPQQ-------LPAAEGMTVRELVAIGRYPWHGALGR-FGAADREKVEEAISLVGLKPLahrlvdSLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
..
gi 446358294 238 NP 239
Cdd:PRK10575 238 GE 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-230 |
2.34e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVR-GNIFFKGVDlgklTVKQWQKLRgRDIAYLVQNPMSm 96
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTvGDIVVSSTS----KQKEIKPVR-KKVGVVFQFPES- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 fnpfQKIEAHILETIL---SHEKCSKRVALSKALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILD 173
Cdd:PRK13643 96 ----QLFEETVLKDVAfgpQNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 174 EPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-206 |
3.49e-16 |
|
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: 73.73 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGE-VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIffkgvdlgkltvkqwQKLR 82
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG---SGRI---------------GMPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLVQNPmsmfnpfqkieahiletilshekcskrvalskaleWMKRLNLDDAISllkkYPF--ELSGGMLQRIMLA 160
Cdd:cd03223 63 GEDLLFLPQRP-----------------------------------YLPLGTLREQLI----YPWddVLSGGEQQRLAFA 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQELqnnGKTLITVTH 206
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-239 |
4.04e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.54 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQWQKLRg 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS---SGEVRLNGRPLAAWSPWELARRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 rdiAYLVQN-PMSmFnPFQKIE-------AHILETILSHEKCSKRVALSKALEWMKRLnlddaisllkkYPfELSGGMLQ 155
Cdd:COG4559 78 ---AVLPQHsSLA-F-PFTVEEvvalgraPHGSSAAQDRQIVREALALVGLAHLAGRS-----------YQ-TLSGGEQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 156 RIMLATIL-------SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVE 228
Cdd:COG4559 141 RVQLARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVA 220
|
250
....*....|.
gi 446358294 229 QGQTQAILSNP 239
Cdd:COG4559 221 QGTPEEVLTDE 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-239 |
5.30e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.52 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQwqklr 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPD----SGRIMLDGQDITHVPAEN----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQN----P-MSMFN-----------PFQKIEAHILEtilshekcskrvalskALEwMKRLNlddaiSLLKKYP 146
Cdd:PRK09452 86 -RHVNTVFQSyalfPhMTVFEnvafglrmqktPAAEITPRVME----------------ALR-MVQLE-----EFAQRKP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 147 FELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGE 225
Cdd:PRK09452 143 HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
250
....*....|....
gi 446358294 226 VVEQGQTQAILSNP 239
Cdd:PRK09452 223 IEQDGTPREIYEEP 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
8.94e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.84 E-value: 8.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQI-GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQ 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK---PTSGSVLIRGEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 KLRGrdiaYLVQNPM-SMFNPF--QKIEAHILETILSHEKCSKRVAlskalEWMKRLNLDDaisLLKKYPFELSGGMLQR 156
Cdd:PRK13652 78 KFVG----LVFQNPDdQIFSPTveQDIAFGPINLGLDEETVAHRVS-----SALHMLGLEE---LRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAI 235
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....
gi 446358294 236 LSNP 239
Cdd:PRK13652 226 FLQP 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-233 |
1.25e-15 |
|
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: 73.69 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQ--IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgMTvRGNIFFKGVDlgkltVKQWQKL 81
Cdd:cd03263 1 LQIRNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR--PT-SGTAYINGYS-----IRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRDIAYLVQNpmSMFNPFQKIEAHILetILSHEKCSKRVALSKALEWMKR-LNLDDaisLLKKYPFELSGGMLQRIMLA 160
Cdd:cd03263 73 ARQSLGYCPQF--DALFDELTVREHLR--FYARLKGLPKSEIKEEVELLLRvLGLTD---KANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQ 233
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKG-RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-230 |
1.47e-15 |
|
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: 73.34 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 6 IRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIP--QG-MTVRGNI---FFKGVDL-GKLTvkqw 78
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdSGtVTVRGRVsslLGLGGGFnPELT---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 qklrGRDIAYLVqnpMSMFN-PFQKIEAHILETIlshekcskrvALSKalewmkrlnLDDAISL-LKKYpfelSGGMLQR 156
Cdd:cd03220 101 ----GRENIYLN---GRLLGlSRKEIDEKIDEII----------EFSE---------LGDFIDLpVKTY----SSGMKAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVD------CHncstisAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDaafqekCQ------RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-230 |
1.73e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.45 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHiPQGMTVRGNIFFKGVDLGKLTVKQwqklRG 83
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH-PSYEVTSGTILFKGQDLLELEPDE----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYL-VQNP-------MSMFnpfqkieahiLETILSHEKCSKRVALSKALEWMKRLnlDDAISLLKkYPFEL------ 149
Cdd:TIGR01978 76 RAGLFLaFQYPeeipgvsNLEF----------LRSALNARRSARGEEPLDLLDFEKLL--KEKLALLD-MDEEFlnrsvn 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 150 ---SGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLG-GQLLVISEGE 225
Cdd:TIGR01978 143 egfSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGR 222
|
....*
gi 446358294 226 VVEQG 230
Cdd:TIGR01978 223 IVKSG 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-226 |
1.83e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.00 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSL---QIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIpqgMTVRGNIFfkgVDLGKLTVKQWQK 80
Cdd:PRK13650 5 IEVKNLTFkykEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL---EAESGQII---IDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRgRDIAYLVQNPMSMF--NPFQKIEAHILETI-LSHEKCSKRValSKALEWMKRLNLDDaisllkKYPFELSGGMLQRI 157
Cdd:PRK13650 79 IR-HKIGMVFQNPDNQFvgATVEDDVAFGLENKgIPHEEMKERV--NEALELVGMQDFKE------REPARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 158 MLATILSLDPQVIILDEPTSAVDCHN----CSTISAILQElqnNGKTLITVTHDY-QLArdLGGQLLVISEGEV 226
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDD---YQMTVISITHDLdEVA--LSDRVLVMKNGQV 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-239 |
1.90e-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: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQWQklrgRDIAYLVQNP 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlYQPTG----GQVLLDGVPLVQYDHHYLH----RQVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMFNPFQKIEAHILEtilsheKCSKRVALSKAlewmKRLNLDDAISLLKK-YPFE-------LSGGMLQRIMLATILSL 165
Cdd:TIGR00958 565 VLFSGSVRENIAYGLT------DTPDEEIMAAA----KAANAHDFIMEFPNgYDTEvgekgsqLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446358294 166 DPQVIILDEPTSAVDchncSTISAILQELQN-NGKTLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAILSNP 239
Cdd:TIGR00958 635 KPRVLILDEATSALD----AECEQLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-240 |
2.65e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMtvrGNIFFKGVDLGKLTVKQWQKlrgRDIAYLVQNPmSMF 97
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---GNIIIDDEDISLLPLHARAR---RGIGYLPQEA-SIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 98 NPFQkIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAISLLKKypfELSGGMLQRIMLATILSLDPQVIILDEPTS 177
Cdd:PRK10895 91 RRLS-VYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 178 AVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-239 |
2.92e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 74.37 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQwqklr 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTE----GQIFIDGEDVTHRSIQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNpMSMFnPFQKIEAHI---LETI-LSHEKCSKRVAlsKALEwmkrlnLDDAISLLKKYPFELSGGMLQRIM 158
Cdd:PRK11432 78 -RDICMVFQS-YALF-PHMSLGENVgygLKMLgVPKEERKQRVK--EALE------LVDLAGFEDRYVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
..
gi 446358294 238 NP 239
Cdd:PRK11432 227 QP 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-246 |
3.33e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.28 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLL--VGHIPQGMTVRGNIFFKGVDLGKLTVKQwQKL 81
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFRVEGKVTFHGKNLYAPDVDP-VEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRdIAYLVQNPmsmfNPFQKieaHILETILSHEKCSK---------RVALSKALEWmkrlnlDDAISLLKKYPFELSGG 152
Cdd:PRK14243 90 RRR-IGMVFQKP----NPFPK---SIYDNIAYGARINGykgdmdelvERSLRQAALW------DEVKDKLKQSGLSLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLA--------------RDLGGQL 218
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAarvsdmtaffnvelTEGGGRY 234
|
250 260
....*....|....*....|....*...
gi 446358294 219 lviseGEVVEQGQTQAILSNPQHNYTKA 246
Cdd:PRK14243 235 -----GYLVEFDRTEKIFNSPQQQATRD 257
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-241 |
3.42e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.32 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-----PQGMTVRGNIFFKGVDLGKLTVKQWQKLRgrdiAYLVQN 92
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaPRGARVTGDVTLNGEPLAAIDAPRLARLR----AVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 PMSMFnPFQKIEAHILETILSHEKCSKRVALSKALEWmKRLNLDDAISLLKKYPFELSGGMLQRIMLATILS-------- 164
Cdd:PRK13547 92 AQPAF-AFSAREIVLLGRYPHARRAGALTHRDGEIAW-QALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphda 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 165 -LDPQVIILDEPTSAVD-CHN---CSTISAILQELQNNgktLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSnP 239
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDlAHQhrlLDTVRRLARDWNLG---VLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-P 245
|
..
gi 446358294 240 QH 241
Cdd:PRK13547 246 AH 247
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-260 |
3.45e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.20 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAK----LLVghiPQGmtvrGNIFFKGVDLgKLTVKQWqKLRGRdiaylv 90
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnaLLI---PSE----GKVYVDGLDT-SDEENLW-DIRNK------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 91 qNPMSMFNPFQKIEAHILETILSH---------EKCSKRVAlskalEWMKRLNLDDaislLKKY-PFELSGGMLQRIMLA 160
Cdd:PRK13633 87 -AGMVFQNPDNQIVATIVEEDVAFgpenlgippEEIRERVD-----ESLKKVGMYE----YRRHaPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAILSN- 238
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEv 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 446358294 239 ----------PQhnyTKALTVQMEYEG-----DILNV 260
Cdd:PRK13633 236 emmkkigldvPQ---VTELAYELKKEGvdipsDILTI 269
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-230 |
5.70e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.37 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHiPQGMTVRGNIFFKGVDLGKLTVKQWQKLrG 83
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAYKILEGDILFKGESILDLEPEERAHL-G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYlvQNPmsmfnpfqkIE------AHILETILShekcSKRVALSK----ALEW----MKRLNLDD-AISLLKKYPFE 148
Cdd:CHL00131 86 IFLAF--QYP---------IEipgvsnADFLRLAYN----SKRKFQGLpeldPLEFleiiNEKLKLVGmDPSFLSRNVNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 -LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHdYQlardlggQLL-------- 219
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-YQ-------RLLdyikpdyv 222
|
250
....*....|..
gi 446358294 220 -VISEGEVVEQG 230
Cdd:CHL00131 223 hVMQNGKIIKTG 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-230 |
5.80e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.04 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqGMTVRGNIFFKGVDLGKLTVKqwqklrgRDIAYLVQNpmSM 96
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT-GLGVSGEVLINGRPLDKRSFR-------KIIGYVPQD--DI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNPFQKIEahilETILSHEKCSKrvalskalewmkrlnlddaisllkkypfeLSGGMLQRIMLATILSLDPQVIILDEPT 176
Cdd:cd03213 93 LHPTLTVR----ETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 177 SAVDCHNCSTISAILQELQNNGKTLITVTHdyQLARDLGG---QLLVISEGEVVEQG 230
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRTIICSIH--QPSSEIFElfdKLLLLSQGRVIYFG 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-230 |
5.90e-15 |
|
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: 70.80 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGE--VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLGKLtvkqwQK 80
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQ----QGEITLDGVPVSDL-----EK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRGRDIAYLVQNPmsmfnpfqkieaHILETILshekcskrvalskalewmkRLNLDDaisllkkypfELSGGMLQRIMLA 160
Cdd:cd03247 72 ALSSLISVLNQRP------------YLFDTTL-------------------RNNLGR----------RFSGGERQRLALA 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTI-SAILQELQNngKTLITVTHDYQlARDLGGQLLVISEGEVVEQG 230
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLlSLIFEVLKD--KTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-236 |
5.94e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGMTVR-------GNIFFKGVDLGklTV 75
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDAGSISlcgepvpSRARHARQRVG--VV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 76 KQWQKLrgrDIAYLVQNPMSMFNPFQKIEAHiletilsheKCSKRVAlsKALEWMKRLNLDDA-ISllkkypfELSGGML 154
Cdd:PRK13537 86 PQFDNL---DPDFTVRENLLVFGRYFGLSAA---------AARALVP--PLLEFAKLENKADAkVG-------ELSGGMK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 155 QRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQA 234
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
..
gi 446358294 235 IL 236
Cdd:PRK13537 225 LI 226
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-240 |
6.26e-15 |
|
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: 71.81 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 25 KIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKltvkqwqklRGRDIAYLVQN-------PMSMF 97
Cdd:TIGR03771 2 SADKGELLGLLGPNGAGKTTLLRAILGLIPPA---KGTVKVAGASPGK---------GWRHIGYVPQRhefawdfPISVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 98 NPFQKIEAHILeTILSHEKCSKRVALSKALEwmkRLNLDDaislLKKYPF-ELSGGMLQRIMLATILSLDPQVIILDEPT 176
Cdd:TIGR03771 70 HTVMSGRTGHI-GWLRRPCVADFAAVRDALR---RVGLTE----LADRPVgELSGGQRQRVLVARALATRPSVLLLDEPF 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 177 SAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISeGEVVEQGqTQAILSNPQ 240
Cdd:TIGR03771 142 TGLDMPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADG-TPQQLQDPA 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-240 |
6.32e-15 |
|
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: 71.94 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVkqwQK 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP---PRSGSIRFDGEDITGLPP---HR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRGRDIAYLVQNpMSMFnPFQKIEAHILetiLSHEKCSKRVALSKALEWMKRL--NLDDaisLLKKYPFELSGGmlQRIM 158
Cdd:COG0410 75 IARLGIGYVPEG-RRIF-PSLTVEENLL---LGAYARRDRAEVRADLERVYELfpRLKE---RRRQRAGTLSGG--EQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 159 LAtI---LSLDPQVIILDEPT-----SAVDchncsTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:COG0410 145 LA-IgraLMSRPKLLLLDEPSlglapLIVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
250
....*....|
gi 446358294 231 QTQAILSNPQ 240
Cdd:COG0410 219 TAAELLADPE 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-227 |
8.44e-15 |
|
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: 69.76 E-value: 8.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFkgvdlgkltvkqwqklR 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlYKPDS----GEILV----------------D 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLvqnpmsmfNPFQKIEAHIlETIlshekcskrvalskalewmkrlnlddaisllkkypFELSGGMLQRIMLATI 162
Cdd:cd03216 61 GKEVSFA--------SPRDARRAGI-AMV-----------------------------------YQLSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446358294 163 LSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-210 |
1.11e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.01 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtvrgniffkgvDLGKLTVKQWQKlrg 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP-------------DEGIVTWGSTVK--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 rdIAYLVQnpmsmfnpfqkieahiletilshekcskrvalskalewmkrlnlddaisllkkypfeLSGGMLQRIMLATIL 163
Cdd:cd03221 65 --IGYFEQ---------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446358294 164 SLDPQVIILDEPTSAVDCHncsTISAILQELQNNGKTLITVTHDYQL 210
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLE---SIEALEEALKEYPGTVILVSHDRYF 129
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-236 |
1.23e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.27 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLaKLL-------VGHI-----------------PQgMTVRGNIFFKGV 68
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKsTLL-KLIagileptSGRVevngrvsallelgagfhPE-LTGRENIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 69 DLGkltvkqwqkLRGRDIaylvqnpmsmfnpfQKIEAHIletilshekcskrVALSkalewmkrlNLDDAISL-LKKYpf 147
Cdd:COG1134 115 LLG---------LSRKEI--------------DEKFDEI-------------VEFA---------ELGDFIDQpVKTY-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 148 elSGGMLQRIMLATILSLDPQVIILDEPTSAVD------CHncstisAILQELQNNGKTLITVTHDYQLARDLGGQLLVI 221
Cdd:COG1134 148 --SSGMRARLAFAVATAVDPDILLVDEVLAVGDaafqkkCL------ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|....*
gi 446358294 222 SEGEVVEQGQTQAIL 236
Cdd:COG1134 220 EKGRLVMDGDPEEVI 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-226 |
1.88e-14 |
|
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: 69.38 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQigevPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLRg 83
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP---PASGEITLDGKPVTRRSPRDAIRAG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 rdIAYLVQNPmsmfnpfqkieahiletilshekcsKRVALskalewMKRLNLDDAISLlkkyPFELSGGMLQRIMLATIL 163
Cdd:cd03215 77 --IAYVPEDR-------------------------KREGL------VLDLSVAENIAL----SSLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 164 SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-239 |
2.78e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.05 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWqklR 82
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD---VSEGDIRFHDIPLTKLQLDSW---R 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRdIAYLVQNPMsMFNpfqkieahilETILSHEKCSKRVALSKALEWMKRL-NL-DDAISLLKKYPFE-------LSGGM 153
Cdd:PRK10789 389 SR-LAVVSQTPF-LFS----------DTVANNIALGRPDATQQEIEHVARLaSVhDDILRLPQGYDTEvgergvmLSGGQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHncsTISAILQELQN--NGKTLITVTHDYQLARDlGGQLLVISEGEVVEQGQ 231
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGR---TEHQILHNLRQwgEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
....*...
gi 446358294 232 TQAILSNP 239
Cdd:PRK10789 533 HDQLAQQS 540
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-230 |
3.62e-14 |
|
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: 71.77 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLGKLTvkQwQKLRgRDIAYLVQNPMs 95
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTS----GRILIDGQDIRDVT--Q-ASLR-AAIGIVPQDTV- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 96 MFNpfqkieahilETIL----------SHEKCsKRVAlskalewmKRLNLDDAI-SLLKKYP-------FELSGGMLQRI 157
Cdd:COG5265 443 LFN----------DTIAyniaygrpdaSEEEV-EAAA--------RAAQIHDFIeSLPDGYDtrvgergLKLSGGEKQRV 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 158 MLA-TILSlDPQVIILDEPTSAVDCHncsTISAILQELQNNGK---TLI------TVTH-DyqlardlggQLLVISEGEV 226
Cdd:COG5265 504 AIArTLLK-NPPILIFDEATSALDSR---TERAIQAALREVARgrtTLViahrlsTIVDaD---------EILVLEAGRI 570
|
....
gi 446358294 227 VEQG 230
Cdd:COG5265 571 VERG 574
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-240 |
7.98e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.90 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQwqk 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGRIFLDGEDITHLPMHK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 lRGRD-IAYLVQNPmSMF-------NpfqkIEAhILETilshekcskrVALSKAlEWMKRLN--LDD-AISLLKKYP-FE 148
Cdd:COG1137 75 -RARLgIGYLPQEA-SIFrkltvedN----ILA-VLEL----------RKLSKK-EREERLEelLEEfGITHLRKSKaYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNG-KTLIT----------VTHDYqlardlggq 217
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGiGVLITdhnvretlgiCDRAY--------- 207
|
250 260
....*....|....*....|...
gi 446358294 218 llVISEGEVVEQGQTQAILSNPQ 240
Cdd:COG1137 208 --IISEGKVLAEGTPEEILNNPL 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
9.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.49 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLgKLTVKQWQKLRgRDIAYLVQNP-MSMF 97
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK---PSSGRILFDGKPI-DYSRKGLMKLR-ESVGMVFQDPdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 98 NP--FQKIEAHILETILSHEKCSKRValSKALEwmkrlnlDDAISLLKKYPFE-LSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:PRK13636 97 SAsvYQDVSFGAVNLKLPEDEVRKRV--DNALK-------RTGIEHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 175 PTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-227 |
1.83e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.59 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 29 GESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGVDLGKLTVKQWQKLRgRDIAYLVQNPMSMFNP--FQKIEA 105
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGiERPSA----GKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRtvYDNVAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 106 HILETILSHEKCSKRValSKALEwmKRLNLDDAisllKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCS 185
Cdd:PRK10908 103 PLIIAGASGDDIRRRV--SAALD--KVGLLDKA----KNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446358294 186 TISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:PRK10908 175 GILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-230 |
2.57e-13 |
|
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: 67.01 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 7 RKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDlgklTVKQWQKLRgRD 85
Cdd:cd03266 9 KRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDA----GFATVDGFD----VVKEPAEAR-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 86 IAYLVQNpmsmFNPFQKIEAhiLETILSHEKCS--KRVALSKALEWM-KRLNLDDaisLLKKYPFELSGGMLQRIMLATI 162
Cdd:cd03266 80 LGFVSDS----TGLYDRLTA--RENLEYFAGLYglKGDELTARLEELaDRLGMEE---LLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 163 LSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-231 |
2.68e-13 |
|
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: 67.11 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHipqGMTVRGNIFFKGvdlgkltvKQWQKlRGRDIAYLVQNpMSMFn 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL---AQPTSGGVILEG--------KQITE-PGPDRMVVFQN-YSLL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 99 PFQKIEAHI---LETILSHEKCSKRVALSKalEWMKRLNLDDAIsllKKYPFELSGGMLQRIMLATILSLDPQVIILDEP 175
Cdd:TIGR01184 67 PWLTVRENIalaVDRVLPDLSKSERRAIVE--EHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 176 TSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQ 231
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQ 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-207 |
3.38e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 6 IRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmtvrgniffkgVDLGKLTVKqwqklRGRD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE-------------PDSGEVSIP-----KGLR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 86 IAYLVQNP------------MSMFNPFQKIEA---HILETILSHEKCSKRVAL--------------SKALEWMKRLNLD 136
Cdd:COG0488 63 IGYLPQEPpldddltvldtvLDGDAELRALEAeleELEAKLAEPDEDLERLAElqeefealggweaeARAEEILSGLGFP 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 137 DAisLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDchncstISAI--LQE-LQNNGKTLITVTHD 207
Cdd:COG0488 143 EE--DLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIewLEEfLKNYPGTVLVVSHD 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-230 |
4.09e-13 |
|
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: 66.62 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLgkltVKQWQKLR 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTS----GRATVAGHDV----VREPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 gRDIAYLVQNPM--SMFNPFQKIEAHILETILSHEKCSKRVAlsKALEWMKRLNLDDaiSLLKKYpfelSGGMLQRIMLA 160
Cdd:cd03265 73 -RRIGIVFQDLSvdDELTGWENLYIHARLYGVPGAERRERID--ELLDFVGLLEAAD--RLVKTY----SGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-224 |
4.18e-13 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 66.67 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTLLAKLLvghipqGMtvrgnifFKGVDLGKLTV--------KQWQK--LRGRDIA 87
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNII------GM-------FDSLDSGSLTLagkevtnlSYSQKiiLRRELIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 88 YLVQ--NPMSMFNPFQKIEAHiletiLSHEKCSKRVALSKALEWMKRLNLDDAislLKKYPFELSGGMLQRIMLATILSL 165
Cdd:NF038007 87 YIFQsfNLIPHLSIFDNVALP-----LKYRGVAKKERIERVNQVLNLFGIDNR---RNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 166 DPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQlARDLGGQLLVISEG 224
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDG 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-232 |
4.28e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQWQKLRg 83
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGNPCARLTPAKAHQLG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 rdiAYLV-QNPMsMFnPFQKIEAHILETILSHEKCSKRV-ALSKALEwmKRLNLDDAISLLkkypfELSGGMLQRIMLAt 161
Cdd:PRK15439 88 ---IYLVpQEPL-LF-PNLSVKENILFGLPKRQASMQKMkQLLAALG--CQLDLDSSAGSL-----EVADRQIVEILRG- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 162 iLSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQT 232
Cdd:PRK15439 155 -LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-230 |
4.33e-13 |
|
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: 66.36 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQ--IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVkqwQK 80
Cdd:cd03244 2 DIEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE---LSSGSILIDGVDISKIGL---HD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRGRdIAYLVQNPMSM-----FN--PF-QKIEAHILETIlshekcsKRVALSKALEWMKRLnLDDAISLLKKypfELSGG 152
Cdd:cd03244 76 LRSR-ISIIPQDPVLFsgtirSNldPFgEYSDEELWQAL-------ERVGLKEFVESLPGG-LDTVVEEGGE---NLSVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQElQNNGKTLITVTH------DYQlardlggQLLVISEGEV 226
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHrldtiiDSD-------RILVLDKGRV 215
|
....
gi 446358294 227 VEQG 230
Cdd:cd03244 216 VEFD 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-206 |
9.00e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 2 EQLEIRKLSLQI--GEvPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKgvdlgkltvkqwq 79
Cdd:COG4178 361 GALALEDLTLRTpdGR-PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG---SGRIARP------------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 klRGRDIAYLVQNPmsmfnpfqkieaHI----LETILSHEKCSKRVALSKALEWMKRLNLDDAISLL---KKYPFELSGG 152
Cdd:COG4178 424 --AGARVLFLPQRP------------YLplgtLREALLYPATAEAFSDAELREALEAVGLGHLAERLdeeADWDQVLSLG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 153 MLQRIMLATILSLDPQVIILDEPTSAVDCHNcstISAILQELQNN--GKTLITVTH 206
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEEN---EAALYQLLREElpGTTVISVGH 542
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-230 |
1.16e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.29 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLAKLLVGHIPQGmtvrGNIFFKGVDLGKLTVkqwQKLRgRDIAYLVQN 92
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKsTLINLLQRVFDPQS----GRILIDGTDIRTVTR---ASLR-RNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 93 PMsMFNpfQKIEAHIL--ETILSHEKCSKRVALSKALEWMKR--LNLDDAISllkkypfE----LSGGMLQRIMLATILS 164
Cdd:PRK13657 418 AG-LFN--RSIEDNIRvgRPDATDEEMRAAAERAQAHDFIERkpDGYDTVVG-------ErgrqLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 165 LDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLItVTHDYQLARDlGGQLLVISEGEVVEQG 230
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
12-240 |
1.26e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 12 QIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLLAKLlvghipQGMTV-RGNIFFKGVDLGKLTVKQWQKLRgrdiAYL 89
Cdd:PRK03695 5 DVAVSTRLGPLSAEVRAGEILHLVGPNGAGKsTLLARM------AGLLPgSGSIQFAGQPLEAWSAAELARHR----AYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 90 VQNPMSMFN-P-FQKIEAHIletilsHEKCSKRVALSKALEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLA-TILSLD 166
Cdd:PRK03695 75 SQQQTPPFAmPvFQYLTLHQ------PDKTRTEAVASALNEVAEALGLDD---KLGRSVNQLSGGEWQRVRLAaVVLQVW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 167 P------QVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDyqLARDL--GGQLLVISEGEVVEQGQTQAILSN 238
Cdd:PRK03695 146 PdinpagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHD--LNHTLrhADRVWLLKQGKLLASGRRDEVLTP 223
|
..
gi 446358294 239 PQ 240
Cdd:PRK03695 224 EN 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-237 |
1.35e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.37 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 22 FSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQwqklrgrdiaylvqNPMSMFnpFQ 101
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLT---PASGSLTLNGQDHTTTPPSR--------------RPVSML--FQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 102 K--IEAH--ILETI---------LSHEKCSKRVALSKalewmkRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQ 168
Cdd:PRK10771 79 EnnLFSHltVAQNIglglnpglkLNAAQREKLHAIAR------QMGIED---LLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 169 VIILDEPTSAVDchncstiSAILQEL--------QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK10771 150 ILLLDEPFSALD-------PALRQEMltlvsqvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-206 |
1.50e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmTVRGNIFFKGVDLGKLTVKQWQKlRG 83
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG-TYEGEIIFEGEELQASNIRDTER-AG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAY----LVQNpMSmfnpfqkieahILETI-LSHEKCSKRV-----ALSKALEWMKRLNLDdaISLLKKYpFELSGGM 153
Cdd:PRK13549 84 IAIIHqelaLVKE-LS-----------VLENIfLGNEITPGGImdydaMYLRAQKLLAQLKLD--INPATPV-GNLGLGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTH 206
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-211 |
2.09e-12 |
|
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: 64.30 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLtvkqwQKLRG 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR---PDSGEVRWNGTPLAEQ-----RDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMsmfnpfQKIEAHILE--TILSHEKCSKRVALSKALEwmkRLNLDDAISLLKKYpfeLSGGMLQRIMLAT 161
Cdd:TIGR01189 73 ENILYLGHLPG------LKPELSALEnlHFWAAIHGGAQRTIEDALA---AVGLTGFEDLPAAQ---LSAGQQRRLALAR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446358294 162 ILSLDPQVIILDEPTSAVDCHNCSTISAILQE-LQNNGKTLITVTHDYQLA 211
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLV 191
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-236 |
3.24e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.89 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTvkqWQKLRgRDIAYLVQNPMSM 96
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP---LTEGEIRLDGRPLSSLS---HSVLR-QGVAMVQQDPVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNPFQkieAHI-LETILSHEKCSKRVALSKALEWMKRLNlDDAISLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEP 175
Cdd:PRK10790 428 ADTFL---ANVtLGRDISEEQVWQALETVQLAELARSLP-DGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 176 TSAVDCHNCSTISAILQELQNNgKTLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAIL 236
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-230 |
4.08e-12 |
|
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: 63.39 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTvKQWQKlrg 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSYQKNI-EALRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 rdIAYLVQNPMsmFNP----FQKIEAHILETILSHEKCSKrvalskALEwmkRLNLDDAISL-LKKYpfelSGGMLQRIM 158
Cdd:cd03268 74 --IGALIEAPG--FYPnltaRENLRLLARLLGIRKKRIDE------VLD---VVGLKDSAKKkVKGF----SLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 159 LATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDY----QLARDLGgqllVISEGEVVEQG 230
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLseiqKVADRIG----IINKGKLIEEG 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-235 |
4.35e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFFKGVDLGKLTVKQWQKLr 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiHEPT----KGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYlvqNPMSMFNpfqkiEAHILETILSHEKCSKRVALSKALEW--------MKRLNLDDAISLLKKYPfELSGGML 154
Cdd:PRK09700 81 GIGIIY---QELSVID-----ELTVLENLYIGRHLTKKVCGVNIIDWremrvraaMMLLRVGLKVDLDEKVA-NLSISHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 155 QRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQA 234
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
.
gi 446358294 235 I 235
Cdd:PRK09700 232 V 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-230 |
4.41e-12 |
|
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: 63.59 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQIGE--VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVkqwQK 80
Cdd:cd03369 6 EIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE---AEEGKIEIDGIDISTIPL---ED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LRgRDIAYLVQNPMsmfnpfqkIEAHILETILSHEKCSKRVALSKALEwmkrlnlddaislLKKYPFELSGGMLQRIMLA 160
Cdd:cd03369 80 LR-SSLTIIPQDPT--------LFSGTIRSNLDPFDEYSDEEIYGALR-------------VSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 161 TILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGkTLITVTHDYQLARDLgGQLLVISEGEVVEQG 230
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS-TILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-227 |
5.22e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQigevPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLRg 83
Cdd:COG1129 257 LEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP---ADSGEIRLDGKPVRIRSPRDAIRAG- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 rdIAY---------LVQNpMSmfnpfqkIEAHIleTILSHEKCSKRVALSK------ALEWMKRLN-----LDDAISllk 143
Cdd:COG1129 329 --IAYvpedrkgegLVLD-LS-------IRENI--TLASLDRLSRGGLLDRrreralAEEYIKRLRiktpsPEQPVG--- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 144 kypfELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD----YQLA-RdlggqL 218
Cdd:COG1129 394 ----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSElpelLGLSdR-----I 464
|
....*....
gi 446358294 219 LVISEGEVV 227
Cdd:COG1129 465 LVMREGRIV 473
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-237 |
6.87e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 8 KLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLvghiPQGMT-VRGNIFFKGVDLGKLTVKQwqklRGRDI 86
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL----SRLMTpAHGHVWLDGEHIQHYASKE----VARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 87 AYLVQNPMSMFN-PFQKIEA---HILETILSHEKCSKRVALSKAlewMKRLNLDDaisLLKKYPFELSGGMLQRIMLATI 162
Cdd:PRK10253 84 GLLAQNATTPGDiTVQELVArgrYPHQPLFTRWRKEDEEAVTKA---MQATGITH---LADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 163 LSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILS 237
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-239 |
6.94e-12 |
|
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: 64.35 E-value: 6.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 34 IIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLGKLTVKQWQKLRGRDIAYLVQNPmSMFnpfqkieAHiletiL 112
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLErPD----SGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEA-RLF-------PH-----L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 113 ShekcskrV------ALSKALEWMKRLNLDDAIS------LLKKYPFELSGGMLQRIMLA-TILSlDPQVIILDEPTSAV 179
Cdd:COG4148 93 S-------VrgnllyGRKRAPRAERRISFDEVVEllgighLLDRRPATLSGGERQRVAIGrALLS-SPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 180 DCHNCSTISAILQELQNNGKT-LITVTHDYQ-LARdLGGQLLVISEGEVVEQGQTQAILSNP 239
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIpILYVSHSLDeVAR-LADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-245 |
8.71e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.52 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLL--VGHIPQGMTVRGNIFFKGVDLGKLTVKQWQKL 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRDIAYLVQN--PMSMFNPFqkieAHILETILSHEKCS----KRVALSKALEWmkrlnlDDAISLLKKYPFELSGGMLQ 155
Cdd:PRK14258 88 RQVSMVHPKPNlfPMSVYDNV----AYGVKIVGWRPKLEiddiVESALKDADLW------DEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 156 RIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGK-TLITVTHD-YQLARDLGGQLLVISE----GEVVEQ 229
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNlHQVSRLSDFTAFFKGNenriGQLVEF 237
|
250
....*....|....*.
gi 446358294 230 GQTQAILSNPQHNYTK 245
Cdd:PRK14258 238 GLTKKIFNSPHDSRTR 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-206 |
9.37e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGKLTVKQWQKLRg 83
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD---SGEILLDGEPVRFRSPRDAQAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 rdIAY------LVQNpMSmfnpfqkieahILETI-LSHEKCSKRV-----ALSKALEWMKRLNLD-DAISLLKkypfELS 150
Cdd:COG1129 81 --IAIihqelnLVPN-LS-----------VAENIfLGREPRRGGLidwraMRRRARELLARLGLDiDPDTPVG----DLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 151 GGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTH 206
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-230 |
9.40e-12 |
|
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: 63.12 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVR--GNIFFK---------GVDLGKLTvKQWQKLR 82
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRvaGLVPWKrrkkflrriGVVFGQKT-QLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLVqnpmsmfnpfqkieAHILEtiLSHEKCSKRVA-LSKALEWMKrlnlddaisLLKKYPFELSGGMLQRIMLAT 161
Cdd:cd03267 112 VIDSFYLL--------------AAIYD--LPPARFKKRLDeLSELLDLEE---------LLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 162 ILSLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-231 |
1.11e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.81 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 21 DFSCKIDMG-----ESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIffkGVDLgkltvkqwqklrgRDIAYlvqnpm 94
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLkPDE----GDI---EIEL-------------DTVSY------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 95 smfNPfQKIEAHILETI--LSHEKCSKRVALSK-ALEWMKRLNLDdaiSLLKKYPFELSGGMLQRIMLATILSLDPQVII 171
Cdd:cd03237 66 ---KP-QYIKADYEGTVrdLLSSITKDFYTHPYfKTEIAKPLQIE---QILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 172 LDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVIsEGEVVEQGQ 231
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFaENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGV 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-207 |
1.13e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmtvRGNIFFKGVDLGkltvkqwQKLRGRDIAYLVQNPMSMFN 98
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA---SGKISILGQPTR-------QALQKNLVAYVPQSEEVDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 99 PFQKIEAHILETILSH------EKCSKRVALSKALEWMkrlnldDAISLLKKYPFELSGGMLQRIMLATILSLDPQVIIL 172
Cdd:PRK15056 93 FPVLVEDVVMMGRYGHmgwlrrAKKRDRQIVTAALARV------DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....*
gi 446358294 173 DEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD 207
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-206 |
2.65e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 61.33 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGvdlgkltvkqwqklrgrDIAYLVQNP--M 94
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK---LSGSVSVPG-----------------SIAYVSQEPwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 95 SmfnpfqkieAHILETILSHEKCS----KRV----ALSKALEWMKRLNL----DDAISLlkkypfelSGGMLQRIMLATI 162
Cdd:cd03250 79 N---------GTIRENILFGKPFDeeryEKVikacALEPDLEILPDGDLteigEKGINL--------SGGQKQRISLARA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446358294 163 LSLDPQVIILDEPTSAVDCHNCSTI--SAILQELQNNgKTLITVTH 206
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNN-KTRILVTH 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-233 |
3.77e-11 |
|
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: 62.53 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 21 DFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMtvRGNIFFKGvdlgkltvkqwqklrgrdiaylvqNPMSMFNPF 100
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKF--EGNVFING------------------------KPVDIRNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 101 QKIEAHIL--------ETILSHEKCSKRVALSKALEWMKRLNLDDA---------ISLLK---KYPF----ELSGGMLQR 156
Cdd:TIGR02633 332 QAIRAGIAmvpedrkrHGIVPILGVGKNITLSVLKSFCFKMRIDAAaelqiigsaIQRLKvktASPFlpigRLSGGNQQK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 157 IMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV----VEQGQT 232
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLkgdfVNHALT 491
|
.
gi 446358294 233 Q 233
Cdd:TIGR02633 492 Q 492
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-210 |
5.62e-11 |
|
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: 62.11 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 29 GESLTIIGESGSGKTLLAKLLVGHI-PQGMTVRGNIffkgvdlgKLTVKQwQKLRGrDIAYLVQNPMSMFNPfQKIEAHI 107
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDL--------KISYKP-QYISP-DYDGTVEEFLRSANT-DDFGSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 108 LETilshekcskrvalskalEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTI 187
Cdd:COG1245 435 YKT-----------------EIIKPLGLEK---LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180
....*....|....*....|....
gi 446358294 188 SAILQEL-QNNGKTLITVTHDYQL 210
Cdd:COG1245 495 AKAIRRFaENRGKTAMVVDHDIYL 518
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-227 |
6.00e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQ-IGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQWQKLR 82
Cdd:COG3845 258 LEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP---PASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 grdIAY---------LVQNpMSmfnpfqkIEAHILETILSHEKCSKRVALSK------ALEWMKRL-----NLDDAISLL 142
Cdd:COG3845 335 ---VAYipedrlgrgLVPD-MS-------VAENLILGRYRRPPFSRGGFLDRkairafAEELIEEFdvrtpGPDTPARSL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 143 kkypfelSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD----YQLA-Rdlggq 217
Cdd:COG3845 404 -------SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDldeiLALSdR----- 471
|
250
....*....|
gi 446358294 218 LLVISEGEVV 227
Cdd:COG3845 472 IAVMYEGRIV 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-209 |
6.27e-11 |
|
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: 60.42 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 16 VPVLRDFSCKIDMGESLTIIGESGSGKTllaKLLVGHIPQGMTVRGNIFFKGVDLGKLTVKQWQKLRGRDIAYLVQNPMS 95
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKS---SLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 96 MfnpfqkiEAHILETILSHEKCSKRvaLSKALewMKRLNLDDAISLLkkyPF-----------ELSGGMLQRIMLATILS 164
Cdd:cd03290 91 L-------NATVEENITFGSPFNKQ--RYKAV--TDACSLQPDIDLL---PFgdqteigergiNLSGGQRQRICVARALY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446358294 165 LDPQVIILDEPTSAVDCHNCSTI--SAILQELQNNGKTLITVTHDYQ 209
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLmqEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-238 |
6.31e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.15 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 2 EQLEIRKLSLQIGEV---------PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDLg 71
Cdd:PRK11160 330 STAAADQVSLTLNNVsftypdqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQ----QGEILLNGQPI- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 72 kltvKQW--QKLRgrdiaylvqNPMSMFNpfQKIeaHILETIL-----------SHEKCS---KRVALSKALEWMKRLNL 135
Cdd:PRK11160 405 ----ADYseAALR---------QAISVVS--QRV--HLFSATLrdnlllaapnaSDEALIevlQQVGLEKLLEDDKGLNA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 136 ddaisLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITVTHD-YQLAR-D 213
Cdd:PRK11160 468 -----WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN-KTVLMITHRlTGLEQfD 541
|
250 260
....*....|....*....|....*
gi 446358294 214 lggQLLVISEGEVVEQGQTQAILSN 238
Cdd:PRK11160 542 ---RICVMDNGQIIEQGTHQELLAQ 563
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-236 |
7.73e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 60.48 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 5 EIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGK-TLL---AKLLvghipqGMTvRGNIFFKGVDLG--------- 71
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKsTLLsmiSRLL------PPD-SGEVLVDGLDVAttpsrelak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 72 -------------KLTVKQwqklrgrdiayLVqnpmsMFNPFqkieAHiletilSHEKCSK--RVALSKALEWMkrlNLD 136
Cdd:COG4604 76 rlailrqenhinsRLTVRE-----------LV-----AFGRF----PY------SKGRLTAedREIIDEAIAYL---DLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 137 DaisLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLG 215
Cdd:COG4604 127 D---LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYA 203
|
250 260
....*....|....*....|.
gi 446358294 216 GQLLVISEGEVVEQGQTQAIL 236
Cdd:COG4604 204 DHIVAMKDGRVVAQGTPEEII 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-226 |
8.12e-11 |
|
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: 60.18 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGMTVRgniffkgVDLGKLTVKQWQKLRgRDIAYLVQNP 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfYQPQGGQVL-------LDGKPISQYEHKYLH-SKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMFNPFQKIEAHILETilshekcskrVALSKALEWMKRLNLDDAISLLKKYPFE--------LSGGMLQRIMLATILSL 165
Cdd:cd03248 98 VLFARSLQDNIAYGLQS----------CSFECVKEAAQKAHAHSFISELASGYDTevgekgsqLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 166 DPQVIILDEPTSAVDCHNCSTISAILQElQNNGKTLITVTHDYQLARDlGGQLLVISEGEV 226
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-231 |
9.19e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 12 QIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIpQGMTVRGNIFFKGVDLGKLTVKQWQKLRGRDIAYlvq 91
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRTGFVTQDDILY--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 92 npmsmfnPFQKI-EAHILETILSHEKC-SKRVALSKALEWMKRLNLDDAISLLKKYPF--ELSGGMLQRIMLATILSLDP 167
Cdd:PLN03211 153 -------PHLTVrETLVFCSLLRLPKSlTKQEKILVAESVISELGLTKCENTIIGNSFirGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 168 QVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD-----YQLARdlggQLLVISEGEVVEQGQ 231
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpssrvYQMFD----SVLVLSEGRCLFFGK 290
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-227 |
1.25e-10 |
|
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: 60.99 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmTVRGNIFFKGVDLGKLTVKQWQKlRG 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG-TWDGEIYWSGSPLKASNIRDTER-AG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAY----LVQNPMSMFNPFQKIEAHILETILSHEKCSKRvalskALEWMKRLNLDDaiSLLKKYPFELSGGMLQRIML 159
Cdd:TIGR02633 80 IVIIHqeltLVPELSVAENIFLGNEITLPGGRMAYNAMYLR-----AKNLLRELQLDA--DNVTRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-231 |
1.27e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNIFFKGVDL-----GKLTVKQwqklrgrDIAYLV 90
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ----KGAVLWQGKPLdyskrGLLALRQ-------QVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 91 QNP-MSMFnpFQKIEAHILETI----LSHEKCSKRValskalewmkrlnlDDAISLLKKYPFE------LSGGMLQRIML 159
Cdd:PRK13638 84 QDPeQQIF--YTDIDSDIAFSLrnlgVPEAEITRRV--------------DEALTLVDAQHFRhqpiqcLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQ 231
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-227 |
1.55e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtvrgniffkgvDLGklTVKqWQKlrG 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP-------------DSG--TVK-WSE--N 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMSMF----NPFQKIEAHILEtilSHEKCSKRVALSKALewmkrLNLDDAisllKKYPFELSGGMLQRIML 159
Cdd:PRK15064 382 ANIGYYAQDHAYDFendlTLFDWMSQWRQE---GDDEQAVRGTLGRLL-----FSQDDI----KKSVKVLSGGEKGRMLF 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHncsTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDME---SIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-234 |
1.90e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.64 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFkgvdLGKlTVKQWQKLrG 83
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIEL----LGR-TVQREGRL-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMSMFNPFQKI-EAHILETILSHEKCSKRVaLSKALEWMKRLNLDDAISLLKKYPF---------ELSGGM 153
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVnRLSVLENVLIGALGSTPF-WRTCFSWFTREQKQRALQALTRVGMvhfahqrvsTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 154 LQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQT 232
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
..
gi 446358294 233 QA 234
Cdd:PRK09984 238 QQ 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-206 |
2.35e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVD------------LG 71
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP---PAAGTIKLDGGDiddpdvaeachyLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 72 -------KLTVKQ----WQKLRGRDiaylvqnpmsmfnpfqkiEAHILETIlshekcskrvalskalewmKRLNLDDAIS 140
Cdd:PRK13539 80 hrnamkpALTVAEnlefWAAFLGGE------------------ELDIAAAL-------------------EAVGLAPLAH 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 141 LLKKYpfeLSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTH 206
Cdd:PRK13539 123 LPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-235 |
4.03e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 20 RDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLGKLTVKQwqKLRgRDIAYLVQNpmsmfnp 99
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA---RGGRIMLNGKEINALSTAQ--RLA-RGLVYLPED------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 100 fQKIEAHILETILSHEKCS----------KRVALSKALEWMKR---LNLDDAISLLKKypfeLSGGMLQRIMLATILSLD 166
Cdd:PRK15439 347 -RQSSGLYLDAPLAWNVCAlthnrrgfwiKPARENAVLERYRRalnIKFNHAEQAART----LSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 167 PQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAI 235
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-238 |
4.30e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHiPQGmtVRGNIFFKGVDlgkltVKQWQK 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRA--TSGRIVFDGKD-----ITDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 81 LR-GRDIAYLVQNPMSMFNPFqKIEAHILETILSHEKCSKRVALSKALEWMKRLNLDDAisllkKYPFELSGGMLQRIML 159
Cdd:PRK11614 75 AKiMREAVAIVPEGRRVFSRM-TVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRI-----QRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSN 238
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-207 |
7.46e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 26 IDMGESLTIIGESGSGKTLLAKLLVGHI-PqgmtvrgniffkgvDLGKLTVKQwqklrgrDIAYlvqnpmsmfNPfQKIE 104
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLkP--------------DEGEVDPEL-------KISY---------KP-QYIK 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 105 AHILETIlshekcskRVALSKA----------LEWMKRLNLDDaisLLKKYPFELSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:PRK13409 411 PDYDGTV--------EDLLRSItddlgssyykSEIIKPLQLER---LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190
....*....|....*....|....*....|....
gi 446358294 175 PTSAVDCHNCSTIS-AILQELQNNGKTLITVTHD 207
Cdd:PRK13409 480 PSAHLDVEQRLAVAkAIRRIAEEREATALVVDHD 513
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-226 |
9.30e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrgniffkgvdlGKLtvkqwqkLR 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSA--------------GEL-------LA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYLVQNPMSMFnpFQkiEAHILetilSHEKCSKRVALSKALEWMKR-LNLDDAISLLKK---YPFELSGGMLQRIM 158
Cdd:PRK11247 72 GTAPLAEAREDTRLM--FQ--DARLL----PWKKVIDNVGLGLKGQWRDAaLQALAAVGLADRaneWPAALSGGQKQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 159 LATILSLDPQVIILDEPTSAVDchncsTISAI-LQEL-----QNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALD-----ALTRIeMQDLieslwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-243 |
1.05e-09 |
|
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: 58.20 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDM---GESLT-IIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGVDLGKLTVKQWQKLRGRDIAYLVQNP 93
Cdd:TIGR02142 9 LGDFSLDADFtlpGQGVTaIFGRSGSGKTTLIRLIAGLTrPDE----GEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 mSMFnPFQKIEAHILETILSHEKCSKRVALSKALEWmkrLNLDdaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILD 173
Cdd:TIGR02142 85 -RLF-PHLSVRGNLRYGMKRARPSERRISFERVIEL---LGIG---HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 174 EPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSNPQHNY 243
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-262 |
1.15e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVDLG-----KLTV 75
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeqlqKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 76 KQWQKlrgrdiaylvqNPMSMFNP----FQKIEAhilETILSHEKCSKRvalskALEWMKRLNLDDAISLLKKYpfeLSG 151
Cdd:PRK10938 81 DEWQR-----------NNTDMLSPgeddTGRTTA---EIIQDEVKDPAR-----CEQLAQQFGITALLDRRFKY---LST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 152 GMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQ 231
Cdd:PRK10938 139 GETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE 218
|
250 260 270
....*....|....*....|....*....|.
gi 446358294 232 TQAILSnpqhnytKALTVQMEYEGDILNVGL 262
Cdd:PRK10938 219 REEILQ-------QALVAQLAHSEQLEGVQL 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
125-207 |
1.59e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 125 KALEWMKRLNLDdaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITV 204
Cdd:COG1245 192 KLDELAEKLGLE---NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVV 268
|
...
gi 446358294 205 THD 207
Cdd:COG1245 269 EHD 271
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-230 |
1.06e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 15 EVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIffkgvdlgkltvkqwqklRGrDIAYLVQNPM 94
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI------------------RG-SVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 95 sMFNpfqkieAHILETIL--------SHEKCSKRVALSKALEWMKRLNLDDaislLKKYPFELSGGMLQRIMLATILSLD 166
Cdd:PLN03232 690 -IFN------ATVRENILfgsdfeseRYWRAIDVTALQHDLDLLPGRDLTE----IGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 167 PQVIILDEPTSAVDCHNCSTI--SAILQELQnnGKTLITVTHDYQLArDLGGQLLVISEGEVVEQG 230
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVfdSCMKDELK--GKTRVLVTNQLHFL-PLMDRIILVSEGMIKEEG 821
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
148-238 |
1.20e-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: 55.40 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 148 ELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQnNGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:TIGR01257 1061 DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
90
....*....|.
gi 446358294 228 EQGqTQAILSN 238
Cdd:TIGR01257 1140 CSG-TPLFLKN 1149
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-206 |
2.30e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 16 VPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLV--------------------------------------------- 50
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 51 ---GHIPQGMTV---RGNIFFKGVDLGKLTVKQWQKLrgrdIAYLVQNPMsMFNpfqkieAHILETILSHEKCSKRVALS 124
Cdd:PTZ00265 1261 tkeGGSGEDSTVfknSGKILLDGVDICDYNLKDLRNL----FSIVSQEPM-LFN------MSIYENIKFGKEDATREDVK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 125 KALEWMKrlnLDDAI-SLLKKY-----PF--ELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQN 196
Cdd:PTZ00265 1330 RACKFAA---IDEFIeSLPNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1406
|
250
....*....|.
gi 446358294 197 NG-KTLITVTH 206
Cdd:PTZ00265 1407 KAdKTIITIAH 1417
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
118-235 |
2.90e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 118 SKRVALSKALEWMKRLNLDDAISllkKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN 197
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAG---RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
90 100 110
....*....|....*....|....*....|....*...
gi 446358294 198 GKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAI 235
Cdd:NF000106 194 GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
120-230 |
3.13e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.65 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 120 RVALSKALEWMKRLNLDdAISLLKKYPfELSGGMLQRIMLATIL--SLDPQVIILDEPTSAVDCHNCSTISAILQELQNN 197
Cdd:cd03270 111 RVGIRERLGFLVDVGLG-YLTLSRSAP-TLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDL 188
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446358294 198 GKTLITVTHDYQLAR------DLG---GqllvISEGEVVEQG 230
Cdd:cd03270 189 GNTVLVVEHDEDTIRaadhviDIGpgaG----VHGGEIVAQG 226
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-230 |
6.46e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTvRGNIFFKGVDLGKLTVkqwQKLRG 83
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVT-GGTVEFKGKDLLELSP---EDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIAYLVQNPMSM---FNPFqkieahILETILShekcskRVALSKALEWMKRLN----LDDAISLLKkYPFEL------- 149
Cdd:PRK09580 78 EGIFMAFQYPVEIpgvSNQF------FLQTALN------AVRSYRGQEPLDRFDfqdlMEEKIALLK-MPEDLltrsvnv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 150 --SGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHdYQLARDL--GGQLLVISEGE 225
Cdd:PRK09580 145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGR 223
|
....*
gi 446358294 226 VVEQG 230
Cdd:PRK09580 224 IVKSG 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
125-207 |
8.88e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 125 KALEWMKRLNLDdaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNgKTLITV 204
Cdd:PRK13409 192 KLDEVVERLGLE---NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEG-KYVLVV 267
|
...
gi 446358294 205 THD 207
Cdd:PRK13409 268 EHD 270
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-239 |
1.00e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.53 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG-HIPQGmtvrGNIFFKGvdlgkltvKQWQKLR 82
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfYKPTG----GTILLRG--------QHIEGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRDIAYlvqnpMSMFNPFQKI----EAHILETIL--SHEKC----------------SKRVALSKALEWMKRLNLDDais 140
Cdd:PRK11300 74 GHQIAR-----MGVVRTFQHVrlfrEMTVIENLLvaQHQQLktglfsgllktpafrrAESEALDRAATWLERVGLLE--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 141 LLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQLARDLGGQLL 219
Cdd:PRK11300 146 HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIY 225
|
250 260
....*....|....*....|
gi 446358294 220 VISEGEVVEQGQTQAILSNP 239
Cdd:PRK11300 226 VVNQGTPLANGTPEEIRNNP 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-210 |
1.35e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.27 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 6 IRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtvrgniffkgvDLGklTVKQWQKLRgrd 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAP-------------DEG--VIKRNGKLR--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 86 IAYLVQNpmsmfnpfQKIEAHILETILSHEKCSKRVALSKALEWMKRLNlddAISLLKKYPFELSGGMLQRIMLATILSL 165
Cdd:PRK09544 69 IGYVPQK--------LYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQ---AGHLIDAPMQKLSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446358294 166 DPQVIILDEPTSAVDCHNCSTISAILQELQNN-GKTLITVTHDYQL 210
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHL 183
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-228 |
1.62e-07 |
|
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: 51.72 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 29 GESLTIIGESGSGKTLLAKLLVGH-IPQgmtvRGNIFFKGVDLGKLTVKQWQKLrgrdiaylvqnpMS-MFNPFqkieaH 106
Cdd:COG4615 358 GELVFIVGGNGSGKSTLAKLLTGLyRPE----SGEILLDGQPVTADNREAYRQL------------FSaVFSDF-----H 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 107 ILETILSHEkcsKRVALSKALEWMKRLNL-------DDAISLLkkypfELSGGmlQRIMLATILSL--DPQVIILDE--- 174
Cdd:COG4615 417 LFDRLLGLD---GEADPARARELLERLELdhkvsveDGRFSTT-----DLSQG--QRKRLALLVALleDRPILVFDEwaa 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 175 ---P-------TsavdchncstisAILQELQNNGKTLITVTHD---YQLArDlggQLLVISEGEVVE 228
Cdd:COG4615 487 dqdPefrrvfyT------------ELLPELKARGKTVIAISHDdryFDLA-D---RVLKMDYGKLVE 537
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-238 |
2.09e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVKQwqkLRgRDIAYLVQNPMsM 96
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE---LEKGRIMIDDCDVAKFGLTD---LR-RVLSIIPQSPV-L 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNPFQKIEahiLETILSHEKCSkrvaLSKALEwmkRLNLDDAISllkKYPFEL-----------SGGMLQRIMLATILSL 165
Cdd:PLN03232 1322 FSGTVRFN---IDPFSEHNDAD----LWEALE---RAHIKDVID---RNPFGLdaevseggenfSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358294 166 DPQVIILDEPTSAVDCHNCSTISAILQElQNNGKTLITVTHDYQLARDLgGQLLVISEGEVVEQGQTQAILSN 238
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-240 |
2.40e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVG--HIPQGMTVRGNIFFKGVDLGKltvkqw 78
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDITSGDLFIGEKRMNDVPPAE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 79 qklRGrdiaylvqnpMSMFnpFQkieAHILETILS-HEKCSKRVALSKA--LEWMKRLNLDDAI----SLLKKYPFELSG 151
Cdd:PRK11000 75 ---RG----------VGMV--FQ---SYALYPHLSvAENMSFGLKLAGAkkEEINQRVNQVAEVlqlaHLLDRKPKALSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 152 GMLQRIMLATILSLDPQVIILDEPTSAVDC----HNCSTISAILQELqnnGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
250
....*....|...
gi 446358294 228 EQGQTQAILSNPQ 240
Cdd:PRK11000 214 QVGKPLELYHYPA 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-229 |
2.97e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGK-TLL---AKLLV---GHIPQGMTVRGNIffkgvdlgkltvkqwqKLRGRDI 86
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKsTLLrmvAGLERitsGEIWIGGRVVNEL----------------EPADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 87 AYLVQN----P-MSMFN-----------PFQKIEAHILETilshekcskrvalSKALEwmkrlnLDDaisLLKKYPFELS 150
Cdd:PRK11650 79 AMVFQNyalyPhMSVREnmayglkirgmPKAEIEERVAEA-------------ARILE------LEP---LLDRKPRELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 151 GGMLQRIMLATILSLDPQVIILDEPTSAVDC----HNCSTIsailQELQNN-GKTLITVTHDyQL-ARDLGGQLLVISEG 224
Cdd:PRK11650 137 GGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvQMRLEI----QRLHRRlKTTSLYVTHD-QVeAMTLADRVVVMNGG 211
|
....*
gi 446358294 225 eVVEQ 229
Cdd:PRK11650 212 -VAEQ 215
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
149-214 |
3.29e-07 |
|
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: 48.90 E-value: 3.29e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLATILSL----DPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDL 214
Cdd:cd03227 78 LSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELA 147
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-236 |
3.42e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGvdlgkltvkqwqklrgrDIAYLVQNP 93
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK---VEGHVHMKG-----------------SVAYVPQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MSMFNPFQKieaHILETILSHEKCSKRVALSKAL-EWMKRLNLDDAISLLKKyPFELSGGMLQRIMLATILSLDPQVIIL 172
Cdd:TIGR00957 709 WIQNDSLRE---NILFGKALNEKYYQQVLEACALlPDLEILPSGDRTEIGEK-GVNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 173 DEPTSAVDCHNCSTI--SAILQELQNNGKTLITVTH--DYQLARDLggqLLVISEGEVVEQGQTQAIL 236
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIfeHVIGPEGVLKNKTRILVTHgiSYLPQVDV---IIVMSGGKISEMGSYQELL 849
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
148-228 |
3.77e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 148 ELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVV 227
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
.
gi 446358294 228 E 228
Cdd:PRK09700 489 Q 489
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-206 |
4.42e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGmtvrGNIFFKGvdlgkltvkqwQKLR 82
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPDS----GEILIDG-----------KPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 GRD--------IAYLVQNPMSmfnpfqkIEAH-ILETI-LSHEKcskrvalskalEWMKRLNLDDAI----SLLKKYPFE 148
Cdd:COG3845 71 IRSprdaialgIGMVHQHFML-------VPNLtVAENIvLGLEP-----------TKGGRLDRKAARarirELSERYGLD 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 149 ---------LSGGMLQRIMLATILSLDPQVIILDEPTS-----AVDchncsTISAILQELQNNGKTLITVTH 206
Cdd:COG3845 133 vdpdakvedLSVGEQQRVEILKALYRGARILILDEPTAvltpqEAD-----ELFEILRRLAAEGKSIIFITH 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-233 |
5.47e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 21 DFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqGMTvRGNIFFKGvdlgkltvkqwQKLRGRDIAYLVQNPMSMFNPF 100
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP-GRW-EGEIFIDG-----------KPVKIRNPQQAIAQGIAMVPED 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 101 QKIEAHILE-------TILSHEKCSKRVALSKALE------WMKRLNLDDAISLLKKYpfELSGGMLQRIMLATILSLDP 167
Cdd:PRK13549 347 RKRDGIVPVmgvgkniTLAALDRFTGGSRIDDAAElktileSIQRLKVKTASPELAIA--RLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 168 QVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHdyQLARDLG--GQLLVISEGEV----VEQGQTQ 233
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISS--ELPEVLGlsDRVLVMHEGKLkgdlINHNLTQ 494
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-206 |
5.55e-07 |
|
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: 50.13 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVpVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmtVRGniffkgvdlGKLTVKQWQKL----------RG 83
Cdd:TIGR00954 464 GDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP----VYG---------GRLTKPAKGKLfyvpqrpymtLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 --RD-IAYlvqnPMSMFNPFQK-IEAHILETILS----HEKCSKRVALSKALEWMKrlnlddaisllkkypfELSGGMLQ 155
Cdd:TIGR00954 530 tlRDqIIY----PDSSEDMKRRgLSDKDLEQILDnvqlTHILEREGGWSAVQDWMD----------------VLSGGEKQ 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446358294 156 RIMLATILSLDPQVIILDEPTSAVdchNCSTISAILQELQNNGKTLITVTH 206
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAV---SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-226 |
5.55e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVL-RDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVrgnifFKGVDLgKLTVKQWQKLRGRDiayLVQNP- 93
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELqPSSGTV-----FRSAKV-RMAVFSQHHVDGLD---LSSNPl 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 ---MSMFN--PFQKIEAHIletilshekCSKRVALSKALEWMkrlnlddaisllkkypFELSGGMLQRIMLATILSLDPQ 168
Cdd:PLN03073 593 lymMRCFPgvPEQKLRAHL---------GSFGVTGNLALQPM----------------YTLSGGQKSRVAFAKITFKKPH 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 169 VIILDEPTSAVDchnCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:PLN03073 648 ILLLDEPSNHLD---LDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
149-237 |
6.10e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDyqLARDLG--GQLLVISEGEV 226
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSD--LPEVLGvaDRIVVMREGRI 474
|
90
....*....|....*.
gi 446358294 227 V-----EQGQTQAILS 237
Cdd:PRK11288 475 AgelarEQATERQALS 490
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
128-207 |
6.74e-07 |
|
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: 49.29 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 128 EWMKRLNLDdaiSLLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD 207
Cdd:cd03236 122 ELVDQLELR---HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-228 |
8.10e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 26 IDMGESLTIIGESGSGKTLLAKLLVG-HIPQgmtvRGNIFfkgVDLGKLTVKQWQKLRgrdiaylvQNPMSMFNPFqkie 104
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGlYQPQ----SGEIL---LDGKPVTAEQPEDYR--------KLFSAVFTDF---- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 105 aHILETILSHEKCSKRVALskALEWMKRLNL-------DDAISLLKkypfeLSGGmlQRIMLATILSLDPQ--VIILDEP 175
Cdd:PRK10522 407 -HLFDQLLGPEGKPANPAL--VEKWLERLKMahkleleDGRISNLK-----LSKG--QKKRLALLLALAEErdILLLDEW 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 176 TSAVDCHNCSTI-SAILQELQNNGKTLITVTHD--YQLARDlggQLLVISEGEVVE 228
Cdd:PRK10522 477 AADQDPHFRREFyQVLLPLLQEMGKTIFAISHDdhYFIHAD---RLLEMRNGQLSE 529
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
80-240 |
8.50e-07 |
|
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: 49.63 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 KLRGRDIAYLVQNPM----SMFN-----PFQK-IEAHILETILSHEKCSKRVALSkalewmkRLNLDDAISllkkypfEL 149
Cdd:TIGR00630 424 TVGGKSIADVSELSIreahEFFNqltltPEEKkIAEEVLKEIRERLGFLIDVGLD-------YLSLSRAAG-------TL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 150 SGGMLQRIMLATIL--SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLAR------DLG---Gql 218
Cdd:TIGR00630 490 SGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRaadyviDIGpgaG-- 567
|
170 180
....*....|....*....|..
gi 446358294 219 lvISEGEVVEQGQTQAILSNPQ 240
Cdd:TIGR00630 568 --EHGGEVVASGTPEEILANPD 587
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-206 |
9.79e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 12 QIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTvrgniffkgvdlGKLTVkqWQKLRG-------- 83
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYS------------NDLTL--FGRRRGsgetiwdi 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 -RDIAYlVQNPMSMFnpfQKIEAHILETILS--------HEKCSKRVALsKALEWMKRLNLDDAISllkKYPFE-LSGGM 153
Cdd:PRK10938 335 kKHIGY-VSSSLHLD---YRVSTSVRNVILSgffdsigiYQAVSDRQQK-LAQQWLDILGIDKRTA---DAPFHsLSWGQ 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446358294 154 lQRIML-ATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKT-LITVTH 206
Cdd:PRK10938 407 -QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-237 |
1.89e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGKTllaKLLVGHIPQGMTVRGNIFFKGVDLGKLTVkqwQKLRGRdIAYLVQNPMSM- 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKS---SLTLGLFRINESAEGEIIIDGLNIAKIGL---HDLRFK-ITIIPQDPVLFs 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 ------FNPFQKieahiletiLSHEKCSKRVALSkalewmkrlNLDDAISLL-KKYPFE-------LSGGMLQRIMLATI 162
Cdd:TIGR00957 1374 gslrmnLDPFSQ---------YSDEEVWWALELA---------HLKTFVSALpDKLDHEcaeggenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446358294 163 LSLDPQVIILDEPTSAVDCHNCSTISAILQElQNNGKTLITVTHDYQLARDLgGQLLVISEGEVVEQGQTQAILS 237
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-209 |
2.06e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 5 EIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQGMTVR-GNiffkgvdlgKLtvkqwqklr 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLqADSGRIHcGT---------KL--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 grDIAYLVQNPMSMfNPFQKIEAHILE---TILSHEKcsKRVALSKALEWM---KRlnlddAISLLKKypfeLSGGMLQR 156
Cdd:PRK11147 383 --EVAYFDQHRAEL-DPEKTVMDNLAEgkqEVMVNGR--PRHVLGYLQDFLfhpKR-----AMTPVKA----LSGGERNR 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446358294 157 IMLATILsLDP-QVIILDEPTSAVDCHNCSTISAILQELQNngkTLITVTHDYQ 209
Cdd:PRK11147 449 LLLARLF-LKPsNLLILDEPTNDLDVETLELLEELLDSYQG---TVLLVSHDRQ 498
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-238 |
2.50e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 14 GEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmTVRGNIFfkgvdlgkltvkqwqkLRGRdIAYLVQnp 93
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP--RSDASVV----------------IRGT-VAYVPQ-- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 94 MS-MFNpfqkieAHILETIL--------SHEKCSKRVALSKALEWMKRLNLDDaislLKKYPFELSGGMLQRIMLATILS 164
Cdd:PLN03130 687 VSwIFN------ATVRDNILfgspfdpeRYERAIDVTALQHDLDLLPGGDLTE----IGERGVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 165 LDPQVIILDEPTSAVDCHNCSTI--SAILQELQnnGKTLITVTHDYQLARDLgGQLLVISEGEVVEQGQTQAILSN 238
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVfdKCIKDELR--GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-230 |
4.14e-06 |
|
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: 46.10 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 6 IRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVDlgkltVKQWQKLRGRD 85
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIP-----YKEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 86 IAYLVQNPMSMfnpfqkieAHIL--ETilshekcskrvalskaLEWMKRLNLDDAISllkkypfELSGGMLQRIMLATIL 163
Cdd:cd03233 85 IIYVSEEDVHF--------PTLTvrET----------------LDFALRCKGNEFVR-------GISGGERKRVSIAEAL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 164 SLDPQVIILDEPTSAVDchnCSTISAILQELQN-----NGKTLITVTHDYQLARDLGGQLLVISEGEVVEQG 230
Cdd:cd03233 134 VSRASVLCWDNSTRGLD---SSTALEILKCIRTmadvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-207 |
7.33e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 1 MEQLEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIP---------QGMTV-----------R 60
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLlddgriiyeQDLIVarlqqdpprnvE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 61 GNIF---FKGV-DLGKLtVKQWQklrgrDIAYLV-QNPM-SMFNPFQKIEAhiletILSHE---KCSKRVAlskalEWMK 131
Cdd:PRK11147 81 GTVYdfvAEGIeEQAEY-LKRYH-----DISHLVeTDPSeKNLNELAKLQE-----QLDHHnlwQLENRIN-----EVLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446358294 132 RLNLDDAISLLkkypfELSGGMLQRIMLATILSLDPQVIILDEPTSAVDchnCSTISAILQELQNNGKTLITVTHD 207
Cdd:PRK11147 145 QLGLDPDAALS-----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD---IETIEWLEGFLKTFQGSIIFISHD 212
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
141-240 |
1.04e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 141 LLKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKT-LITVTHDYQLARDLGGQLL 219
Cdd:PRK11144 121 LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVV 200
|
90 100
....*....|....*....|.
gi 446358294 220 VISEGEVVEQGQTQAILSNPQ 240
Cdd:PRK11144 201 VLEQGKVKAFGPLEEVWASSA 221
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
148-225 |
3.13e-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: 43.33 E-value: 3.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 148 ELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQEL-QNNGKTLITVTHDYQLARDLGGQLLVIsEGE 225
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLsEEGKKTALVVEHDLAVLDYLSDRIHVF-EGE 148
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
149-219 |
3.68e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLATIL---SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLAR------------- 212
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKvadyvlelgpegg 889
|
....*..
gi 446358294 213 DLGGQLL 219
Cdd:PRK00635 890 NLGGYLL 896
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-241 |
4.72e-05 |
|
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: 44.52 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 18 VLRDFSCKIDMGESLTIIGESGSGK-TLLAKLLvghipQGMTVRGNIFFKGVDLGKLTVKQWQKLRGrdiaYLVQNPMSM 96
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKsTLLSALL-----RLLSTEGEIQIDGVSWNSVTLQTWRKAFG----VIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNPFQK-IEAHILETILSHEKCSKRVALSKALE-WMKRLNLddaisLLKKYPFELSGGMLQRIMLA-TILSlDPQVIILD 173
Cdd:TIGR01271 1305 SGTFRKnLDPYEQWSDEEIWKVAEEVGLKSVIEqFPDKLDF-----VLVDGGYVLSNGHKQLMCLArSILS-KAKILLLD 1378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 174 EPTSAVDCHNCSTISAILQELQNNGkTLITVTHDYQLARDLgGQLLVISEGEVVEQGQTQAILSNPQH 241
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQSFSNC-TVILSEHRVEALLEC-QQFLVIEGSSVKQYDSIQKLLNETSL 1444
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
149-240 |
4.92e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLAT-I---LSldpQVI-ILDEPTsavdchncstIS----------AILQELQNNGKTLITVTHDYQLAR- 212
Cdd:COG0178 486 LSGGEAQRIRLATqIgsgLV---GVLyVLDEPS----------IGlhqrdndrliETLKRLRDLGNTVIVVEHDEDTIRa 552
|
90 100 110
....*....|....*....|....*....|....*....
gi 446358294 213 -----DLG------GqllviseGEVVEQGQTQAILSNPQ 240
Cdd:COG0178 553 adyiiDIGpgagehG-------GEVVAQGTPEEILKNPD 584
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
149-207 |
5.13e-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: 42.70 E-value: 5.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 149 LSGGMLQRIMLATIL--SLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHD 207
Cdd:cd03238 88 LSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-206 |
5.13e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGmTVRGNIFFKGvdlgkltvkqwQKLRG 83
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHG-SYEGEILFDG-----------EVCRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 84 RDIA--------------YLVqnP-MSmfnpfqkieahILETI-LSHEKCSKRV-----ALSKALEWMKRLNLDDAISLL 142
Cdd:NF040905 70 KDIRdsealgiviihqelALI--PyLS-----------IAENIfLGNERAKRGVidwneTNRRARELLAKVGLDESPDTL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 143 KKypfELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTH 206
Cdd:NF040905 137 VT---DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-206 |
5.22e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 10 SLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMTVRGNIFFKGVDLGKLTVKQWQKLRGRDI--- 86
Cdd:PLN03073 184 SISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDGIPKNCQILHVEQEVVGDDTTALQCVLNTDIert 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 87 ------AYLVQNPMSMFNPFQKIEAHI-LETILSHEKCSKRVAlskalEWMKRLNLDDAIS-----------------LL 142
Cdd:PLN03073 264 qlleeeAQLVAQQRELEFETETGKGKGaNKDGVDKDAVSQRLE-----EIYKRLELIDAYTaearaasilaglsftpeMQ 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 143 KKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQnngKTLITVTH 206
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSH 399
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
149-215 |
5.39e-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: 44.23 E-value: 5.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358294 149 LSGGMLQRIMLATILS---LDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTH--------DYQLarDLG 215
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHnldviktaDYII--DLG 905
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-207 |
5.55e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.16 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGH-IPQGMTVRgniffkgvdLGKlTVKqwqklr 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTIE---------IGE-TVK------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 83 grdIAYLVQNPMSMfNPfqkiEAHILETI---LSHEKCSKRVALSKAleWMKRLNLDDAISllKKYPFELSGGMLQRIML 159
Cdd:TIGR03719 387 ---LAYVDQSRDAL-DP----NKTVWEEIsggLDIIKLGKREIPSRA--YVGRFNFKGSDQ--QKKVGQLSGGERNRVHL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446358294 160 ATILSLDPQVIILDEPTSAVDCHncsTISAILQELQNNGKTLITVTHD 207
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVE---TLRALEEALLNFAGCAVVISHD 499
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
119-206 |
6.30e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.75 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 119 KRVALSKALEWMKRLNLD-DAISLLKkypfELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNN 197
Cdd:PRK11288 114 RRLLNYEAREQLEHLGVDiDPDTPLK----YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE 189
|
....*....
gi 446358294 198 GKTLITVTH 206
Cdd:PRK11288 190 GRVILYVSH 198
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-237 |
6.96e-05 |
|
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: 42.97 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPqgmTVRGNIFFKGVDLGKLTVkqwQKLRGRdIAYLVQNPMsM 96
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD---IFDGKIVIDGIDISKLPL---HTLRSR-LSIILQDPI-L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNpfqkieAHILETILSHEKCSKRvALSKALEWMKRLNLDDAI-----SLLKKYPFELSGGMLQRIMLATILSLDPQVII 171
Cdd:cd03288 107 FS------GSIRFNLDPECKCTDD-RLWEALEIAQLKNMVKSLpggldAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 172 LDEPTSAVDChncsTISAILQELQNNG---KTLITVTHDYQLARDlGGQLLVISEGEVVEQGQTQAILS 237
Cdd:cd03288 180 MDEATASIDM----ATENILQKVVMTAfadRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-241 |
7.20e-05 |
|
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: 43.30 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLSLQIGEV--PVLRDFSCKIDMGESLTIIGESGSGK-TLLAKLLvghipQGMTVRGNIFFKGVDLGKLTVKQWQ 79
Cdd:cd03289 2 QMTVKDLTAKYTEGgnAVLENISFSISPGQRVGLLGRTGSGKsTLLSAFL-----RLLNTEGDIQIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 80 KLRGrdiaYLVQNPMSMFNPFQK----IEAHILETILsheKCSKRVALSKALE-WMKRLNLddaisLLKKYPFELSGGML 154
Cdd:cd03289 77 KAFG----VIPQKVFIFSGTFRKnldpYGKWSDEEIW---KVAEEVGLKSVIEqFPGQLDF-----VLVDGGCVLSHGHK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 155 QRIMLATILSLDPQVIILDEPTSAVDchnCSTISAILQELQNNGKTLITVTHDYQLARDLGGQ-LLVISEGEVVEQGQTQ 233
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLD---PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQrFLVIEENKVRQYDSIQ 221
|
....*...
gi 446358294 234 AILSNPQH 241
Cdd:cd03289 222 KLLNEKSH 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
149-202 |
1.49e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLI 202
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI 458
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-206 |
1.61e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.46 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 31 SLT-IIGESGSGKTLLAKLLVGHIPQGmTVRGNIFFKGVDLGKltvkqwqKLRgRDIAYLVQNPmsMFNPFQKIEahilE 109
Cdd:cd03232 34 TLTaLMGESGAGKTTLLDVLAGRKTAG-VITGEILINGRPLDK-------NFQ-RSTGYVEQQD--VHSPNLTVR----E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 110 TILSHEKCSkrvALSkaLEWMKRLNlddaisllkkypfelsggmlqrimLATILSLDPQVIILDEPTSAVDCHNCSTISA 189
Cdd:cd03232 99 ALRFSALLR---GLS--VEQRKRLT------------------------IGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170
....*....|....*..
gi 446358294 190 ILQELQNNGKTLITVTH 206
Cdd:cd03232 150 FLKKLADSGQAILCTIH 166
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
148-215 |
1.62e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 1.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 148 ELSGGMLQRIMLATILSL---DPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLAR------DLG 215
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKcadwiiDLG 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-226 |
1.94e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 8 KLSLQIGEV--PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQgmtVRGNIFFKGVDLgklTVKQWQKLRGRD 85
Cdd:PRK10762 255 EVRLKVDNLsgPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPR---TSGYVTLDGHEV---VTRSPQDGLANG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 86 IAYL--------------VQNPMSM--FNPFQKIEAHIletilSHEKCSKRVALSKALEWMKRLNLDDAISLLkkypfel 149
Cdd:PRK10762 329 IVYIsedrkrdglvlgmsVKENMSLtaLRYFSRAGGSL-----KHADEQQAVSDFIRLFNIKTPSMEQAIGLL------- 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446358294 150 SGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
156-207 |
2.53e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446358294 156 RIMLATILSLDPQVIILDEPTSAVDCHncsTISAILQELQNNGKTLITVTHD 207
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDIN---TIRWLEDVLNERNSTMIIISHD 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-226 |
3.84e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 4 LEIRKLSLQIGEVPVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI-PQgmtvRGNI-FFKGVDLGKLTVKQWQKL 81
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELaPV----SGEIgLAKGIKLGYFAQHQLEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 82 RGRDiaylvqnpmsmfNPFQKIeahiletilshekcsKRVAlSKALEWMKRlnlddaiSLLKKYPFE----------LSG 151
Cdd:PRK10636 389 RADE------------SPLQHL---------------ARLA-PQELEQKLR-------DYLGGFGFQgdkvteetrrFSG 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446358294 152 GMLQRIMLATILSLDPQVIILDEPTSAVDchnCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV 226
Cdd:PRK10636 434 GEKARLVLALIVWQRPNLLLLDEPTNHLD---LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-206 |
4.97e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 3 QLEIRKLslqigevpvLRDFSCKIDMGESLTIIGESGSGK-TLLAKLL---------------VGHIPQ-----GMTVRG 61
Cdd:PTZ00243 669 ELEPKVL---------LRDVSVSVPRGKLTVVLGATGSGKsTLLQSLLsqfeisegrvwaersIAYVPQqawimNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 62 NI-FFKGVDLGKLT----VKQWQklrgrdiAYLVQNPMSMfnpfqkiEAHILEtilshekcskrvalskalewmKRLNld 136
Cdd:PTZ00243 740 NIlFFDEEDAARLAdavrVSQLE-------ADLAQLGGGL-------ETEIGE---------------------KGVN-- 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446358294 137 daisllkkypfeLSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTI--SAILQELQnnGKTLITVTH 206
Cdd:PTZ00243 783 ------------LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVveECFLGALA--GKTRVLATH 840
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
149-180 |
5.41e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 5.41e-04
10 20 30
....*....|....*....|....*....|..
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVD 180
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-214 |
6.60e-04 |
|
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: 39.28 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 29 GESLTIIGESGSGKTLLAKLLVGHIPqgmtvRGNIFFKGVDLGKLTVKQWQKLRGRDIaylvqnpmsmfnpfqkieahil 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELG-----PPGGGVIYIDGEDILEEVLDQLLLIIV---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 109 etilshekcskrvalskalewmkrlnlddaisllKKYPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHN----- 183
Cdd:smart00382 55 ----------------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQealll 100
|
170 180 190
....*....|....*....|....*....|..
gi 446358294 184 -CSTISAILQELQNNGKTLITVTHDYQLARDL 214
Cdd:smart00382 101 lLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
120-180 |
7.08e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 7.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 120 RVAlskalEWMKRLNLDDAISLLkkyPFELSGGMLQRIMLATILSLDPQVIILDEPTSAVD 180
Cdd:NF033858 377 RVA-----EMLERFDLADVADAL---PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
149-207 |
7.17e-04 |
|
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: 40.69 E-value: 7.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHncsTISAILQELQNNGKTLITVTHD 207
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHD 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-206 |
8.93e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 8.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 148 ELSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQ-NNGKTLITVTH 206
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAH 638
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-53 |
9.33e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 39.84 E-value: 9.33e-04
10 20 30
....*....|....*....|....*....|....*..
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHI 53
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGEL 87
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
227-247 |
9.84e-04 |
|
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: 36.61 E-value: 9.84e-04
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
149-232 |
1.40e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 149 LSGGMLQRIMLATILSLDPQVIILDEPTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEV-- 226
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVag 471
|
....*..
gi 446358294 227 -VEQGQT 232
Cdd:PRK10982 472 iVDTKTT 478
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
148-206 |
1.45e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 1.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 148 ELSGGMLQRIMLATILSLDPQVIILDEPTSAV-DCHNCSTISAIlQELQNNGKTLITVTH 206
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVI-RELKSQGRGIVYISH 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-205 |
2.56e-03 |
|
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: 39.12 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGHIPQGMtvrgniffkgvdlGKLtvkqwqKLRGRdIAYLVQNPMSM 96
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE-------------GKI------KHSGR-ISFSPQTSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 97 FNpfqKIEAHILETILSHEKCSKRValskalewMKRLNLDDAISLL---KKYPF-----ELSGGMLQRIMLATILSLDPQ 168
Cdd:TIGR01271 500 PG---TIKDNIIFGLSYDEYRYTSV--------IKACQLEEDIALFpekDKTVLgeggiTLSGGQRARISLARAVYKDAD 568
|
170 180 190
....*....|....*....|....*....|....*...
gi 446358294 169 VIILDEPTSAVDCHNCSTI-SAILQELQNNgKTLITVT 205
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIfESCLCKLMSN-KTRILVT 605
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-238 |
5.32e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 37.95 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 19 LRDFSCKIDMGESLTIIGESGSGKTLLAKLLVGhipQGMTVRGNIFFKG-VDLGKLTVKQWQKLRGrdiaylvqnpmsmf 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAG---VTMPNKGTVDIKGsAALIAISSGLNGQLTG-------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 98 npFQKIEAHILETILSHEKCSKrvALSKALEWM---KRLNlddaiSLLKKYpfelSGGMLQRIMLATILSLDPQVIILDE 174
Cdd:PRK13545 103 --IENIELKGLMMGLTKEKIKE--IIPEIIEFAdigKFIY-----QPVKTY----SSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358294 175 PTSAVDCHNCSTISAILQELQNNGKTLITVTHDYQLARDLGGQLLVISEGEVVEQGQTQAILSN 238
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
17-146 |
7.43e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.23 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358294 17 PVLRDFSCKIDMGeSLTIIGESGSGKTLLAKLLVGhipQGMTVRGNIFF--KGVDLGKLTvkqwQKLRGRDIAYLVQNPM 94
Cdd:COG3451 193 PVFFDFHDGLDNG-NTLILGPSGSGKSFLLKLLLL---QLLRYGARIVIfdPGGSYEILV----RALGGTYIDLSPGSPT 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446358294 95 SmFNPFQ------KIE--AHILETILSHEKCS----KRVALSKALEWM-------KRLNLDDAISLLKKYP 146
Cdd:COG3451 265 G-LNPFDledteeKRDflLELLELLLGREGEPltpeERAAIDRAVRALyrradpeERTTLSDLYELLKEQP 334
|
|
| |
