|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-244 |
3.75e-87 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 259.25 E-value: 3.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWasQELANKSGVIGYVPQ 90
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLlPPTSGTVRLFG--KPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 KAMFEASLPLTVMDFILLN-QTRFPLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLV 169
Cdd:COG1121 83 RAEVDWDFPITVRDVVLMGrYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 170 LDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDILVPEKIERIFNH 244
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGG 237
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-227 |
2.86e-69 |
|
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: 212.78 E-value: 2.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKSGVIGYVPQKAM 93
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLlKPTSGSIRV--FGKPLEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 94 FEASLPLTVMDFILLNQTRFPLFWRKRGKEQ-QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDE 172
Cdd:cd03235 79 IDRDFPISVRDVVLMGLYGHKGLFRRLSKADkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 173 PTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSG 227
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-243 |
4.53e-56 |
|
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: 180.24 E-value: 4.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDI------QWASQELANKsgvIG 86
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLdgrdlaSLSRRELARR---IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKAmfEASLPLTVMDFILLNqtRFPL--FWRKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:COG1120 79 YVPQEP--PAPFGLTVRELVALG--RYPHlgLFGRPSAEDREAVEEaLERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 164 DPALLVLDEPTTGMDeqgVRY----LECLIKECVKEGKTVLAVHHDVT-AVRRLDaHVHVVNR-ILVDSGRHQDILVPEK 237
Cdd:COG1120 155 EPPLLLLDEPTSHLD---LAHqlevLELLRRLARERGRTVVMVLHDLNlAARYAD-RLVLLKDgRIVAQGPPEEVLTPEL 230
|
....*.
gi 1055853272 238 IERIFN 243
Cdd:COG1120 231 LEEVYG 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-246 |
4.64e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 4.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI-----DIQWASQELANKsgvIGY 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTSGEVrvlgeDVARDPAEVRRR---IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQKAMFEASLplTVMDFILLnqtrFPLFWRKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPA 166
Cdd:COG1131 78 VPQEPALYPDL--TVRENLRF----FARLYGLPRKEARERIDElLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 167 LLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDSGRHQDILvpEKI-ERIFNH 244
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPDELK--ARLlEDVFLE 229
|
..
gi 1055853272 245 YT 246
Cdd:COG1131 230 LT 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-213 |
7.22e-46 |
|
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: 152.63 E-value: 7.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWASQELANKS--GVIGYV 88
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLlPPSAGEVLWNGEPIRDAREDyrRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQK-AMFEAslpLTVMDFILlnqtrfplFWRK-RGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:COG4133 81 GHAdGLKPE---LTVRENLR--------FWAAlYGLRADREAIDeaLEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHD---VTAVRRLD 213
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQpleLAAARVLD 201
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-221 |
2.06e-41 |
|
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: 139.84 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANKsgvIGY 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLlKPDSGEIkvlgkDIKKEPEEVKRR---IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQKAMFEASLplTVMDFIllnqtrfplfwrkrgkeqqnalaqlervgmasradrrmgQLSGGEQQRVLFAQALLDDPAL 167
Cdd:cd03230 78 LPEEPSLYENL--TVRENL---------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 168 LVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-228 |
1.11e-40 |
|
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: 138.34 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKsgvIGY 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLlKPSSGEILLdgkdlaSLSPKELARK---IAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQkamfeaslpltvmdfillnqtrfplfwrkrgkeqqnalaQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPAL 167
Cdd:cd03214 78 VPQ---------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 168 LVLDEPTTGMDeqgVRY----LECLIKECVKEGKTVLAVHHDVTAVRRLDAHVhvvnrILVDSGR 228
Cdd:cd03214 119 LLLDEPTSHLD---IAHqielLELLRRLARERGKTVVMVLHDLNLAARYADRV-----ILLKDGR 175
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-220 |
2.14e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.41 E-value: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiQWASQELANKSGV-----IGY 87
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLdPPTSGEI--YLDGKPLSAMPPPewrrqVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQK-AMFEAslplTVMDFIllnqtRFPLFWRKRGKEQQNALAQLERVGMASRA-DRRMGQLSGGEQQRVLFAQALLDDP 165
Cdd:COG4619 79 VPQEpALWGG----TVRDNL-----PFPFQLRERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 166 ALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRL-DAHVHVVN 220
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVaDRVLTLEA 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-233 |
4.38e-40 |
|
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: 145.05 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHY--GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQI--DIQWASQELANKS----- 82
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIsgEVLLDGRDLLELSealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 GVIGYVPQKAMfeASL-PLTVMDfillnQTRFPLFWRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:COG1123 83 RRIGMVFQDPM--TQLnPVTVGD-----QIAEALENLGLSRAEarARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDSGRHQDIL 233
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEIL 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-216 |
6.15e-40 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 136.98 E-value: 6.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 23 YGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGqidiqwasqELANKSGV-IGYVPQKAMFEASLPL 100
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvLRPTSG---------TVRRAGGArVAYVPQRSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 101 TVMDFILLNQTRFPLFWRKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDE 179
Cdd:NF040873 73 TVRDLVAMGRWARRGLWRRLTRDDRAAVDDaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055853272 180 QGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHV 216
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-244 |
7.70e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 138.71 E-value: 7.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDI------QWASQELANKSGVig 86
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLngrplaAWSPWELARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 yVPQKAmfEASLPLTVMDFILLNqtRFPLFwRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALL---- 162
Cdd:COG4559 80 -LPQHS--SLAFPFTVEEVVALG--RAPHG-SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 163 ---DDPALLVLDEPTTGMD---EQGVryLEcLIKECVKEGKTVLAVHHDVTavrrLDAHV--HVV---NRILVDSGRHQD 231
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDlahQHAV--LR-LARQLARRGGGVVAVLHDLN----LAAQYadRILllhQGRLVAQGTPEE 226
|
250
....*....|...
gi 1055853272 232 ILVPEKIERIFNH 244
Cdd:COG4559 227 VLTDELLERVYGA 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-213 |
8.50e-40 |
|
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: 137.24 E-value: 8.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGEN----TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELA--- 79
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVdgtdisKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 80 NKSgvIGYVPQkamFEASLP-LTVMDFILLnqtrfPLFWRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:cd03255 81 RRH--IGFVFQ---SFNLLPdLTALENVEL-----PLLLAGVPKKErrERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQ-GVRYLECLIKECVKEGKTVLAVHHDVTAVRRLD 213
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVTHDPELAEYAD 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-244 |
3.01e-39 |
|
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: 136.48 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWAS----QELANKsg 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLlRPDSGEVlidgeDISGLSeaelYRLRRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 vIGYVPQK-AMFEAslpLTVMDFIllnqtRFPLFWRKRGKE---QQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:cd03261 79 -MGMLFQSgALFDS---LTVFENV-----AFPLREHTRLSEeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRldahvhVVNRILV-DSGRhqdILVPEK 237
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFA------IADRIAVlYDGK---IVAEGT 220
|
....*..
gi 1055853272 238 IERIFNH 244
Cdd:cd03261 221 PEELRAS 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-211 |
3.19e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.73 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHY-GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIdiQWASQELANKSGV----- 84
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVePTSGEI--LVDGQDVTALRGRalrrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ---IGYVPQKamFEasLP--LTVMDFIL---LNQTR-----FPLFWRKrgkEQQNALAQLERVGMASRADRRMGQLSGGE 151
Cdd:COG3638 79 rrrIGMIFQQ--FN--LVprLSVLTNVLagrLGRTStwrslLGLFPPE---DRERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 152 QQRVLFAQALLDDPALLVLDEPTTGMDEQ-GVRYLECLIKECVKEGKTVLAVHHDVTAVRR 211
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLRRIAREDGITVVVNLHQVDLARR 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-228 |
1.33e-37 |
|
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: 131.44 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHY--GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQ---WASQELANKSGVIGYV 88
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLlGPTSGEVLVDgkdLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQKA--MFeasLPLTVMD---FILLNQTRfplfwrKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:cd03225 81 FQNPddQF---FGPTVEEevaFGLENLGL------PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRldahvhVVNRILV-DSGR 228
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLE------LADRVIVlEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-228 |
1.84e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.52 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHY----GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiQWASQELANKSGVI 85
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLeKPTSGEV--LVDGKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAmfeASLP-LTVMDFIllnqtRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:COG1116 83 GVVFQEP---ALLPwLTVLDNV-----ALGLELRGVPKAERRERARelLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 163 DDPALLVLDEPTTGMDEQGVRYL-ECLIKECVKEGKTVLAVHHDVT-AVRrldahvhVVNRILVDSGR 228
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLqDELLRLWQETGKTVLFVTHDVDeAVF-------LADRVVVLSAR 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-228 |
2.65e-37 |
|
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: 131.30 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY-GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI---DIQWASQELANKSGVIGYV 88
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLlKPTSGEVlvdGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQKA---MFEAslplTVMD---FILLNQtrfplfwrKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQA 160
Cdd:COG1122 81 FQNPddqLFAP----TVEEdvaFGPENL--------GLPREEIRERVEeaLELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 161 LLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLdahvhvVNRILV-DSGR 228
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAEL------ADRVIVlDDGR 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-233 |
1.00e-36 |
|
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: 129.48 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI-----DIQWASQELANKSGvIGY 87
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIrfdgrDITGLPPHERARAG-IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQ-KAMFEaslPLTVMDFILLNQTRfplfwRKRGKEQqnalAQLERV-GM----ASRADRRMGQLSGGEQQRVLFAQAL 161
Cdd:cd03224 80 VPEgRRIFP---ELTVEENLLLGAYA-----RRRAKRK----ARLERVyELfprlKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 162 LDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVN--RIlVDSGRHQDIL 233
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLErgRV-VLEGTAAELL 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-246 |
1.06e-36 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 133.81 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI---DIQWASQELANKSGVIG 86
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVlvaGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKAMFeaSLPLTVMDFILLNQT----RFPlfwrKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQAL 161
Cdd:PRK09536 81 SVPQDTSL--SFEFDVRQVVEMGRTphrsRFD----TWTETDRAAVERaMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 162 LDDPALLVLDEPTTGMD-EQGVRYLEcLIKECVKEGKTVLAVHHDVT-AVRRLDAHVHVVNRILVDSGRHQDILVPEKIE 239
Cdd:PRK09536 155 AQATPVLLLDEPTASLDiNHQVRTLE-LVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
....*..
gi 1055853272 240 RIFNHYT 246
Cdd:PRK09536 234 AAFDART 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-221 |
3.71e-36 |
|
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: 127.69 E-value: 3.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGeCHVVMGPNGGGKTSLLRSILGLT-PFSGQI-----DIQWASQELankSGVIGY 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTpPSSGTIridgqDVLKQPQKL---RRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQKAMFEASLplTVMDFilLNQtrfpLFWRKR---GKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:cd03264 77 LPQEFGVYPNF--TVREF--LDY----IAWLKGipsKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 165 PALLVLDEPTTGMD-EQGVRYLEcLIKEcVKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd03264 149 PSILIVDEPTAGLDpEERIRFRN-LLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNK 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-228 |
4.82e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 127.85 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYG----ENTILTDINHRFSAGECHVVMGPNGGGKTSLLrSILGL--TPFSGQI-----DI-QWASQELA 79
Cdd:COG1136 3 PLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGldRPTSGEVlidgqDIsSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 80 ---NKSgvIGYVPQkamfeaS---LP-LTVMDFILLnqtrfPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGG 150
Cdd:COG1136 82 rlrRRH--IGFVFQ------FfnlLPeLTALENVAL-----PLLLAGVSRKERRERARelLERVGLGDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 151 EQQRVLFAQALLDDPALLVLDEPTTGMDEQ-GVRYLEcLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGR 228
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKtGEEVLE-LLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-212 |
5.25e-36 |
|
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: 128.17 E-value: 5.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWAS----QELANK 81
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLlRPDSGEIlvdgqDITGLSekelYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 sgvIGYVPQK-AMFEAslpLTVMD---FILLNQTRFPlfwrKRGKEQQnALAQLERVGMASRADRRMGQLSGGEQQRVLF 157
Cdd:COG1127 84 ---IGMLFQGgALFDS---LTVFEnvaFPLREHTDLS----EAEIREL-VLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 158 AQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRL 212
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAI 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-242 |
9.70e-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: 127.67 E-value: 9.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQ---WASQELANKSgVIGYVP 89
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILIDgedVRKEPREARR-QIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 90 QKAMFEASlpLTVMDFILLnqtrFPLFWRKRGKEQQNALAQL-ERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALL 168
Cdd:COG4555 81 DERGLYDR--LTVRENIRY----FAELYGLFDEELKKRIEELiELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 169 VLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDSGRHQDIL---VPEKIERIF 242
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKgKVVAQGSLDELReeiGEENLEDAF 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-211 |
1.67e-35 |
|
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: 126.91 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKSGVI 85
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLvEPTSGSVLIdgtdinKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKamFEASLPLTVMDFIL---LNQTRF--PLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQA 160
Cdd:cd03256 81 GMIFQQ--FNLIERLSVLENVLsgrLGRRSTwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 161 LLDDPALLVLDEPTTGMDEQGVRYLECLIKE-CVKEGKTVLAVHHDVTAVRR 211
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLARE 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-242 |
1.99e-35 |
|
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: 126.05 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGEN----TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKSGVIGYV 88
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTSGEVLV--DGEPVTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQKAmfeASLP-LTVMDFILlnqtrFPL--FWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDP 165
Cdd:cd03293 79 FQQD---ALLPwLTVLDNVA-----LGLelQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 166 ALLVLDEPTTGMDEQGVRYL-ECLIKECVKEGKTVLAVHHDVtavrrlDAHVHVVNRILVDSGRhqdilvPEKIERIF 242
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLqEELLDIWRETGKTVLLVTHDI------DEAVFLADRVVVLSAR------PGRIVAEV 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-204 |
3.62e-35 |
|
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: 126.35 E-value: 3.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP--FSGQIDI------QWASQELANKsgvI 85
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptYGNDVRLfgerrgGEDVWELRKR---I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQkAMFEA-SLPLTVMDFILlnqTRFplF-----WRKRGKEQQN-ALAQLERVGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:COG1119 81 GLVSP-ALQLRfPRDETVLDVVL---SGF--FdsiglYREPTDEQRErARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKT--VLAVHH 204
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtlVLVTHH 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-228 |
5.89e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.78 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGEN-TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIqwASQELAN--KSGV----- 84
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQVLV--NGQDLSRlkRREIpylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 -IGYVPQkamfeaslpltvmDFILL-NQT-----RFPLfwRKRGKE----QQNALAQLERVGMASRADRRMGQLSGGEQQ 153
Cdd:COG2884 80 rIGVVFQ-------------DFRLLpDRTvyenvALPL--RVTGKSrkeiRRRVREVLDLVGLSDKAKALPHELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 154 RVLFAQALLDDPALLVLDEPTTGMD-EQGVRYLEcLIKECVKEGKTVLAVHHDVTAVRRLDAHV-HVVNRILVDSGR 228
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDpETSWEIME-LLEEINRRGTTVLIATHDLELVDRMPKRVlELEDGRLVRDEA 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-228 |
1.16e-34 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 123.79 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANKSGVIGY 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLeEPDSGTIiidglKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQK-AMFEAslpLTVMDFILLNQTRFplfwRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:cd03262 81 VFQQfNLFPH---LTVLENITLAPIKV----KGMSKAEaeERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRrldahvHVVNR-ILVDSGR 228
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAR------EVADRvIFMDDGR 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-209 |
3.00e-34 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 124.07 E-value: 3.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQWASQelanksgvIGYVPQKA 92
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIKRNGKLR--------IGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 MFEASLPLTVMDFILLnqtrfplfwrKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDE 172
Cdd:PRK09544 77 YLDTTLPLTVNRFLRL----------RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055853272 173 PTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAV 209
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLV 184
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-228 |
3.31e-34 |
|
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: 123.32 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI-----DI-QWASQELANKsGvIG 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGfLRPTSGSVlfdgeDItGLPPHEIARL-G-IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQK-AMFEAslpLTVMDFILL----NQTRFPLFWRKRGKEQQ---NALAQLERVGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:cd03219 79 RTFQIpRLFPE---LTVLENVMVaaqaRTGSGLLLARARREEREareRAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLdahvhvVNRILV-DSGR 228
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSL------ADRVTVlDQGR 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-205 |
3.84e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.18 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQI-----DIQWASQELANKSGVIGY 87
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTItvdgeDLTDSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQKamFEasL-P-LTVMDFILLNQTRFplfwRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:COG1126 82 VFQQ--FN--LfPhLTVLENVTLAPIKV----KKMSKAEaeERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHD 205
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHE 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-244 |
5.51e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 123.34 E-value: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDI------QWASQELANKSGV 84
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLngrplaDWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IgyvPQKamfeASL--PLTVMDFILLNqtRFPlfWRKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQAL 161
Cdd:PRK13548 81 L---PQH----SSLsfPFTVEEVVAMG--RAP--HGLSRAEDDALVAAaLAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 162 L------DDPALLVLDEPTTGMD---EQGVryLEcLIKECVKE-GKTVLAVHHDVT-AVRRLDaHVHVVNR-ILVDSGRH 229
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDlahQHHV--LR-LARQLAHErGLAVIVVLHDLNlAARYAD-RIVLLHQgRLVADGTP 225
|
250
....*....|....*
gi 1055853272 230 QDILVPEKIERIFNH 244
Cdd:PRK13548 226 AEVLTPETLRRVYGA 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-221 |
7.00e-34 |
|
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: 121.86 E-value: 7.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWAS-QELANKSGVIGYVPQK 91
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLeRPDSGEILIDGRDvTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 -AMFeaslP-LTVMDFIllnqtRFPLFWRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPAL 167
Cdd:cd03259 81 yALF----PhLTVAENI-----AFGLKLRGVPKAEirARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 168 LVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
14-211 |
2.23e-33 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 121.25 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQwaSQELANKSGV------- 84
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLvEPSSGSILLE--GTDITKLRGKklrklrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 -IGYVPQKamFEASLPLTVMDFILLNQTRFPLFWRK-----RGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:TIGR02315 80 rIGMIFQH--YNLIERLTVLENVLHGRLGYKPTWRSllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQ-GVRYLECLIKECVKEGKTVLAVHHDVTAVRR 211
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKtSKQVMDYLKRINKEDGITVIINLHQVDLAKK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-228 |
3.39e-33 |
|
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: 120.30 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY----GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQwaSQELANKSGV---- 84
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlKPTSGSIIFD--GKDLLKLSRRlrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ----IGYVPQKAMfeASLP--LTVMDFI---LLNQTRFplfwRKRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQQR 154
Cdd:cd03257 80 rrkeIQMVFQDPM--SSLNprMTIGEQIaepLRIHGKL----SKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMD--EQgVRYLECLIKECVKEGKTVLAVHHDVTAVRRLdahvhvVNRILV-DSGR 228
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDvsVQ-AQILDLLKKLQEELGLTLLFITHDLGVVAKI------ADRVAVmYAGK 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-221 |
3.86e-33 |
|
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: 119.69 E-value: 3.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQWASQELANKSgVIGYVPQka 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPDSGEVLFDGKPLDIAARN-RIGYLPE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 mfEASL--PLTVMDfillnQTRFplFWRKRGKEQQNALAQ----LERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPA 166
Cdd:cd03269 78 --ERGLypKMKVID-----QLVY--LAQLKGLKKEEARRRidewLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 167 LLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-221 |
7.07e-33 |
|
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: 117.35 E-value: 7.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIdiqwasqelanksgvigyvpqkam 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 94 feaslpltvmdfillnqtrfplFWRKRGKEQQNALAQLERVGMasradrrMGQLSGGEQQRVLFAQALLDDPALLVLDEP 173
Cdd:cd00267 57 ----------------------LIDGKDIAKLPLEELRRRIGY-------VPQLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055853272 174 TTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
11-205 |
8.63e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.51 E-value: 8.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiqwasqELANK--SGV--- 84
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFeTPDSGRI-------LLDGRdvTGLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ---IGYVPQK-AMFeaslP-LTVMDFIllnqtRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLF 157
Cdd:COG3842 76 krnVGMVFQDyALF----PhLTVAENV-----AFGLRMRGVPKAEIRARVAelLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055853272 158 AQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHD 205
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHD 195
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-246 |
1.46e-32 |
|
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: 119.52 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGE----NTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDiqWASQELANKS-----G 83
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLeRPWSGEVT--FDGRPVTRRRrkafrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 VIGYVPQKAMfeASL-P-LTVMDFILLnqtrfPLFWRKRGKEQQNALAQLERVGMASR-ADRRMGQLSGGEQQRVLFAQA 160
Cdd:COG1124 80 RVQMVFQDPY--ASLhPrHTVDRILAE-----PLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 161 LLDDPALLVLDEPTTGMD----EQGVRYLECLIKEcvkEGKTVLAVHHDVTAVRRLdahvhvVNRILV-DSGRHQDILVP 235
Cdd:COG1124 153 LILEPELLLLDEPTSALDvsvqAEILNLLKDLREE---RGLTYLFVSHDLAVVAHL------CDRVAVmQNGRIVEELTV 223
|
250
....*....|..
gi 1055853272 236 EKIERIFNH-YT 246
Cdd:COG1124 224 ADLLAGPKHpYT 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-228 |
1.75e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.02 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 16 LKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQwasqelanKSGVIGYVPQKAMF 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEPDSGEVSIP--------KGLRIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 95 EASLplTVMDFILLNQTRF-------------PLFWRKRGKEQQNALAQLERVG---MASRA--------------DRRM 144
Cdd:COG0488 73 DDDL--TVLDTVLDGDAELraleaeleeleakLAEPDEDLERLAELQEEFEALGgweAEARAeeilsglgfpeedlDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 145 GQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKecvKEGKTVLAVHHDvtavRR-LDAhvhVVNRIL 223
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK---NYPGTVLVVSHD----RYfLDR---VATRIL 220
|
....*.
gi 1055853272 224 -VDSGR 228
Cdd:COG0488 221 eLDRGK 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-204 |
1.03e-31 |
|
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: 116.16 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQIDI-QWASQELANKSGVIGyvpqk 91
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFdGKSYQKNIEALRRIG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMFEAslP-----LTVMDFILLNQTRFplfwRKRGKEQQNALaqlERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPA 166
Cdd:cd03268 76 ALIEA--PgfypnLTARENLRLLARLL----GIRKKRIDEVL---DVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055853272 167 LLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHH 204
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH 184
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-228 |
5.27e-31 |
|
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: 115.08 E-value: 5.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP-FSGQI-----DIQ-WASQELAnKSGvIGY 87
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIrfdgeDITgLPPHRIA-RLG-IGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQ-KAMFEAslpLTVMDFILLnqtrfPLFWRKRGKEQQnalAQLERVG-----MASRADRRMGQLSGGEQQRVLFAQAL 161
Cdd:COG0410 83 VPEgRRIFPS---LTVEENLLL-----GAYARRDRAEVR---ADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 162 LDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLdAHVHVVnrilVDSGR 228
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEI-ADRAYV----LERGR 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-221 |
7.53e-31 |
|
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: 115.14 E-value: 7.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI-----DIQ-WASQELANKsGV 84
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGfYRPTSGRIlfdgrDITgLPPHRIARL-GI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ------IGYVPQkamfeaslpLTVMDFILL------------NQTRFPLFWRKRGKEQQNALAQLERVGMASRADRRMGQ 146
Cdd:COG0411 82 artfqnPRLFPE---------LTVLENVLVaaharlgrgllaALLRLPRARREEREARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 147 LSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDF 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-175 |
8.74e-31 |
|
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: 111.97 E-value: 8.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 29 LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQ---WASQELANKSGVIGYVPQKAMFeasLP-LTVM 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTILLDgqdLTDDERKSLRKEIGYVFQDPQL---FPrLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 104 DFILLNQTRFPLFWRKRGKEQQNALAQLERVGMASR-ADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTT 175
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-200 |
9.69e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.98 E-value: 9.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIdiQWASQEL-ANKSGVIGYVPQ 90
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDSGEV--LWDGEPLdPEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 kamfEASLP--LTVMDFILLnqtrfplFWRKRGKEQQNALAQ----LERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:COG4152 79 ----ERGLYpkMKVGEQLVY-------LARLKGLSKAEAKRRadewLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVL 200
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVI 183
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-233 |
1.34e-30 |
|
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: 119.48 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHY-GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDI-----------QWASQe 77
Cdd:COG4988 334 PPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGfLPPYSGSILIngvdlsdldpaSWRRQ- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 78 lanksgvIGYVPQKAMFeasLPLTVMDFILLNQTRFPlfwrkrGKEQQNAL--AQLERV------GMASRADRRMGQLSG 149
Cdd:COG4988 413 -------IAWVPQNPYL---FAGTIRENLRLGRPDAS------DEELEAALeaAGLDEFvaalpdGLDTPLGEGGRGLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 150 GEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRH 229
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTH 555
|
....
gi 1055853272 230 QDIL 233
Cdd:COG4988 556 EELL 559
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-216 |
1.67e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.96 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRsILGL--TPFSGQIDIQWASQELANKSGV------ 84
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLleMPRSGTLNIAGNHFDFSKTPSDkairel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ---IGYVPQKamFEASLPLTVMDfillNQTRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:PRK11124 81 rrnVGMVFQQ--YNLWPHLTVQQ----NLIEAPCRVLGLSKDQALARAEklLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHV 216
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRV 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-233 |
3.21e-30 |
|
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: 117.70 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHY-----GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DI-QWASQELA 79
Cdd:COG1123 259 PLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLlRPTSGSIlfdgkDLtKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 80 NKSGVIGYVPQKAmfEASL-P-LTVMDFI---LLNQTRFPlfwrkRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQQ 153
Cdd:COG1123 339 ELRRRVQMVFQDP--YSSLnPrMTVGDIIaepLRLHGLLS-----RAERRERVAELLERVGLpPDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 154 RVLFAQALLDDPALLVLDEPTTGMDEQgVRY--LECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVN--RIlVDSGRH 229
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVS-VQAqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYdgRI-VEDGPT 489
|
....
gi 1055853272 230 QDIL 233
Cdd:COG1123 490 EEVF 493
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-216 |
3.69e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.80 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRsILGL--TPFSGQIDI------------QWASQEL 78
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLleTPDSGQLNIaghqfdfsqkpsEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 79 ANKsgvIGYVPQKamFEASLPLTVMDfillNQTRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:COG4161 81 RQK---VGMVFQQ--YNLWPHLTVME----NLIEAPCKVLGLSKEQAREKAMklLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHV 216
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQV 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-243 |
3.82e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.19 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDI------QWASQELANKsgvI 85
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTPQSGTVFLgdkpisMLSSRQLARR---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAMfeasLP--LTVMDFILLNQTRFPLFWRKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:PRK11231 79 ALLPQHHL----TPegITVRELVAYGRSPWLSLWGRLSAEDNARVNQaMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 163 DDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVT-AVRRLDAHVHVVNRILVDSGRHQDILVPEKIERI 241
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTV 234
|
..
gi 1055853272 242 FN 243
Cdd:PRK11231 235 FD 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-206 |
4.56e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 111.58 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQWASQELANKSGVIGYVPQKA 92
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 ---MFEASlpltVMDFILLNQTRFPlfwrkRGKEQQNALaqLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLV 169
Cdd:cd03226 81 dyqLFTDS----VREELLLGLKELD-----AGNEQAETV--LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055853272 170 LDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDV 206
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDY 186
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-228 |
2.86e-29 |
|
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: 110.22 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGEN----TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGqiDIQWASQELAN------ 80
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSG--TVRLAGQDLFAldedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 81 ---KSGVIGYVPQKAMFeasLP-LTVMDFILLnqtrfPLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:COG4181 85 arlRARHVGFVFQSFQL---LPtLTALENVML-----PLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQ-GVRYLEcLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGR 228
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAAtGEQIID-LLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-228 |
7.72e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.41 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSIL-------------GLTPFSGQIDIQWASQElan 80
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINkleeitsgdlivdGLKVNDPKVDERLIRQE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 81 ksgvIGYVPQKamFEASLPLTVMDFILLNqtrfPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:PRK09493 79 ----AGMVFQQ--FYLFPHLTALENVMFG----PLRVRGASKEEAEKQARelLAKVGLAERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQgVRYlECL--IKECVKEGKTVLAVHHDVTAVRRldahvhVVNR-ILVDSGR 228
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPE-LRH-EVLkvMQDLAEEGMTMVIVTHEIGFAEK------VASRlIFIDKGR 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-228 |
9.45e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 110.67 E-value: 9.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDI--QWASQELANKSGVIGYV 88
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThPDAGSISLcgEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQkamFEASLPltvmDFILLNQTRfpLFWRKRGKEQQNALAQ----LERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:PRK13537 86 PQ---FDNLDP----DFTVRENLL--VFGRYFGLSAAAARALvpplLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVvnrilVDSGR 228
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCV-----IEEGR 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-205 |
1.29e-28 |
|
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: 108.36 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYG--ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI-----DIQwASQELANKSgvI 85
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAyingySIR-TDRKAARQS--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQK-AMFEAslpLTVMDFILLnqtrFPLFWRKRGKE-QQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:cd03263 78 GYCPQFdALFDE---LTVREHLRF----YARLKGLPKSEiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHD 205
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHS 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-212 |
2.76e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.31 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI---DIQWASQELANKSGvIGYV 88
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKItvlGVPVPARARLARAR-IGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQKAMFEasLPLTVMDFILLnqtrFPLFWRKRGKEQQNALAQL-ERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPAL 167
Cdd:PRK13536 120 PQFDNLD--LEFTVRENLLV----FGRYFGMSTREIEAVIPSLlEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055853272 168 LVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRL 212
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERL 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-213 |
3.02e-28 |
|
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: 106.67 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDiqWASQELANKSGvigyVPQKA 92
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrPDSGEVR--WNGTPLAEQRD----EPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 MFEAS-LP-----LTVMDfillNQTrfplFWRK-RGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDP 165
Cdd:TIGR01189 75 ILYLGhLPglkpeLSALE----NLH----FWAAiHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 166 ALLVLDEPTTGMDEQGVRYLECLIKE-CVKEGKTVLAVHHDV--TAVRRLD 213
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLglVEARELR 197
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-224 |
3.13e-28 |
|
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: 105.76 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT--ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELAnksGV 84
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlRPTSGRVRLdgadisQWDPNELG---DH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQKAMFeasLPLTVMDFIllnqtrfplfwrkrgkeqqnalaqlervgmasradrrmgqLSGGEQQRVLFAQALLDD 164
Cdd:cd03246 78 VGYLPQDDEL---FSGSIAENI----------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDahvhvvnRILV 224
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASAD-------RILV 167
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-233 |
3.66e-28 |
|
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: 112.55 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHY--GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDI------QWASQELANk 81
Cdd:COG4987 331 GPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRfLDPQSGSITLggvdlrDLDEDDLRR- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 sgVIGYVPQKA-MFEAslplTVMDFILLnqtrfplfwrkrGKEQ--QNALAQ-LERVGMASRADR-------RMG----Q 146
Cdd:COG4987 410 --RIAVVPQRPhLFDT----TLRENLRL------------ARPDatDEELWAaLERVGLGDWLAAlpdgldtWLGeggrR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 147 LSGGEQQRVLFAQALLDDPALLVLDEPTTGMD---EQGVryLECLIKECvkEGKTVLAVHHDVTAVRRLDAHVHVVNRIL 223
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDaatEQAL--LADLLEAL--AGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
250
....*....|
gi 1055853272 224 VDSGRHQDIL 233
Cdd:COG4987 548 VEQGTHEELL 557
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-233 |
6.31e-28 |
|
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: 112.23 E-value: 6.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 10 LGPSIELKNLNLHYGENT--ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DI-QWASQELAN 80
Cdd:COG2274 470 LKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLyEPTSGRIlidgiDLrQIDPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 81 KsgvIGYVPQKA-MFEAslplTVMDFILLNQTRFPLfwrkrgKEQQNAL--AQLERV--GMASRADRRMG----QLSGGE 151
Cdd:COG2274 550 Q---IGVVLQDVfLFSG----TIRENITLGDPDATD------EEIIEAArlAGLHDFieALPMGYDTVVGeggsNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 152 QQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQD 231
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRR-LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEE 695
|
..
gi 1055853272 232 IL 233
Cdd:COG2274 696 LL 697
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-242 |
1.16e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 106.99 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 17 KNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKsgvIGYVP 89
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLmTPAHGHVWLdgehiqHYASKEVARR---IGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 90 QKAMFEASLplTVMDfiLLNQTRFP---LFWRKRgKEQQNALAQLER-VGMASRADRRMGQLSGGEQQRVLFAQALLDDP 165
Cdd:PRK10253 88 QNATTPGDI--TVQE--LVARGRYPhqpLFTRWR-KEDEEAVTKAMQaTGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 166 ALLVLDEPTTGMD-EQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAH-VHVVNRILVDSGRHQDILVPEKIERIF 242
Cdd:PRK10253 163 AIMLLDEPTTWLDiSHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHlIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-205 |
1.89e-27 |
|
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: 105.00 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 16 LKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLrSILGL--TPFSGQIDIQWASQELANKS-------GVIG 86
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLL-NIIGLleKFDSGQVYLNGQETPPLNSKkaskfrrEKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQkamfeaslpltvmDFILL-NQT-----RFPL-FWRKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:TIGR03608 80 YLFQ-------------NFALIeNETveenlDLGLkYKKLSKKEKREKKKEaLEKVGLNLKLKQKIYELSGGEQQRVALA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHD 205
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHD 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-228 |
1.97e-27 |
|
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: 103.62 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT--ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKsgv 84
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGEILIdgvdlrDLDLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQKA-MFEAslplTVMDFILlnqtrfplfwrkrgkeqqnalaqlervgmasradrrmgqlSGGEQQRVLFAQALLD 163
Cdd:cd03228 78 IAYVPQDPfLFSG----TIRENIL----------------------------------------SGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 164 DPALLVLDEPTTGMDEQgvryLECLIKECVKE---GKTVLAVHHDVTAVRRLDahvhvvnRILV-DSGR 228
Cdd:cd03228 114 DPPILILDEATSALDPE----TEALILEALRAlakGKTVIVIAHRLSTIRDAD-------RIIVlDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-220 |
3.68e-27 |
|
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: 103.42 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANKSGVIGY 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLeEPDSGSIlidgeDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQkamfeaslpltvmDFILlnqtrFPLfwrkrgkeqqnaLAQLERVGMAsradrrmgqLSGGEQQRVLFAQALLDDPAL 167
Cdd:cd03229 81 VFQ-------------DFAL-----FPH------------LTVLENIALG---------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 168 LVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVN 220
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-205 |
6.25e-27 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 103.64 E-value: 6.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTI-LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKSG-------- 83
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRV--NGQDVSDLRGraipylrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 VIGYVPQKamFEASLPLTVMD---FILLNQTRFPLFWRKRGKeqqnalAQLERVGMASRADRRMGQLSGGEQQRVLFAQA 160
Cdd:cd03292 79 KIGVVFQD--FRLLPDRNVYEnvaFALEVTGVPPREIRKRVP------AALELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055853272 161 LLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHD 205
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-228 |
1.21e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.00 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI---DIQWASQELANKSGViGYV 88
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLeTPDSGRIvlnGRDLFTNLPPRERRV-GFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQK-AMFeaslP-LTVMDFIllnqtRFPLFWRKRGKEQQNALA--QLERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:COG1118 81 FQHyALF----PhMTVAENI-----AFGLRVRPPSKAEIRARVeeLLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 165 PALLVLDEPTTGMDEQgVRY-LECLIKECVKE-GKTVLAVHHDvtavrRLDAhVHVVNRILV-DSGR 228
Cdd:COG1118 152 PEVLLLDEPFGALDAK-VRKeLRRWLRRLHDElGGTTVFVTHD-----QEEA-LELADRVVVmNQGR 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-212 |
1.29e-26 |
|
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: 103.03 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL------TPFSGQI--------DIQWASQELA 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgAPDEGEVlldgkdiyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 80 NKsgvIGYVPQKA-MFeaslPLTVMDFIllnqtRFPLfwRKRG---KEQQNALAQ--LERVGMASRADRRMG--QLSGGE 151
Cdd:cd03260 81 RR---VGMVFQKPnPF----PGSIYDNV-----AYGL--RLHGiklKEELDERVEeaLRKAALWDEVKDRLHalGLSGGQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 152 QQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDVTAVRRL 212
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAE-LKKEYTIVIVTHNMQQAARV 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-224 |
1.39e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIqwasqelaNKSGVIGYVPQK- 91
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGeLEPDSGTVKL--------GETVKIGYFDQHq 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMFEASlpLTVMDFIllnqtrfplfWR-KRGKEQQNALAQLERVG-MASRADRRMGQLSGGEQQRVLFAQALLDDPALLV 169
Cdd:COG0488 388 EELDPD--KTVLDEL----------RDgAPGGTEQEVRGYLGRFLfSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 170 LDEPTTGMDEQGVRYLECLIKECvkEGkTVLAVHHDVTAVRRldahvhVVNRILV 224
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDR------VATRILE 501
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
14-243 |
3.99e-26 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 102.23 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLnlhyGENTILTDINHRFSAGE-CHVVmGPNGGGKTSLLRSILGLTPFSGQIDI------QWASQELANKSGvig 86
Cdd:COG4138 1 LQLNDV----AVAGRLGPISAQVNAGElIHLI-GPNGAGKSTLLARMAGLLPGQGEILLngrplsDWSAAELARHRA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKAMfeASLPLTVMDFILLNQTRFPlfwrkRGKEQQNALAQL-ERVGMASRADRRMGQLSGGEQQRVLFAQALL--- 162
Cdd:COG4138 73 YLSQQQS--PPFAMPVFQYLALHQPAGA-----SSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 163 ----DDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVT-AVRrldaHVHVV----NRILVDSGRHQDIL 233
Cdd:COG4138 146 ptinPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNhTLR----HADRVwllkQGKLVASGETAEVM 221
|
250
....*....|
gi 1055853272 234 VPEKIERIFN 243
Cdd:COG4138 222 TPENLSEVFG 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-243 |
4.17e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 103.04 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 26 NTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQIDIQWASQELANKSGVIGYVPQKAMFEASLPLTVMD 104
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 105 FILLNQ-TRFPLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVR 183
Cdd:PRK15056 100 VVMMGRyGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 184 YLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDILVPEKIERIFN 243
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFS 239
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
14-211 |
1.34e-25 |
|
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: 100.02 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIqwASQELANKSGvigyvPQK 91
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGaLTPSRGQVRI--AGEDVNRLRG-----RQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMFEASLPLTVMDF-ILLNQTRF-----PLFWRKRGKE--QQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:TIGR02673 75 PLLRRRIGVVFQDFrLLPDRTVYenvalPLEVRGKKEReiQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRR 211
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDR 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-238 |
2.50e-25 |
|
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: 100.00 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQwaSQEL----ANKSGViGYV 88
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLD--GKDItnlpPHKRPV-NTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQK-AMFeaslP-LTVMDFILlnqtrFPLFWRKRGKEQQNA--LAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:cd03300 78 FQNyALF----PhLTVFENIA-----FGLRLKKLPKAEIKErvAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDvtavrRLDAHVhVVNRILV-DSGRHQDILVPEKI 238
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHD-----QEEALT-MSDRIAVmNKGKIQQIGTPEEI 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-228 |
5.85e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 5.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSI-LGLTPFSGQI---DIQW-ASQELANKSGVIGYV 88
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPEAGTIrvgDITIdTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQKAMFE-ASLPLTVMDFILLNQTRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQALLDDP 165
Cdd:PRK11264 84 RQHVGFVfQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 166 ALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRrldahvHVVNR-ILVDSGR 228
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFAR------DVADRaIFMDQGR 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-204 |
1.12e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.64 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQWASQELANKSGVIGYV-PQK 91
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLpPAAGTIKLDGGDIDDPDVAEACHYLgHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMFEAslpLTVMDFIllnqtrfpLFWRK-RGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVL 170
Cdd:PRK13539 83 AMKPA---LTVAENL--------EFWAAfLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1055853272 171 DEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHH 204
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-213 |
1.12e-24 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 97.56 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGqiDIQWASQELANKSGVIG----YV 88
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAG--RVLLNGGPLDFQRDSIArgllYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQKAMFEASLPltvmdfILLNQTrfplFWRKRGKEQQnALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALL 168
Cdd:cd03231 79 GHAPGIKTTLS------VLENLR----FWHADHSDEQ-VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055853272 169 VLDEPTTGMDEQGV-RYLECLIKECVKEGKTVLAVHHDV----TAVRRLD 213
Cdd:cd03231 148 ILDEPTTALDKAGVaRFAEAMAGHCARGGMVVLTTHQDLglseAGARELD 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-243 |
1.19e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.90 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTIltDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGqiDIQWASQELANKSgvIGYVPQKA 92
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSG--RILWNGQDLTALP--PAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 MF-EASL--PLTVMDFILL----NqtrfplfwRKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:COG3840 76 LFqENNLfpHLTVAQNIGLglrpG--------LKLTAEQRAQVEQaLERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 165 PALLVLDEPTTGMDeQGVRYlEC--LIKE-CVKEGKTVLAVHHDVTAVRRLDAHVhvvnrILVDSGRhqdILVPEKIERI 241
Cdd:COG3840 148 RPILLLDEPFSALD-PALRQ-EMldLVDElCRERGLTVLMVTHDPEDAARIADRV-----LLVADGR---IAADGPTAAL 217
|
..
gi 1055853272 242 FN 243
Cdd:COG3840 218 LD 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-228 |
1.25e-24 |
|
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: 97.66 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHY--GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DI-QWASQELankSG 83
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVlldgtDIrQLDPADL---RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 VIGYVPQKAM-FEASL--------PLtVMDFILLNQTRFPLFwrkrgkeqqNALAQLERVGMASRADRRMGQLSGGEQQR 154
Cdd:cd03245 79 NIGYVPQDVTlFYGTLrdnitlgaPL-ADDERILRAAELAGV---------TDFVNKHPNGLDLQIGERGRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDvTAVRRLdahvhvVNRILV-DSGR 228
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQ-LLGDKTLIIITHR-PSLLDL------VDRIIVmDSGR 215
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
10-205 |
2.20e-24 |
|
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: 99.73 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 10 LGPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANksg 83
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLeRQTAGTIyqggrDITRLPPQKRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 vIGYVPQK-AMFeaslP-LTVMDFIllnqtRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:TIGR03265 78 -YGIVFQSyALF----PnLTVADNI-----AYGLKNRGMGRAEVAERVAelLDLVGLPGSERKYPGQLSGGQQQRVALAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQgVR-YLECLIKECVKE-GKTVLAVHHD 205
Cdd:TIGR03265 148 ALATSPGLLLLDEPLSALDAR-VReHLRTEIRQLQRRlGVTTIMVTHD 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-224 |
3.07e-24 |
|
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: 94.44 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIqwasqelaNKSGVIGYVPQka 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIVTW--------GSTVKIGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 mfeaslpltvmdfillnqtrfplfwrkrgkeqqnalaqlervgmasradrrmgqLSGGEQQRVLFAQALLDDPALLVLDE 172
Cdd:cd03221 71 ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 173 PTTGMDEQGVRYLECLIKEcvKEGkTVLAVHHDVTAVRRldahvhVVNRILV 224
Cdd:cd03221 97 PTNHLDLESIEALEEALKE--YPG-TVILVSHDRYFLDQ------VATKIIE 139
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-173 |
3.19e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.38 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQwasQELANKSGV----IGY 87
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLeDPTSGEILIG---GRDVTDLPPkdrnIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQK-AMFeaslP-LTVMDFILlnqtrFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:COG3839 80 VFQSyALY----PhMTVYENIA-----FPLKLRKVPKAEIDRRVReaAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170
....*....|
gi 1055853272 164 DPALLVLDEP 173
Cdd:COG3839 151 EPKVFLLDEP 160
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-228 |
3.23e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.44 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiqwasqeLAnksgviGYVP 89
Cdd:PRK11247 10 GTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGEL--------LA------GTAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 90 QKAMFEaslpltvmDFILLNQTRFPLFWRK---------RGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQA 160
Cdd:PRK11247 76 LAEARE--------DTRLMFQDARLLPWKKvidnvglglKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 161 LLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVrrldahVHVVNR-ILVDSGR 228
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEA------VAMADRvLLIEEGK 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-224 |
3.45e-24 |
|
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: 100.98 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 24 GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DI-QWASQELANksgVIGYVPQK-AMFE 95
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwPPTAGSVrldgaDLsQWDREELGR---HIGYLPQDvELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 96 AslplTVMDfillNQTRFPLfwrkrgkeqqnalAQLERVGMASRA--------------DRRMGQ----LSGGEQQRVLF 157
Cdd:COG4618 420 G----TIAE----NIARFGD-------------ADPEKVVAAAKLagvhemilrlpdgyDTRIGEggarLSGGQRQRIGL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 158 AQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRrldahvhVVNRILV 224
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-------AVDKLLV 538
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-218 |
3.92e-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: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHY-GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI---DIQWASQELANKSGVIG 86
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIavnGVPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKA-MFEAslplTVMDFILLNQ---TRFPLfwrkRGKEQQNALAQLERV---GMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:TIGR02857 400 WVPQHPfLFAG----TIAENIRLARpdaSDAEI----REALERAGLDEFVAAlpqGLDTPIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQgvryLECLIKE---CVKEGKTVLAVHHDVTAVRRLDAHVHV 218
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAE----TEAEVLEalrALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-241 |
5.07e-24 |
|
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: 96.64 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTiLTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI-----DIQWASQELANksgvIGY 87
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfIKPDSGKIllngkDITNLPPEKRD----ISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQ-KAMFeaslP-LTVMDFIllnqtRFPLFWRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:cd03299 76 VPQnYALF----PhMTVYKNI-----AYGLKKRKVDKKEieRKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDSGRHQDILVPEKIERI 241
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNgKLIQVGKPEEVFKKPKNEFV 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-216 |
5.15e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFS----AGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQW---------ASQE 77
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSfsigEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGqpmsklssaAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 78 LANKSgvIGYVPQkamFEASLPltvmDFILLNQTRFPLFW--RKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRV 155
Cdd:PRK11629 84 LRNQK--LGFIYQ---FHHLLP----DFTALENVAMPLLIgkKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEC-VKEGKTVLAVHHDVTAVRRLDAHV 216
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-221 |
6.38e-24 |
|
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: 95.90 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQW--ASQELANKSGVIGYVPQ 90
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGhdVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 KAMFEASLplTVMDFILLnQTRfpLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVL 170
Cdd:cd03265 81 DLSVDDEL--TGWENLYI-HAR--LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 171 DEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDH 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-213 |
6.57e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 95.26 E-value: 6.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIdiQWASQELANksgvigyvpQKA 92
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLArPDAGEV--LWQGEPIRR---------QRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 MFEASL-----------PLTVmdfilLNQTRFplFWRKRGKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQA 160
Cdd:PRK13538 71 EYHQDLlylghqpgiktELTA-----LENLRF--YQRLHGPGDDEALWEaLAQVGLAGFEDVPVRQLSAGQQRRVALARL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 161 LLDDPALLVLDEPTTGMDEQGVRYLECLIKE-CVKEGKTVLAVHHDVT----AVRRLD 213
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPvasdKVRKLR 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-233 |
9.70e-24 |
|
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: 95.73 E-value: 9.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGEN----TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKS 82
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVdgtdltLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 GVIGYVPQKAMFEASLplTVMDFILLnqtrfPL-FWRKRGKEQ-QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQA 160
Cdd:cd03258 82 RRIGMIFQHFNLLSSR--TVFENVAL-----PLeIAGVPKAEIeERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 161 LLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVV-NRILVDSGRHQDIL 233
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMeKGEVVEEGTVEEVF 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
12-228 |
1.79e-23 |
|
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: 97.48 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELkNLNLHYGENTIltDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQ---WASQElankSGV--- 84
Cdd:COG4148 1 MMLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLErPDSGRIRLGgevLQDSA----RGIflp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 -----IGYVPQkamfEASL-P-LTVMDFILLNQtrfplfWRKRGKEQQNALAQL-ERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:COG4148 74 phrrrIGYVFQ----EARLfPhLSVRGNLLYGR------KRAPRAERRISFDEVvELLGIGHLLDRRPATLSGGERQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQgvR------YLECLIKEcvkEGKTVLAVHHDVTAVRRLDAHVhvvnrILVDSGR 228
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLA--RkaeilpYLERLRDE---LDIPILYVSHSLDEVARLADHV-----VLLEQGR 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-205 |
2.14e-23 |
|
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: 98.59 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 6 TSSVLGPSIELKNLNLHY-GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI---DIQWASQELAN 80
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVtldGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 81 KSGVIGYVPQKA-MFEAslplTVMDFILLNqtrfplfwRKRGKEQQnALAQLERVGMASRADRR----------MGQ-LS 148
Cdd:TIGR02868 407 VRRRVSVCAQDAhLFDT----TVRENLRLA--------RPDATDEE-LWAALERVGLADWLRALpdgldtvlgeGGArLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 149 GGEQQRVLFAQALLDDPALLVLDEPTTGMD-EQGVRYLECLIKecVKEGKTVLAVHHD 205
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDaETADELLEDLLA--ALSGRTVVLITHH 529
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-206 |
2.30e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 95.31 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGEN----TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIqwASQELANKSGVIG 86
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAPSSGEITL--DGVPVTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKamfEASLP-LTVMDfillnQTRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:COG4525 80 VVFQK---DALLPwLNVLD-----NVAFGLRLRGVPKAERRARAEelLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055853272 164 DPALLVLDEPTTGMD----EQgvrYLECLIKECVKEGKTVLAVHHDV 206
Cdd:COG4525 152 DPRFLLMDEPFGALDaltrEQ---MQELLLDVWQRTGKGVFLITHSV 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-206 |
3.21e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQiDIQWASQELANKSGVIGYVPQKam 93
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHG-SITLDGKPVEGPGAERGVVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 94 fEASLP-LTVMDfillnQTRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVL 170
Cdd:PRK11248 79 -EGLLPwRNVQD-----NVAFGLQLAGVEKMQRLEIAHqmLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055853272 171 DEPTTGMD----EQgvrYLECLIKECVKEGKTVLAVHHDV 206
Cdd:PRK11248 153 DEPFGALDaftrEQ---MQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
39-221 |
6.39e-23 |
|
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: 93.20 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 39 GECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQW--ASQELANKSGVIGYVPQK-AMFEAslpLTVMDFILLnqtrfp 114
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDGfdVVKEPAEARRRLGFVSDStGLYDR---LTARENLEY------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 115 lFWRKRGKEQQNALAQLE----RVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIK 190
Cdd:cd03266 102 -FAGLYGLKGDELTARLEeladRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170 180 190
....*....|....*....|....*....|.
gi 1055853272 191 ECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd03266 181 QLRALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-205 |
8.75e-23 |
|
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: 92.70 E-value: 8.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwasqelanKSGVIGYVPQK- 91
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRIYI---------GGRDVTDLPPKd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 ---AMFEASLPL----TVMDFIllnqtRFPLFWRKRGKEQQNalaqlERVGMASRA-------DRRMGQLSGGEQQRVLF 157
Cdd:cd03301 72 rdiAMVFQNYALyphmTVYDNI-----AFGLKLRKVPKDEID-----ERVREVAELlqiehllDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055853272 158 AQALLDDPALLVLDEPTTGMDEQgVRY-LECLIKECVKE-GKTVLAVHHD 205
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAK-LRVqMRAELKRLQQRlGTTTIYVTHD 190
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
24-206 |
8.84e-23 |
|
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: 92.10 E-value: 8.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 24 GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQ-----WASQELANKSGVIGYV---PQKAMF 94
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQSGAVLIDgepldYSRKGLLERRQRVGLVfqdPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 95 EASLPLTVmDFILLNQTRFPLFWRKRGKEQqnalaqLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPT 174
Cdd:TIGR01166 83 AADVDQDV-AFGPLNLGLSEAEVERRVREA------LTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1055853272 175 TGMDEQGVRYLECLIKECVKEGKTVLAVHHDV 206
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDV 187
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-173 |
1.40e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.16 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTP-FSGQIDIQWASQEL----ANKSGvIG 86
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPaFSASGEVLLNGRRLtalpAEQRR-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKAMFeasLP-LTVMD---FILLNQTrfplfwrKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:COG4136 80 ILFQDDLL---FPhLSVGEnlaFALPPTI-------GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170
....*....|.
gi 1055853272 163 DDPALLVLDEP 173
Cdd:COG4136 150 AEPRALLLDEP 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-213 |
1.95e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANKSGvI 85
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVyQPDSGEIlldgePVRFRSPRDAQAAG-I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQkamfEASL-P-LTVMDFILLNQ--TRFPLFwrKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQAL 161
Cdd:COG1129 82 AIIHQ----ELNLvPnLSVAENIFLGRepRRGGLI--DWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 162 LDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHdvtavrRLD 213
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH------RLD 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-204 |
1.98e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 91.95 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 28 ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP----FSGQIDI--QWASQELANKSgvIGYVPQkamFEASLP-L 100
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggtTSGQILFngQPRKPDQFQKC--VAYVRQ---DDILLPgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 101 TVMDFIL-LNQTRFPLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDE 179
Cdd:cd03234 97 TVRETLTyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180
....*....|....*....|....*
gi 1055853272 180 QGVRYLECLIKECVKEGKTVLAVHH 204
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIH 201
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
11-204 |
2.51e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNL-HYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQIDIQwASQELAnksgvigYV 88
Cdd:COG4178 360 DGALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgSGRIARP-AGARVL-------FL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQKA-MFEASL------PLTVMDFillnqtrfplfwrkrgkEQQNALAQLERVGMASRADR-----RMGQ-LSGGEQQRV 155
Cdd:COG4178 432 PQRPyLPLGTLreallyPATAEAF-----------------SDAELREALEAVGLGHLAERldeeaDWDQvLSLGEQQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGkTVLAVHH 204
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGH 542
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-240 |
3.18e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQIDI--QWASQELANKSGViGYVP 89
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQtSGHIRFhgTDVSRLHARDRKV-GFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 90 QK-AMFEAslpLTVMDFILLNQTRFPLFWRKRGKE-QQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPAL 167
Cdd:PRK10851 81 QHyALFRH---MTVFDNIAFGLTVLPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 168 LVLDEPTTGMDEQGVRYLECLIKECVKEGK-TVLAVHHDvtavrrLDAHVHVVNRILVDS-GRHQDILVPEKIER 240
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHD------QEEAMEVADRVVVMSqGNIEQAGTPDQVWR 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-224 |
6.30e-22 |
|
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: 92.42 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY----GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQID--IQWASQELANKSG---- 83
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSgeILFDGEDLLKLSEkelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 -----VIGYVPQKAMfeASL-P-LTV----MDFILLNQtrfplfwRKRGKE-QQNALAQLERVGMaSRADRRMG----QL 147
Cdd:COG0444 82 kirgrEIQMIFQDPM--TSLnPvMTVgdqiAEPLRIHG-------GLSKAEaRERAIELLERVGL-PDPERRLDryphEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 148 SGGEQQRVLFAQALLDDPALLVLDEPTTGMD---EQGVryLEcLIKECVKE-GKTVLAVHHDVTAVRrldahvHVVNRIL 223
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDvtiQAQI--LN-LLKDLQRElGLAILFITHDLGVVA------EIADRVA 222
|
.
gi 1055853272 224 V 224
Cdd:COG0444 223 V 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-178 |
6.36e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 94.57 E-value: 6.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIdiQWAsqELANksgvIGYVPQKA 92
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGeLEPDSGTV--KWS--ENAN----IGYYAQDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 MFEASLPLTVMDFIllNQtrfplfWRKRGKEQQNALAQLERvgMASRAD---RRMGQLSGGEQQRVLFAQALLDDPALLV 169
Cdd:PRK15064 392 AYDFENDLTLFDWM--SQ------WRQEGDDEQAVRGTLGR--LLFSQDdikKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
....*....
gi 1055853272 170 LDEPTTGMD 178
Cdd:PRK15064 462 MDEPTNHMD 470
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-233 |
7.60e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.46 E-value: 7.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 8 SVLGPSIELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DI-QWASQELA 79
Cdd:COG1132 334 PPVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPTSGRIlidgvDIrDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 80 NKsgvIGYVPQKA-MFEAslplTVMDFILLnqtrfplfwrkrGKEQ------QNAL--AQLERV------GMASRADRRM 144
Cdd:COG1132 414 RQ---IGVVPQDTfLFSG----TIRENIRY------------GRPDatdeevEEAAkaAQAHEFiealpdGYDTVVGERG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 145 GQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD---EQGV-RYLECLIKecvkeGKTVLAVHHDVTAVRRLDaHVHVVN 220
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDtetEALIqEALERLMK-----GRTTIVIAHRLSTIRNAD-RILVLD 548
|
250
....*....|....*
gi 1055853272 221 --RIlVDSGRHQDIL 233
Cdd:COG1132 549 dgRI-VEQGTHEELL 562
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-228 |
1.10e-21 |
|
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: 92.48 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 31 DINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQ---WASQE----LANKSGVIGYVPQkamfEASL-P-L 100
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVLNgrtLFDSRkgifLPPEKRRIGYVFQ----EARLfPhL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 101 TVMDFILLNqtrfplFWRKRGKEQQNALAQLERV-GMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDE 179
Cdd:TIGR02142 91 SVRGNLRYG------MKRARPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 180 QGVR----YLECLIKECvkeGKTVLAVHHDVTAVRRLDAHVhvvnrILVDSGR 228
Cdd:TIGR02142 165 PRKYeilpYLERLHAEF---GIPILYVSHSLQEVLRLADRV-----VVLEDGR 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-219 |
1.99e-21 |
|
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: 89.28 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 43 VVMGPNGGGKTSLLRSILGL-TPFSGQIDIQ---WASQE----LANKSGVIGYVPQKAmfeASLP-LTVMDFILlnqtrF 113
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLeKPDGGTIVLNgtvLFDSRkkinLPPQQRKIGLVFQQY---ALFPhLNVRENLA-----F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 114 PLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECV 193
Cdd:cd03297 99 GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180
....*....|....*....|....*..
gi 1055853272 194 KE-GKTVLAVHHDVTAVRRLDAHVHVV 219
Cdd:cd03297 179 KNlNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-221 |
4.07e-21 |
|
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: 88.94 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQW--ASQELANKSGViGYVP 89
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTILFGGedATDVPVQERNV-GFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 90 QK-AMFEAslpLTVMDFIllnqtRFPLFWRKRGKEQQNALAQ------LERVGMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:cd03296 81 QHyALFRH---MTVFDNV-----AFGLRVKPRSERPPEAEIRakvhelLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 163 DDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-206 |
6.23e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 88.37 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQwaSQELANKS-------GvI 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLD--GQDITKLPmhkrarlG-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQkamfEASL--PLTVMDFIL--LNQTRFPlfwRKRGKEQQNALaqLERVGMASRADRRMGQLSGGEQQRVLFAQAL 161
Cdd:cd03218 78 GYLPQ----EASIfrKLTVEENILavLEIRGLS---KKEREEKLEEL--LEEFHITHLRKSKASSLSGGERRRVEIARAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055853272 162 LDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDV 206
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNV 193
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-224 |
9.73e-21 |
|
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: 85.94 E-value: 9.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiQWASQELANKSgvigyvPQKA 92
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLyKPDSGEI--LVDGKEVSFAS------PRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 mfeaslpltvmdfillnqtrfplfwRKRGkeqqnalaqlerVGMASradrrmgQLSGGEQQRVLFAQALLDDPALLVLDE 172
Cdd:cd03216 73 -------------------------RRAG------------IAMVY-------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 173 PTTGMDEQGVRYLECLIKECVKEGKTVLAVHHdvtavrRLDAHVHVVNRILV 224
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISH------RLDEVFEIADRVTV 154
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-228 |
1.36e-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: 86.78 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINhrFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQ---WASQELANKsgvigyvP 89
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT--FAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINgvdVTAAPPADR-------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 90 QKAMF-EASL--PLTVMDFILLNqtRFPLFwRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPA 166
Cdd:cd03298 72 VSMLFqENNLfaHLTVEQNVGLG--LSPGL-KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 167 LLVLDEPTTGMDEqGVRY--LECLIKECVKEGKTVLAVHHDVTAVRRLDAHVhvvnrILVDSGR 228
Cdd:cd03298 149 VLLLDEPFAALDP-ALRAemLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRV-----VFLDNGR 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-178 |
2.25e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.85 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 2 KKVTTSSVLGPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI--DIQWASQEL 78
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRImlDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 79 ANKSGVIGYVPQKAMFeaslP-LTVMDFIllnqtRFPLFWRKRGKEQ-----QNALA--QLErvgmaSRADRRMGQLSGG 150
Cdd:PRK09452 83 AENRHVNTVFQSYALF----PhMTVFENV-----AFGLRMQKTPAAEitprvMEALRmvQLE-----EFAQRKPHQLSGG 148
|
170 180
....*....|....*....|....*...
gi 1055853272 151 EQQRVLFAQALLDDPALLVLDEPTTGMD 178
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-234 |
2.53e-20 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 86.51 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI---DIQWASQELANKSGVIGYV 88
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQIlidGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQKAMFeasLPLTVMDFILLNQTRFPlfwrkrgKEQQNALAQLERV---------GMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:cd03254 83 LQDTFL---FSGTIMENIRLGRPNAT-------DEEVIEAAKEAGAhdfimklpnGYDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQgvryLECLIKECVK---EGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDILV 234
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTE----TEKLIQEALEklmKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-204 |
2.84e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 84.90 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILT-DINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQIDIQWASQELanksgvigYVPQK 91
Cdd:cd03223 1 IELENLSLATPDGRVLLkDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRIGMPEGEDLL--------FLPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMFEASLpltvmdfiLLNQTRFPlfWRKRgkeqqnalaqlervgmasradrrmgqLSGGEQQRVLFAQALLDDPALLVLD 171
Cdd:cd03223 73 PYLPLGT--------LREQLIYP--WDDV--------------------------LSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|...
gi 1055853272 172 EPTTGMDEQGVRYLECLIKEcvkEGKTVLAVHH 204
Cdd:cd03223 117 EATSALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
14-221 |
2.94e-20 |
|
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: 86.33 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNL----NLHY-GENTI--LTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWASQ--ELANKS- 82
Cdd:COG4778 5 LEVENLsktfTLHLqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVRHDGGwvDLAQASp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 --------GVIGYVPQkamFEASLPLT-----VMDfillnqtrfPLfwRKRGKEQQNALAQ----LERVGMasraDRRMG 145
Cdd:COG4778 85 reilalrrRTIGYVSQ---FLRVIPRVsaldvVAE---------PL--LERGVDREEARARarelLARLNL----PERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 146 QL-----SGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVN 220
Cdd:COG4778 147 DLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
.
gi 1055853272 221 R 221
Cdd:COG4778 227 P 227
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
14-211 |
4.12e-20 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 86.19 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSI------------------LGLTPFSGQIDIQwas 75
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndlvpgvriegkvlfDGQDIYDKKIDVV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 76 qELANKsgvIGYVPQKAmfeASLPLTVMDFILLNQTRFPLfwrkRGKEQQNALAQ--LERVGM----ASRADRRMGQLSG 149
Cdd:TIGR00972 79 -ELRRR---VGMVFQKP---NPFPMSIYDNIAYGPRLHGI----KDKKELDEIVEesLKKAALwdevKDRLHDSALGLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 150 GEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDVTAVRR 211
Cdd:TIGR00972 148 GQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQE-LKKKYTIVIVTHNMQQAAR 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-204 |
5.18e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 84.91 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 27 TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF---SGQIDIQWASQELANKSGVIGYVPQKAMFEASLplTV- 102
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTL--TVr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 103 --MDFIllnqtrfplfwrkrgkeqqnalAQLErvgmasradrrmgQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDE- 179
Cdd:cd03213 101 etLMFA----------------------AKLR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSs 145
|
170 180
....*....|....*....|....*
gi 1055853272 180 QGVRYLECLIKECvKEGKTVLAVHH 204
Cdd:cd03213 146 SALQVMSLLRRLA-DTGRTIICSIH 169
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-220 |
5.78e-20 |
|
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: 85.82 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKsgvI 85
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEIFIdgedirEQDPVELRRK---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAMFeasLP-LTVMDFILLnqtrFP--LFWrKRGKEQQNALAQLERVGM--ASRADRRMGQLSGGEQQRVLFAQA 160
Cdd:cd03295 78 GYVIQQIGL---FPhMTVEENIAL----VPklLKW-PKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 161 LLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVN 220
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMK 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
31-233 |
6.84e-20 |
|
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: 86.16 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 31 DINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI-----DIQWAS----QELANKSgvIGYVPQKamFeASLP- 99
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTSGKVlidgqDIAAMSrkelRELRRKK--ISMVFQS--F-ALLPh 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 100 LTVMDfillnQTRFPLFWRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGM 177
Cdd:cd03294 117 RTVLE-----NVAFGLEVQGVPRAEreERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 178 DEQGVRYLECLIKECVKE-GKTVLAVHHDvtavrrLDAHVHVVNRI-------LVDSGRHQDIL 233
Cdd:cd03294 192 DPLIRREMQDELLRLQAElQKTIVFITHD------LDEALRLGDRIaimkdgrLVQVGTPEEIL 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-200 |
9.43e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 9.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiQWASQEL-------ANKSG 83
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLyQPDSGEI--LIDGKPVrirsprdAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 vIGYVPQKAM-FEaslPLTVMDFILLNQTRFPLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:COG3845 82 -IGMVHQHFMlVP---NLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055853272 163 DDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVL 200
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-243 |
9.65e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.52 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLrSILG--LTPFSGQIDI------QWASQELANKsgvI 85
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISrlLPPDSGEVLVdgldvaTTPSRELAKR---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAMFeaSLPLTVMDfiLLNQTRFPlfwRKRG---KEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQAL 161
Cdd:COG4604 78 AILRQENHI--NSRLTVRE--LVAFGRFP---YSKGrltAEDREIIDEaIAYLDLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 162 LDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVT-AVRRLDahvHVV---NRILVDSGRHQDILVPE 236
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINfASCYAD---HIVamkDGRVVAQGTPEEIITPE 227
|
....*..
gi 1055853272 237 KIERIFN 243
Cdd:COG4604 228 VLSDIYD 234
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
17-242 |
1.25e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 85.02 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 17 KNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQwaSQELANK-------SGvIGYV 88
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVrPDAGKILID--GQDITHLpmherarLG-IGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQkamfEASL--PLTVMDFIL-LNQTRFPLFwRKRGKEQQNALaqLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDP 165
Cdd:TIGR04406 82 PQ----EASIfrKLTVEENIMaVLEIRKDLD-RAEREERLEAL--LEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 166 ALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVN--RILvDSGRHQDILVPEKIERIF 242
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISdgKVL-AEGTPAEIVANEKVRRVY 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
14-206 |
2.06e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-----TPFSgQID-----IQWA---SQELAN 80
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGS-HIEllgrtVQREgrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 81 KSGVIGYVPQKamFEASLPLTVMDFILLNQTRFPLFWRK-----RGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRV 155
Cdd:PRK09984 84 SRANTGYIFQQ--FNLVNRLSVLENVLIGALGSTPFWRTcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQGVR-YLECLIKECVKEGKTVLAVHHDV 206
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARiVMDTLRDINQNDGITVVVTLHQV 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-178 |
4.26e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGEchVV--MGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELAN-------K 81
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGE--IVglLGPNGAGKTTTFYMIVGLvKPDSGRIFL--DGEDITHlpmhkraR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 SGvIGYVPQkamfEASL--PLTVMDFIL--LNQTRFPlfwRKRGKEQQNALaqLERVGMASRADRRMGQLSGGEQQRVLF 157
Cdd:COG1137 78 LG-IGYLPQ----EASIfrKLTVEDNILavLELRKLS---KKEREERLEEL--LEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180
....*....|....*....|.
gi 1055853272 158 AQALLDDPALLVLDEPTTGMD 178
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVD 168
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-209 |
4.95e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.13 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI-----DIQWASQELANKSGVIG 86
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRIlfdgkPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YV---PQKAMFEASLPLTVmDFILLNqTRFPlfwrkRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:PRK13636 86 MVfqdPDNQLFSASVYQDV-SFGAVN-LKLP-----EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAV 209
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIV 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-228 |
5.29e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.74 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY----GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKSGV---- 84
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLeRPTSGSVLV--DGVDLTALSERelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ----IGYVPQkamfeaslpltvmDFILLNQtR-------FPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGE 151
Cdd:COG1135 80 arrkIGMIFQ-------------HFNLLSS-RtvaenvaLPLEIAGVPKAEIRKRVAelLELVGLSDKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 152 QQRVLFAQALLDDPALLVLDEPTTGMDEQGVRY-LEcLIKECVKE-GKTVLAVHHDVTAVRRldahvhVVNRILV-DSGR 228
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSiLD-LLKDINRElGLTIVLITHEMDVVRR------ICDRVAVlENGR 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-213 |
7.28e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 81.21 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGEN--TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI-----DIQWASQELANKsgvI 85
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEItldgvPVSDLEKALSSL---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKA-MFEASLpltvmdfillnqtrfplfwrkrgkeqqnalaqLERVGMasradrrmgQLSGGEQQRVLFAQALLDD 164
Cdd:cd03247 78 SVLNQRPyLFDTTL--------------------------------RNNLGR---------RFSGGERQRLALARILLQD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDVTAVRRLD 213
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHMD 164
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-242 |
8.51e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 22 HYGENTILTDINHRFSAGE-CHVVmGPNGGGKTSLLRSILGLTPFSGQIDI------QWASQELANKSgviGYVPQKAMF 94
Cdd:PRK03695 5 DVAVSTRLGPLSAEVRAGEiLHLV-GPNGAGKSTLLARMAGLLPGSGSIQFagqpleAWSAAELARHR---AYLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 95 EASLPltVMDFILLNQTRFPlfwrkRGKEQQNALAQL-ERVGMASRADRRMGQLSGGEQQRVLFAQALLD-DPA------ 166
Cdd:PRK03695 81 PFAMP--VFQYLTLHQPDKT-----RTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDinpagq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 167 LLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRldaHVHVV----NRILVDSGRHQDILVPEKIERIF 242
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLR---HADRVwllkQGKLLASGRRDEVLTPENLAQVF 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
14-207 |
1.67e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.62 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwaSQELANKSGV----IGYV 88
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFI---DGEDVTHRSIqqrdICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 PQK-AMF-EASLPLTVmdfillnqtRFPLFWRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:PRK11432 84 FQSyALFpHMSLGENV---------GYGLKMLGVPKEErkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVT 207
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQS 198
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-227 |
1.83e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.65 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG---LTPFSGQI-----DI-QWASQELANK---- 81
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTSGSIlldgeDIlELSPDERARAgifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 --------SGVigyvpqkamfeaslplTVMDFI--LLNQTRFP----LFWRKRGKEQqnalaqLERVGM-ASRADRRMGQ 146
Cdd:COG0396 82 afqypveiPGV----------------SVSNFLrtALNARRGEelsaREFLKLLKEK------MKELGLdEDFLDRYVNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 147 -LSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAV-HHDvtavRRLDA----HVHVVN 220
Cdd:COG0396 140 gFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIItHYQ----RILDYikpdFVHVLV 215
|
....*....
gi 1055853272 221 --RIlVDSG 227
Cdd:COG0396 216 dgRI-VKSG 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-218 |
2.02e-18 |
|
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: 84.35 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFS----AGECHVVMGPNGGGKTSLLRSILGLTPFSGQI---DIQWASQELANKS-- 82
Cdd:COG4172 5 PLLSVEDLSVAFGQGGGTVEAVKGVSfdiaAGETLALVGESGSGKSVTALSILRLLPDPAAHpsgSILFDGQDLLGLSer 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 -------GVIGYVPQKAMfeASL-PL-TVMDfillnQTRFPLFWRK--RGKE-QQNALAQLERVGMAsRADRRMG----Q 146
Cdd:COG4172 85 elrrirgNRIAMIFQEPM--TSLnPLhTIGK-----QIAEVLRLHRglSGAAaRARALELLERVGIP-DPERRLDayphQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 147 LSGGEQQRVLFAQALLDDPALLVLDEPTTGMDeqgV----RYLEcLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHV 218
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALD---VtvqaQILD-LLKDLQRElGMALLLITHDLGVVRRFADRVAV 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-206 |
2.57e-18 |
|
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: 84.29 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 39 GECHVVMGPNGGGKTSLLRSILGLTPF-SGQIDIQWASQeLANKSGV---IGYVPQkamFEAslpltvMDFILLNQTRFP 114
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVtSGDATVAGKSI-LTNISDVhqnMGYCPQ---FDA------IDDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 115 LFWRKRG--KEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIK 190
Cdd:TIGR01257 2035 LYARLRGvpAEEIEKVANwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170
....*....|....*.
gi 1055853272 191 ECVKEGKTVLAVHHDV 206
Cdd:TIGR01257 2115 SIIREGRAVVLTSHSM 2130
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-209 |
2.90e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.66 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWASQELANKS--------G 83
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPIKYDKKSllevrktvG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 VIGYVPQKAMFEASLPLTVMdFILLNQTRFPLFWRKRGKEQqnalaqLERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:PRK13639 82 IVFQNPDDQLFAPTVEEDVA-FGPLNLGLSKEEVEKRVKEA------LKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAV 209
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLV 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-219 |
5.34e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.96 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWASQELANKSGVigYVPQKA 92
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDHGEILFDGENIPAMSRSRL--YTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 93 M---FEASLPLTvmDFILLNQTRFPLFWRKRGKE---QQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPA 166
Cdd:PRK11831 86 MsmlFQSGALFT--DMNVFDNVAYPLREHTQLPApllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 167 LLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVV 219
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIV 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-238 |
8.32e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 3 KVTTSSVLGPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQwaSQELANk 81
Cdd:PRK11607 9 QAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLD--GVDLSH- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 sgVIGYV-PQKAMFE--ASLP-LTVMDFIL--LNQTRFPlfwrkRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRV 155
Cdd:PRK11607 86 --VPPYQrPINMMFQsyALFPhMTVEQNIAfgLKQDKLP-----KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQgVR---YLECL-IKECVkeGKTVLAVHHDVTAVRRLDAHVHVVNRilvdsGRHQD 231
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKK-LRdrmQLEVVdILERV--GVTCVMVTHDQEEAMTMAGRIAIMNR-----GKFVQ 230
|
....*..
gi 1055853272 232 ILVPEKI 238
Cdd:PRK11607 231 IGEPEEI 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-220 |
1.01e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.03 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQ-WASQELANKsGV 84
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFyKPTGGTIllrgqHIEgLPGHQIARM-GV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQKAMFEAslpLTVMDFILLNQTRF------------PLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQ 152
Cdd:PRK11300 83 VRTFQHVRLFRE---MTVIENLLVAQHQQlktglfsgllktPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 153 QRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVN 220
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
17-242 |
1.03e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.55 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 17 KNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQI-----DIQWASQELANKSGvIGYVPQ 90
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdAGNIiiddeDISLLPLHARARRG-IGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 kamfEASL--PLTVMDFIL-LNQTRFPLFWRKRgKEQQNALaqLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPAL 167
Cdd:PRK10895 86 ----EASIfrRLSVYDNLMaVLQIRDDLSAEQR-EDRANEL--MEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 168 LVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDSGRHQDILVPEKIERIF 242
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEILQDEHVKRVY 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-205 |
1.40e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANKSgvI 85
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLlfegeDISTLKPEIYRQQ--V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAMFEASlplTVMDFILlnqtrFPLFWRKRGKEQQNALAQLERVGMA-SRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:PRK10247 84 SYCAQTPTLFGD---TVYDNLI-----FPWQIRNQQPDPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHD 205
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-214 |
1.48e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 29 LTDINHRFSAGECHVVMGPNGGGKTSLLRsILG--LTPFSGQIDIQWASQELAN-----KSGVI------GYVPQkamfe 95
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLK-ILSgnYQPDAGSILIDGQEMRFASttaalAAGVAiiyqelHLVPE----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 96 aslpLTVMDFILLNQtrFP--LFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEP 173
Cdd:PRK11288 94 ----MTVAENLYLGQ--LPhkGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055853272 174 TTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRL-DA 214
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALcDA 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-233 |
2.19e-17 |
|
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: 78.74 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY---GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DI-QWASQELANKsg 83
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPTSGEIlldgvDIrDLNLRWLRSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 vIGYVPQK-AMFEAslplTVMDFILLnqtrfplfwrkrGKEQqnalAQLERVGMASRA--------------DRRMG--- 145
Cdd:cd03249 79 -IGLVSQEpVLFDG----TIAENIRY------------GKPD----ATDEEVEEAAKKanihdfimslpdgyDTLVGerg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 146 -QLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGvrylECLIKEC---VKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:cd03249 138 sQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES----EKLVQEAldrAMKGRTTIVIAHRLSTIRNADLIAVLQNG 213
|
250
....*....|..
gi 1055853272 222 ILVDSGRHQDIL 233
Cdd:cd03249 214 QVVEQGTHDELM 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
49-200 |
2.43e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 49 GGGKTSLLRSILGLTPF-SGQI-----DIQWASQELANKSGvIGYVP----QKAMFeasLPLTVMD-FILLNQTRF-PLF 116
Cdd:COG1129 288 GAGRTELARALFGADPAdSGEIrldgkPVRIRSPRDAIRAG-IAYVPedrkGEGLV---LDLSIREnITLASLDRLsRGG 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 117 WRKRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEqGVRYlE--CLIKECV 193
Cdd:COG1129 364 LLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV-GAKA-EiyRLIRELA 441
|
....*..
gi 1055853272 194 KEGKTVL 200
Cdd:COG1129 442 AEGKAVI 448
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-216 |
2.75e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 18 NLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWASQELA-NKSGVIGYVPQKA--M 93
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLeKPSEGSIVVNGQTINLVrDKDGQLKVADKNQlrL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 94 FEASLPLTVMDF-------ILLNQTRFPL--FWRKRGKEQQNALAQLERVGMASRA-DRRMGQLSGGEQQRVLFAQALLD 163
Cdd:PRK10619 90 LRTRLTMVFQHFnlwshmtVLENVMEAPIqvLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHV 216
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHV 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-209 |
2.95e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.10 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTI-----LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWAS----------Q 76
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALlKPSSGTITIAGYHitpetgnknlK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 77 ELANKSGVIGYVPQKAMFEAslplTVMDFILLNQTRFPlFWRKRGKEQqnALAQLERVGMA-SRADRRMGQLSGGEQQRV 155
Cdd:PRK13641 82 KLRKKVSLVFQFPEAQLFEN----TVLKDVEFGPKNFG-FSEDEAKEK--ALKWLKKVGLSeDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAV 209
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDV 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-237 |
3.77e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.98 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP------FSGqiDIQWASQELANKSGV 84
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrYSG--DVLLGGRSIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQKAMF---EASLPLTVMDFILLNQTRFPLFWRK--RGKEQqnalAQLERVGMASRADRRMG----QLSGGEQQRV 155
Cdd:PRK14271 97 LEFRRRVGMLfqrPNPFPMSIMDNVLAGVRAHKLVPRKefRGVAQ----ARLTEVGLWDAVKDRLSdspfRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDILVP 235
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
..
gi 1055853272 236 EK 237
Cdd:PRK14271 253 PK 254
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-233 |
4.23e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHY--GENTILTDINHRFSAGEcHV-VMGPNGGGKTSLLRSilgLT----PFSGQIDI------QWASQEL 78
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGE-KVaLLGRTGCGKSTLLQL---LTrawdPQQGEILLngqpiaDYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 79 ANKSGVigyVPQKA-MFEASLpltvMDFILLNQtrfplfwrkrGKEQQNALAQ-LERVGMASRADRRMG----------Q 146
Cdd:PRK11160 413 RQAISV---VSQRVhLFSATL----RDNLLLAA----------PNASDEALIEvLQQVGLEKLLEDDKGlnawlgeggrQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 147 LSGGEQQRVLFAQALLDDPALLVLDEPTTGMD---EQgvRYLECLIKECvkEGKTVLAVHHDVTAVRRLDaHVHVV-NRI 222
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaetER--QILELLAEHA--QNKTVLMITHRLTGLEQFD-RICVMdNGQ 550
|
250
....*....|.
gi 1055853272 223 LVDSGRHQDIL 233
Cdd:PRK11160 551 IIEQGTHQELL 561
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-205 |
4.40e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.06 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG---------LTPF-----SGQI--DIQWAs 75
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndLTLFgrrrgSGETiwDIKKH- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 76 qelanksgvIGYVPQKAMFEASLPLTVMDFILLNqtrfplFWRKRG-----KEQQNALAQ--LERVGMASR-ADRRMGQL 147
Cdd:PRK10938 338 ---------IGYVSSSLHLDYRVSTSVRNVILSG------FFDSIGiyqavSDRQQKLAQqwLDILGIDKRtADAPFHSL 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 148 SGGEQQRVLFAQALLDDPALLVLDEPTTGMD---EQGV-RYLECLIkecvKEGKTVL--AVHHD 205
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDplnRQLVrRFVDVLI----SEGETQLlfVSHHA 462
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-239 |
5.82e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLR------------SILGLTPFSGQIDIQWASQELANK 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrlielypeaRVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 SGVIGYVPQK----AMFE-ASLPLTVMDFIllnQTRFPLFWRKRGKEQQnalAQL-ERVgmASRADRRMGQLSGGEQQRV 155
Cdd:PRK14247 84 VQMVFQIPNPipnlSIFEnVALGLKLNRLV---KSKKELQERVRWALEK---AQLwDEV--KDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDILVP 235
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
....
gi 1055853272 236 EKIE 239
Cdd:PRK14247 236 PRHE 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-224 |
8.57e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.85 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT---ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQwaSQELA-----NKSGV 84
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLlEAESGQIIID--GDLLTeenvwDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQKA--MFEASlplTVMD---FILLNQTrFPLfwrkrgKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:PRK13650 83 IGMVFQNPdnQFVGA---TVEDdvaFGLENKG-IPH------EEMKERVNEaLELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDvtavrrLDaHVHVVNRILV 224
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHD------LD-EVALSDRVLV 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-233 |
8.89e-17 |
|
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: 77.14 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYG--ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWASQELANKSGV---IGY 87
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLrrqVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQKAMFeasLPLTVMDFILLNQTRFPLfwrkrgkEQQNALAQLE---------RVGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:cd03252 81 VLQENVL---FNRSIRDNIALADPGMSM-------ERVIEAAKLAgahdfiselPEGYDTIVGEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKeGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDIL 233
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-224 |
9.67e-17 |
|
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: 75.55 E-value: 9.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGentiLTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANKSGvI 85
Cdd:cd03215 3 PVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLrPPASGEItldgkPVTRRSPRDAIRAG-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVP----QKAMFeasLPLTVMDFILLNQtrfplfwrkrgkeqqnalaqlervgmasradrrmgQLSGGEQQRVLFAQAL 161
Cdd:cd03215 78 AYVPedrkREGLV---LDLSVAENIALSS-----------------------------------LLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 162 LDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDvtavrrLDAHVHVVNRILV 224
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE------LDELLGLCDRILV 176
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-238 |
1.13e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.36 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHYGENT--ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKS----- 82
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLlLPEAGTITV--GGMVLSEETvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 GVIGYVPQKA--MFEASlplTVMD---FILLNQTrFPlfwrkRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLF 157
Cdd:PRK13635 81 RQVGMVFQNPdnQFVGA---TVQDdvaFGLENIG-VP-----REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 158 AQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGK-TVLAVHHDVTAVRRLDahvhvvnRILV-DSGRHQDILVP 235
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQAD-------RVIVmNKGEILEEGTP 224
|
...
gi 1055853272 236 EKI 238
Cdd:PRK13635 225 EEI 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-238 |
1.36e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 77.09 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT--ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKSGV------ 84
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLlLPTSGKVTV--DGLDTLDEENLweirkk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQKA--MFEASlplTVMD---FILLNQtRFPlfwrkRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:TIGR04520 79 VGMVFQNPdnQFVGA---TVEDdvaFGLENL-GVP-----REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDahvhvvnRILV-DSGRHQDILVPEK 237
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVLAD-------RVIVmNKGKIVAEGTPRE 222
|
.
gi 1055853272 238 I 238
Cdd:TIGR04520 223 I 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-212 |
1.39e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWAS-----QELANKSGvI 85
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNINynkldHKLAAQLG-I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQkamfEASL--PLTVMDFILLNqtRFP---------LFWRKRgkeQQNALAQLERVGMASRADRRMGQLSGGEQQR 154
Cdd:PRK09700 83 GIIYQ----ELSVidELTVLENLYIG--RHLtkkvcgvniIDWREM---RVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRL 212
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRI 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-204 |
1.52e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 24 GENTILTDINHRFSAGECHVVMGPNGGGKTSLL-----RSILGLTpFSGQIDIQWASQELANKSGVIGYVPQKAMFEASL 98
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVK-GSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 99 plTVMDFiLLNQTRFPLFWRKRGKEQQNALAQ-LERVGMASRADRRMGQ------LSGGEQQRVLFAQALLDDPALLVLD 171
Cdd:TIGR00955 115 --TVREH-LMFQAHLRMPRRVTKKEKRERVDEvLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|...
gi 1055853272 172 EPTTGMDEQGVRYLECLIKECVKEGKTVLAVHH 204
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-204 |
1.69e-16 |
|
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: 75.64 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 16 LKNLNLHY--GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL---TPFSGQI-----DIQWASQELANKSGvI 85
Cdd:cd03217 1 LEIKDLHVsvGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkyEVTEGEIlfkgeDITDLPPEERARLG-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAmfeASLP-LTVMDFIllnqtRFplfwrkrgkeqqnalaqlerVGMAsradrrmgqLSGGEQQRVLFAQALLDD 164
Cdd:cd03217 80 FLAFQYP---PEIPgVKNADFL-----RY--------------------VNEG---------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHH 204
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-241 |
1.70e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.95 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYG--ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKS 82
Cdd:PRK13632 6 VMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlKPQSGEIKIdgitisKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 GVIGYVPQKAMFEAslplTVMD---FILLNQtRFPlfwRKRGKEQQNALAQleRVGMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:PRK13632 86 GIIFQNPDNQFIGA----TVEDdiaFGLENK-KVP---PKKMKDIIDDLAK--KVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEG-KTVLAVHHDVTAVRRLDaHVHVVNR-ILVDSGRHQDILVPEK 237
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILAD-KVIVFSEgKLIAQGKPKEILNNKE 234
|
....
gi 1055853272 238 IERI 241
Cdd:PRK13632 235 ILEK 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-233 |
2.21e-16 |
|
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: 76.11 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYG-ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANKSgvIG 86
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFyDVSSGSIlidgqDIREVTLDSLRRA--IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQkamfeaslpltvmDFILLNQT-----RFplfwrkrGK-----EQQNALAQLERV---------GMASRADRRMGQL 147
Cdd:cd03253 79 VVPQ-------------DTVLFNDTigyniRY-------GRpdatdEEVIEAAKAAQIhdkimrfpdGYDTIVGERGLKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 148 SGGEQQRVLFAQALLDDPALLVLDEPTTGMD---EQGVryLECLIKECvkEGKTVLAVHHDVTAVRRLDAHVHVVNRILV 224
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDthtEREI--QAALRDVS--KGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
....*....
gi 1055853272 225 DSGRHQDIL 233
Cdd:cd03253 215 ERGTHEELL 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-233 |
2.95e-16 |
|
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: 75.73 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYG--ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQwaSQELANKSGVI 85
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFyDVDSGRIlidghDVR--DYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKA-MFEAslplTVMDFILLNQTRFPLFWRKRGKEQQNALAQLERV--GMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:cd03251 79 GLVSQDVfLFND----TVAENIAYGRPGATREEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 163 DDPALLVLDEPTTGMDEQGVRYLECLIKECVKeGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDIL 233
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-232 |
5.30e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.56 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILT--DINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI---DIQWASQELANKSGVI 85
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIeKVKSGEIfynNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKA--MFEASLPLTVMDFILLNQTrFPLfwrkrgKEQQNALAQ-LERVGMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGLENHA-VPY------DEMHRRVSEaLKQVDMLERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 163 DDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGK--TVLAVHHDVTAVRRLDaHVHVVNRILV-DSGRHQDI 232
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRK-VKSEHniTIISITHDLSEAMEAD-HVIVMNKGTVyKEGTPTEI 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
12-216 |
5.52e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 75.22 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKSGVIG-YVP 89
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLeTPDSGEIRV--GGEEIRLKPDRDGeLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 90 ----QKAMFEASLPLTVMDF-------ILLNQTRFPLFWRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:COG4598 85 adrrQLQRIRTRLGMVFQSFnlwshmtVLENVIEAPVHVLGRPKAEaiERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQGVRylECL--IKECVKEGKTVLAVHHDVTAVRRLDAHV 216
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVG--EVLkvMRDLAEEGRTMLVVTHEMGFARDVSSHV 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-242 |
6.37e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.25 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 26 NTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSG-------------------QIDiqwaSQELANKSGVIg 86
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtgdvtlngeplaAID----APRLARLRAVL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 yvPQKAmfEASLPLTVMDFILLNqtRFPLFWRKRGKEQQN---ALAQLERVGMASRADRRMGQLSGGEQQRVLFAQAL-- 161
Cdd:PRK13547 89 --PQAA--QPAFAFSAREIVLLG--RYPHARRAGALTHRDgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 162 -------LDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKT-VLAVHHDVT-AVRRLDAHVHVVNRILVDSGRHQDI 232
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADV 242
|
250
....*....|
gi 1055853272 233 LVPEKIERIF 242
Cdd:PRK13547 243 LTPAHIARCY 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-213 |
7.24e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRS------------------ILGLTPFSGQIDiqwa 74
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearvegevrLFGRNIYSPDVD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 75 SQELANKSGVIGYVPQkamfeaSLP-LTVMDFILLNqTRFPLFWRKRGKEQQNALAQLERVGMASRADRRM----GQLSG 149
Cdd:PRK14267 80 PIEVRREVGMVFQYPN------PFPhLTIYDNVAIG-VKLNGLVKSKKELDERVEWALKKAALWDEVKDRLndypSNLSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 150 GEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLD 213
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSD 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-220 |
9.54e-16 |
|
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: 74.84 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 19 LNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiQWASQELANKSGvigyvPQKAMFEAS 97
Cdd:TIGR02769 17 LFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLeKPAQGTV--SFRGQDLYQLDR-----KQRRAFRRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 98 LPLTVMDFILLNQTRFPLFW-----------RKRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQQRVLFAQALLDDP 165
Cdd:TIGR02769 90 VQLVFQDSPSAVNPRMTVRQiigeplrhltsLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 166 ALLVLDEPTTGMDeqgvRYLECLIKECVKE-----GKTVLAVHHDVTAVRRLDAHVHVVN 220
Cdd:TIGR02769 170 KLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMD 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-205 |
9.65e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 75.61 E-value: 9.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 44 VMGPNGGGKTSLLRSILGL-TPFSGQI--DIQWASQELANKSGvIGYVPQK-AMFEAslpLTVMDFIllnqtRFPLFWRK 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFeQPDSGSImlDGEDVTNVPPHLRH-INMVFQSyALFPH---MTVEENV-----AFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 120 RGKEQQNA--LAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-G 196
Cdd:TIGR01187 72 VPRAEIKPrvLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlG 151
|
....*....
gi 1055853272 197 KTVLAVHHD 205
Cdd:TIGR01187 152 ITFVFVTHD 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-228 |
1.00e-15 |
|
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: 76.51 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 28 ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiqWASQELAnksgvIGYVPQKAMFEASLplTVMDFI 106
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFNGEA---RPQPGIK-----VGYLPQEPQLDPTK--TVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 107 LLN-------QTRF----------PLFWRKRGKEQ---QNALA---------QLERVGMASRA---DRRMGQLSGGEQQR 154
Cdd:TIGR03719 90 EEGvaeikdaLDRFneisakyaepDADFDKLAAEQaelQEIIDaadawdldsQLEIAMDALRCppwDADVTKLSGGERRR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcvKEGkTVLAVHHDvtavrR--LDahvHVVNRIL-VDSGR 228
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPG-TVVAVTHD-----RyfLD---NVAGWILeLDRGR 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-227 |
1.25e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLL-------RSILGLTPFSGQIDIQWASQELANKSgv 84
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLgtlcgdpRATSGRIVFDGKDITDWQTAKIMREA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQ-KAMFEAslpLTVMDFILLNQtrfplFWRKRGKEQQnalaQLERV-----GMASRADRRMGQLSGGEQQRVLFA 158
Cdd:PRK11614 82 VAIVPEgRRVFSR---MTVEENLAMGG-----FFAERDQFQE----RIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR---ILVDSG 227
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENghvVLEDTG 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-220 |
1.30e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGEN----TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQiDIQWASQELAN--------- 80
Cdd:PRK10584 7 VEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSG-EVSLVGQPLHQmdeearakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 81 KSGVIGYVPQKAMFEASLPLtvmdfilLNQTRFPLFWRKRGKEQ--QNALAQLERVGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNA-------LENVELPALLRGESSRQsrNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQ-GVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVN 220
Cdd:PRK10584 159 RAFNGRPDVLFADEPTGNLDRQtGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-173 |
1.99e-15 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 74.36 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTI-LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQwaSQELANKSGV-----IG 86
Cdd:COG1125 2 IEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLiEPTSGRILID--GEDIRDLDPVelrrrIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKAmfeASLP-LTVMDFI-----LLNqtrfplfW-RKRGKEQQNALaqLERVGM--ASRADRRMGQLSGGEQQRVLF 157
Cdd:COG1125 80 YVIQQI---GLFPhMTVAENIatvprLLG-------WdKERIRARVDEL--LELVGLdpEEYRDRYPHELSGGQQQRVGV 147
|
170
....*....|....*.
gi 1055853272 158 AQALLDDPALLVLDEP 173
Cdd:COG1125 148 ARALAADPPILLMDEP 163
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-242 |
2.00e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.67 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 16 LKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRsILGL--TPFSGQIDI------QWASQELANKsgvIGY 87
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRhqPPSEGEILLdaqpleSWSSKAFARK---VAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQKamFEASLPLTVMDFILLNqtRFPlfW-----RKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:PRK10575 90 LPQQ--LPAAEGMTVRELVAIG--RYP--WhgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 163 DDPALLVLDEPTTGMD-EQGVRYLECLIKECVKEGKTVLAVHHDVT-AVRRLDAHVHVVNRILVDSGRHQDILVPEKIER 240
Cdd:PRK10575 164 QDSRCLLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRGETLEQ 243
|
..
gi 1055853272 241 IF 242
Cdd:PRK10575 244 IY 245
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-229 |
2.06e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 22 HYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI-----DI-QWASQELANKSGVIGYVPQKAMF 94
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIErPSAGKIwfsghDItRLKNREVPFLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 95 easlpltVMDFILLNQTRFPLFWRKRGKE--QQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDE 172
Cdd:PRK10908 91 -------LMDRTVYDNVAIPLIIAGASGDdiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 173 PTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRH 229
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-204 |
2.09e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.96 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 28 ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQWASQELANKSGVIGYVpqkamfeASLPLTVMDFI 106
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDGKTATRGDRSRFMAYL-------GHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 107 LLNQTRF--PLFWRKRGKEQQNALAQlerVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRY 184
Cdd:PRK13543 99 TLENLHFlcGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180
....*....|....*....|
gi 1055853272 185 LECLIKECVKEGKTVLAVHH 204
Cdd:PRK13543 176 VNRMISAHLRGGGAALVTTH 195
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-233 |
4.74e-15 |
|
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: 74.39 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 2 KKVTTSSVLGPSIELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWASQELA 79
Cdd:TIGR01193 462 KKRTELNNLNGDIVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFfQARSGEILLNGFSLKDI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 80 NKS---GVIGYVPQKA-MFEASlpltVMDFILLNQtrfplfwrKRGKEQQNALAQLERV-----------GMASRADRRM 144
Cdd:TIGR01193 542 DRHtlrQFINYLPQEPyIFSGS----ILENLLLGA--------KENVSQDEIWAACEIAeikddienmplGYQTELSEEG 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 145 GQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD---EQgvRYLECLIKecVKEgKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDtitEK--KIVNNLLN--LQD-KTIIFVAHRLSVAKQSDKIIVLDHG 684
|
250
....*....|..
gi 1055853272 222 ILVDSGRHQDIL 233
Cdd:TIGR01193 685 KIIEQGSHDELL 696
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-206 |
4.83e-15 |
|
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: 72.44 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 36 FSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWASqelanksgvIGYVPQKamFEASLPLTVMDF---ILLNQT 111
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGvLKPDEGDIEIELDT---------VSYKPQY--IKADYEGTVRDLlssITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 112 RFPlFWRKrgkEQQNALaQLERVgmasrADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD-EQGVRYLECLIK 190
Cdd:cd03237 91 THP-YFKT---EIAKPL-QIEQI-----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDvEQRLMASKVIRR 160
|
170
....*....|....*.
gi 1055853272 191 ECVKEGKTVLAVHHDV 206
Cdd:cd03237 161 FAENNEKTAFVVEHDI 176
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-226 |
5.02e-15 |
|
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: 72.37 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 23 YGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQID----IQWASQE--LANKSGVIGyvpQKAMFE 95
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTSGEVRvaglVPWKRRKkfLRRIGVVFG---QKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 96 ASLPltVMDFILLNQT--RFPLFWRKRGKEQQNALAQLERVgmasrADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEP 173
Cdd:cd03267 108 WDLP--VIDSFYLLAAiyDLPPARFKKRLDELSELLDLEEL-----LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 174 TTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVN--RILVDS 226
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDkgRLLYDG 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
12-228 |
5.57e-15 |
|
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: 71.76 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGEN--TILTDINHRFSAGEcHV-VMGPNGGGKTSLLRSILGLT-PFSGQIDI------QWASQELANK 81
Cdd:cd03244 1 GDIEFKNVSLRYRPNlpPVLKNISFSIKPGE-KVgIVGRTGSGKSSLLLALFRLVeLSSGSILIdgvdisKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 sgvIGYVPQKA-MFEASLpltvmdfillnqtRFPL--FWRKRGKEQQNALaqlERVGMASRADRRMGQL----------- 147
Cdd:cd03244 80 ---ISIIPQDPvLFSGTI-------------RSNLdpFGEYSDEELWQAL---ERVGLKEFVESLPGGLdtvveeggenl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 148 SGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKeGKTVLAVHHdvtavrRLDaHVHVVNRILV-DS 226
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAH------RLD-TIIDSDRILVlDK 212
|
..
gi 1055853272 227 GR 228
Cdd:cd03244 213 GR 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-224 |
5.78e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYG-----ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWASQELANKSGV--- 84
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALlLPDTGTIEWIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ------------------------IGYVPQKA---MFEAslplTVMDFILLNQTRFPLfwrKRGKEQQNALAQLERVGM- 136
Cdd:PRK13651 83 vleklviqktrfkkikkikeirrrVGVVFQFAeyqLFEQ----TIEKDIIFGPVSMGV---SKEEAKKRAAKYIELVGLd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 137 ASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDvtavrrLDAHV 216
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD------LDNVL 229
|
....*...
gi 1055853272 217 HVVNRILV 224
Cdd:PRK13651 230 EWTKRTIF 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-218 |
8.93e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 25 ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSG----QIDIQWASQELANKS-----GV----IGYVPQK 91
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPvvypSGDIRFHGESLLHASeqtlrGVrgnkIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMfeASL-PLTVMDFILlnqtrFPLFWRKRGKEQQNA----LAQLERVGMaSRADRRMG----QLSGGEQQRVLFAQALL 162
Cdd:PRK15134 101 PM--VSLnPLHTLEKQL-----YEVLSLHRGMRREAArgeiLNCLDRVGI-RQAAKRLTdyphQLSGGERQRVMIAMALL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 163 DDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHV 218
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAV 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-206 |
9.97e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.08 E-value: 9.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKSGVI 85
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVmgrevnAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAMFEAslplTVMDFILLNqtrfPLFWRKRGKEQQN-ALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDD 164
Cdd:PRK13647 85 FQDPDDQVFSS----TVWDDVAFG----PVNMGLDKDEVERrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055853272 165 PALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDV 206
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDV 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-221 |
1.26e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY-GENTILTDINhrFSAGECH--VVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWASQELANKSGV---IG 86
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNIN--FIAPRNSriAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEPITKENIREVrkfVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKAMFEASLPlTVMDFILLNQTRFPLFWRKRGKEQQNALAQLervGMASRADRRMGQLSGGEQQRVLFAQALLDDPA 166
Cdd:PRK13652 82 LVFQNPDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHML---GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 167 LLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDK 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-205 |
1.30e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.22 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY--GENTI--LTDINHRFSAGECHVVMGPNGGGKTSLLrSILGL--TPFSGQIDIqwASQELANKSG---- 83
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCldKPTSGTYRV--AGQDVATLDAdala 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 -----VIGYVPQKAMFEASLPLtvmdfilLNQTRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:PRK10535 82 qlrreHFGFIFQRYHLLSHLTA-------AQNVEVPAVYAGLERKQRLLRAQelLQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHD 205
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-224 |
2.03e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTD-INHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQIDI-----------QWASQelan 80
Cdd:PRK11174 349 TIEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKIngielreldpeSWRKH---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 81 ksgvIGYVPQkamfEASLPL-TVMDFILLNQTRFplfwrkrGKEQ-QNALAQ---LERV-----GMASRADRRMGQLSGG 150
Cdd:PRK11174 425 ----LSWVGQ----NPQLPHgTLRDNVLLGNPDA-------SDEQlQQALENawvSEFLpllpqGLDTPIGDQAAGLSVG 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 151 EQQRVLFAQALLDDPALLVLDEPTTGMD---EQGVryLECLIKEcvKEGKTVLAVHHdvtavrRLDAhVHVVNRILV 224
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDahsEQLV--MQALNAA--SRRQTTLMVTH------QLED-LAQWDQIWV 555
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
13-232 |
2.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.93 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENT-----ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKS---- 82
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPTQGSVRV--DDTLITSTSknkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 --------GVIGYVPQKAMFEAslplTVMDFILLNQTRFPLfwrkrGKEQQNALA--QLERVGMA-SRADRRMGQLSGGE 151
Cdd:PRK13649 80 ikqirkkvGLVFQFPESQLFEE----TVLKDVAFGPQNFGV-----SQEEAEALAreKLALVGISeSLFEKNPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 152 QQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDSGRHQ 230
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPK 230
|
..
gi 1055853272 231 DI 232
Cdd:PRK13649 231 DI 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-221 |
2.82e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENT-----ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQ--WASQELANKSGV 84
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLiKSKYGTIQVGdiYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQKamfeaslpltVMDFILLNQT-----RFP---LF---------------WRKRGKEQQNALAQLERVGM-ASRA 140
Cdd:PRK13631 101 TNPYSKK----------IKNFKELRRRvsmvfQFPeyqLFkdtiekdimfgpvalGVKKSEAKKLAKFYLNKMGLdDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 141 DRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVN 220
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
.
gi 1055853272 221 R 221
Cdd:PRK13631 251 K 251
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-228 |
2.83e-14 |
|
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: 69.42 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGE-----NTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIqwasqelankSGVIGY 87
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSV----------PGSIAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQKA-MFEAslplTVMDFIL----LNQTRFplfwrkrgkeqQNAL--AQLER-VGMASRADRRM-GQ----LSGGEQQR 154
Cdd:cd03250 71 VSQEPwIQNG----TIRENILfgkpFDEERY-----------EKVIkaCALEPdLEILPDGDLTEiGEkginLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYlecLIKECV----KEGKTVLAVHHDVTAVRRLDaHVhvvnrILVDSGR 228
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRH---IFENCIlgllLNNKTRILVTHQLQLLPHAD-QI-----VVLDNGR 204
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-204 |
4.04e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.07 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 5 TTSSVLGPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSI---LGLTP---FSGQI-----DIqw 73
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPgarVEGEIlldgeDI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 74 asqelaNKSGV--------IGYVPQKAmfeASLPLTVMDFILlnqtrFPLfwRKRGKEQQNALAQ-----LERVGM---- 136
Cdd:COG1117 81 ------YDPDVdvvelrrrVGMVFQKP---NPFPKSIYDNVA-----YGL--RLHGIKSKSELDEiveesLRKAALwdev 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 137 ASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHH 204
Cdd:COG1117 145 KDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE-LKKDYTIVIVTH 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-221 |
4.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.53 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-----ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI----------QWASQE 77
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGKVTVgdivvsstskQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 78 LANKSGVIGYVPQKAMFEAslplTVMDFILLNQTRFPLfwrKRGKEQQNALAQLERVGMASRA-DRRMGQLSGGEQQRVL 156
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEE----TVLKDVAFGPQNFGI---PKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-244 |
4.26e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.99 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY----GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI-----DI-QWASQELANKS 82
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLErPTSGRVlvdgqDLtALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 GVIGYVPQ-------KAMFE-ASLPLTvmdfillnqtrfpLFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQR 154
Cdd:PRK11153 82 RQIGMIFQhfnllssRTVFDnVALPLE-------------LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVvnrilVDSGRhqdiL 233
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAV-----IDAGR----L 219
|
250
....*....|..
gi 1055853272 234 VPE-KIERIFNH 244
Cdd:PRK11153 220 VEQgTVSEVFSH 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-206 |
4.42e-14 |
|
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: 69.42 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 29 LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQwaSQELANKSgvigyvPQK-AMFE--ASLP-LTVM 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAqPTSGGVILE--GKQITEPG------PDRmVVFQnySLLPwLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 104 DFILLNQTRFplfWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQG 181
Cdd:TIGR01184 73 ENIALAVDRV---LPDLSKSERRAIVEehIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180
....*....|....*....|....*.
gi 1055853272 182 VRYL-ECLIKECVKEGKTVLAVHHDV 206
Cdd:TIGR01184 150 RGNLqEELMQIWEEHRVTVLMVTHDV 175
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-228 |
4.78e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 69.42 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 28 ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKSGVIGYVPQkaMFEASlpl 100
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFyQPQGGQVLLdgkpisQYEHKYLHSKVSLVGQEPV--LFARS--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 101 tVMDFILLNQTRFPLFWRKRGKEQQNA---LAQLERvGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGM 177
Cdd:cd03248 104 -LQDNIAYGLQSCSFECVKEAAQKAHAhsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 178 DEQGVRYLECLIKECvKEGKTVLAVHHDVTAVRRLDahvhvvnRILV-DSGR 228
Cdd:cd03248 182 DAESEQQVQQALYDW-PERRTVLVIAHRLSTVERAD-------QILVlDGGR 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-186 |
4.80e-14 |
|
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: 71.50 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwasqelaNKSGVIGYV---- 88
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTIEI--------GETVKLAYVdqsr 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 ----PQKAMFEA-SLPLTVMDFillnqtrfplfwrkrGKEQQNALAQLERVG-MASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:TIGR03719 395 daldPNKTVWEEiSGGLDIIKL---------------GKREIPSRAYVGRFNfKGSDQQKKVGQLSGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|....
gi 1055853272 163 DDPALLVLDEPTTGMDEQGVRYLE 186
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALE 483
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-233 |
6.71e-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: 71.00 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHY-GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQElankS- 82
Cdd:COG5265 355 GGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFyDVTSGRIlidgqDIRDVTQA----Sl 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 -GVIGYVPQkamfeaslpltvmDFILLNQT-----RFplfwrkrGK------EQQNA--LAQLERV------GMASRADR 142
Cdd:COG5265 431 rAAIGIVPQ-------------DTVLFNDTiayniAY-------GRpdaseeEVEAAarAAQIHDFieslpdGYDTRVGE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 143 RMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD---EQGVryLECLIKecVKEGKTVLAVHHdvtavrRL----DAH 215
Cdd:COG5265 491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDsrtERAI--QAALRE--VARGRTTLVIAH------RLstivDAD 560
|
250 260
....*....|....*....|.
gi 1055853272 216 VHVV---NRIlVDSGRHQDIL 233
Cdd:COG5265 561 EILVleaGRI-VERGTHAELL 580
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-202 |
1.08e-13 |
|
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: 70.22 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSL---LRSILGLTPFSGQIDIQWAsqeLANKSGVIGyVPQ 90
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIIYHVA---LCEKCGYVE-RPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 KA-----MFEASLPLTVMDF----------------ILLNQTrFPLFWRKR---------------GKEQ-QNALAQLER 133
Cdd:TIGR03269 77 KVgepcpVCGGTLEPEEVDFwnlsdklrrrirkriaIMLQRT-FALYGDDTvldnvlealeeigyeGKEAvGRAVDLIEM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 134 VGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAV 202
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVL 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
27-228 |
1.37e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.56 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 27 TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiQWASQELANKSGvigyvPQKAMFEASLPLTVMDF 105
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNV--SWRGEPLAKLNR-----AQRKAFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 106 ILLNQTRFPLFW-----------RKRGKEQQNALAQLERVGMA-SRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEP 173
Cdd:PRK10419 99 ISAVNPRKTVREiireplrhllsLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 174 TTGMD----EQGVRYLECLIKecvKEGKTVLAVHHDVTAVRRLDAHVhvvnrILVDSGR 228
Cdd:PRK10419 179 VSNLDlvlqAGVIRLLKKLQQ---QFGTACLFITHDLRLVERFCQRV-----MVMDNGQ 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-204 |
1.43e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.91 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 25 ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL---TPFSGQI---DIQWASQELANksgvIGYVPQKAMFEASL 98
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqgNNFTGTIlanNRKPTKQILKR----TGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 99 plTVMD-FILLNQTRFPlfwRKRGKEQQNALAQ--LERVGMASRADRRMGQ-----LSGGEQQRVLFAQALLDDPALLVL 170
Cdd:PLN03211 156 --TVREtLVFCSLLRLP---KSLTKQEKILVAEsvISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190
....*....|....*....|....*....|....
gi 1055853272 171 DEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHH 204
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-239 |
1.45e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 16 LKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLR-------------SILGLTPFSGQIDIQWASQELANKS 82
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKvlnrlieiydskiKVDGKVLYFGKDIFQIDAIKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 GVIGYVPQkamfeaSLP-LTVMDFIllnqtRFPLfwRKRGKEQQNALAQ-----LERVGMASRADRRM----GQLSGGEQ 152
Cdd:PRK14246 93 GMVFQQPN------PFPhLSIYDNI-----AYPL--KSHGIKEKREIKKiveecLRKVGLWKEVYDRLnspaSQLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 153 QRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDI 232
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
....*..
gi 1055853272 233 LVPEKIE 239
Cdd:PRK14246 240 FTSPKNE 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-218 |
1.73e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 5 TTSSVLGPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWASQE-----L 78
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIvPPDSGTLEIGGNPCArltpaK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 79 ANKSGvIGYVPQKAMFEASlpLTVMDFILLNQTRFPLFWRKrgkeQQNALAQLervGMASRADRRMGQLSGGEQQRVLFA 158
Cdd:PRK15439 83 AHQLG-IYLVPQEPLLFPN--LSVKENILFGLPKRQASMQK----MKQLLAAL---GCQLDLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 159 QALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHV 218
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISV 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-227 |
1.89e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 39 GECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIqwasqELAnksgvIGYVPQKamFEASLPLTVMDFILLNQTRFPLFW 117
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGvLKPDEGEVDP-----ELK-----ISYKPQY--IKPDYDGTVEDLLRSITDDLGSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 118 RKrgKEQQNALaQLERVgmasrADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD-EQGV-------RYLEcli 189
Cdd:PRK13409 433 YK--SEIIKPL-QLERL-----LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDvEQRLavakairRIAE--- 501
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055853272 190 kecvKEGKTVLAVHHDVTAvrrLDahvHVVNRILVDSG 227
Cdd:PRK13409 502 ----EREATALVVDHDIYM---ID---YISDRLMVFEG 529
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-229 |
2.55e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP---FSGqiDIQWASQELANKS-------G 83
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtYEG--EIIFEGEELQASNirdteraG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 -VIGY-----VPQkamfeaslpLTVMDFILLNQTrfplfWRKRGKEQQNALAQ-----LERVGMASRADRRMGQLSGGEQ 152
Cdd:PRK13549 84 iAIIHqelalVKE---------LSVLENIFLGNE-----ITPGGIMDYDAMYLraqklLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 153 QRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNrilvdSGRH 229
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIR-----DGRH 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-178 |
3.44e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG---LTPFSGqiDIQWASQELANKSgvigyv 88
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKILEG--DILFKGESILDLE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 P----QKAMFEA-SLPLTV-----MDFILL--NQTRfplfwRKRGKEQQNALA-------QLERVGM-ASRADRRMGQ-L 147
Cdd:CHL00131 78 PeeraHLGIFLAfQYPIEIpgvsnADFLRLayNSKR-----KFQGLPELDPLEfleiineKLKLVGMdPSFLSRNVNEgF 152
|
170 180 190
....*....|....*....|....*....|.
gi 1055853272 148 SGGEQQRVLFAQALLDDPALLVLDEPTTGMD 178
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLD 183
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-224 |
4.90e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.38 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENT-----ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI--------DIQWASQEL 78
Cdd:PRK13637 2 SIKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlKPTSGKIiidgvditDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 79 ANKSGVIGYVPQKAMFEAslplTVMDFILLNQTRFPLF---WRKRGKEQQNALAqLERVGMAsraDRRMGQLSGGEQQRV 155
Cdd:PRK13637 82 RKKVGLVFQYPEYQLFEE----TIEKDIAFGPINLGLSeeeIENRVKRAMNIVG-LDYEDYK---DKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGK-TVLAVHHDVTAVRRLdahvhvVNRILV 224
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKL------ADRIIV 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-205 |
7.37e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.65 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYG-----ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIqwASQELANK-----S 82
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDSGSILI--DGKDVTKLpeykrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 GVIGYV---PQKAMFEAslpLTVMDFILLNQTR---FPLFWRKRGKEQQNALAQLERVGM--ASRADRRMGQLSGGEQQR 154
Cdd:COG1101 80 KYIGRVfqdPMMGTAPS---MTIEENLALAYRRgkrRGLRRGLTKKRRELFRELLATLGLglENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGK-TVLAVHHD 205
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHN 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-218 |
8.67e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNlhyGENTIltDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiqWASQELANKSGV------ 84
Cdd:PRK15439 267 PVLTVEDLT---GEGFR--NISLEVRAGEILGLAGVVGAGRTELAETLYGLrPARGGRI---MLNGKEINALSTaqrlar 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 -IGYVP----QKAMF-EASLPLTVMDFILLNQTrfplFWRKRGKEQqnalAQLERVGMA-----SRADRRMGQLSGGEQQ 153
Cdd:PRK15439 339 gLVYLPedrqSSGLYlDAPLAWNVCALTHNRRG----FWIKPAREN----AVLERYRRAlnikfNHAEQAARTLSGGNQQ 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 154 RVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHV 218
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLV 475
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-224 |
8.91e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWASQELANKSGV------ 84
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAGEVHYRMRDGQLRDLYALseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ------IGYVPQKAMfeASLPLTV----------MDfillnqtrfpLFWRKRGKEQQNALAQLERVGM-ASRADRRMGQL 147
Cdd:PRK11701 85 rllrteWGFVHQHPR--DGLRMQVsaggnigerlMA----------VGARHYGDIRATAGDWLERVEIdAARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 148 SGGEQQRVLFAQALLDDPALLVLDEPTTGMDeqgV----RYLEcLIKECVKE-GKTVLAVHHDVtAVRRLDAHvhvvnRI 222
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD---VsvqaRLLD-LLRGLVRElGLAVVIVTHDL-AVARLLAH-----RL 222
|
..
gi 1055853272 223 LV 224
Cdd:PRK11701 223 LV 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-205 |
1.00e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 25 ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL---TPFSGQIDIQWasQELANKSGVIGYVPQKAMFEAslplt 101
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkgTPVAGCVDVPD--NQFGREASLIDAIGRKGDFKD----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 102 vmdfillnqtrfplfwrkrgkeqqnALAQLERVGMASRAD--RRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDE 179
Cdd:COG2401 115 -------------------------AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*...
gi 1055853272 180 QGVRYLE-CLIKECVKEGKT-VLAVHHD 205
Cdd:COG2401 170 QTAKRVArNLQKLARRAGITlVVATHHY 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-228 |
1.33e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 28 ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiqWASQELAnksgvIGYVPQ---------------- 90
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKEFEGEA---RPAPGIK-----VGYLPQepqldpektvrenvee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 -----KAM---FEA-----SLPLTVMDFILLNQTRFplfwrkrgkeqQNALA---------QLERVGMASR---ADRRMG 145
Cdd:PRK11819 94 gvaevKAAldrFNEiyaayAEPDADFDALAAEQGEL-----------QEIIDaadawdldsQLEIAMDALRcppWDAKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 146 QLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcvKEGkTVLAVHHDvtavrR--LDahvHVVNRIL 223
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD--YPG-TVVAVTHD-----RyfLD---NVAGWIL 231
|
....*.
gi 1055853272 224 -VDSGR 228
Cdd:PRK11819 232 eLDRGR 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-229 |
1.38e-12 |
|
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: 67.16 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP---FSGqiDIQWASQELANKS------GV 84
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtWDG--EIYWSGSPLKASNirdterAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQKAMFEASLplTVMDFILL--------NQTRFPLFWRKrgkeQQNALAQLERvgMASRADRRMGQLSGGEQQRVL 156
Cdd:TIGR02633 80 IVIIHQELTLVPEL--SVAENIFLgneitlpgGRMAYNAMYLR----AKNLLRELQL--DADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNrilvdSGRH 229
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIR-----DGQH 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-230 |
1.45e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.05 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY---GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI------QWASQELANKSG 83
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQPTGGQVLLdgvplvQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 VIGYVPQkaMFEASlpltVMDFILLNQTRFPlfwrkrgKEQQNALAQLERV-----GMASRADRRMG----QLSGGEQQR 154
Cdd:TIGR00958 559 LVGQEPV--LFSGS----VRENIAYGLTDTP-------DEEIMAAAKAANAhdfimEFPNGYDTEVGekgsQLSGGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKecvKEGKTVLAVHHDVTAVRRLDaHVHVVNR-ILVDSGRHQ 230
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLSTVERAD-QILVLKKgSVVEMGTHK 698
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-212 |
1.48e-12 |
|
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: 65.25 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY----------------------GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQID 70
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYpPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 71 IQwasqelANKSGVIGYvpqKAMFEASlpLTVMDFILLNQtrfpLFWRKRGKEQQN------ALAQLERVGmasraDRRM 144
Cdd:cd03220 81 VR------GRVSSLLGL---GGGFNPE--LTGRENIYLNG----RLLGLSRKEIDEkideiiEFSELGDFI-----DLPV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 145 GQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRL 212
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRL 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-233 |
1.51e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 37 SAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWasQELANKSgvigYVPQKAMFEAS--------LPLTVMDF-- 105
Cdd:PRK10938 27 NAGDSWAFVGANGSGKSALARALAGeLPLLSGERQSQF--SHITRLS----FEQLQKLVSDEwqrnntdmLSPGEDDTgr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 106 ----ILLNQTRFPlfwrkrgkEQQNALAQLerVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQG 181
Cdd:PRK10938 101 ttaeIIQDEVKDP--------ARCEQLAQQ--FGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 182 VRYLECLIKECVKEGKTVLAVhhdvtaVRRLD------AHVHVV-NRILVDSGRHQDIL 233
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLV------LNRFDeipdfvQFAGVLaDCTLAETGEREEIL 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-233 |
2.08e-12 |
|
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: 66.66 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTI--LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI---DIQWASQELANKSGVIGY 87
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYePDSGQIlldGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQKAMfeaslpltVMDFILLNQTRFplfwrkrGKEQQNALAQLERVGMASRA-----------DRRMGQ----LSGGEQ 152
Cdd:TIGR02203 411 VSQDVV--------LFNDTIANNIAY-------GRTEQADRAEIERALAAAYAqdfvdklplglDTPIGEngvlLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 153 QRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQDI 232
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALER-LMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
.
gi 1055853272 233 L 233
Cdd:TIGR02203 555 L 555
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-178 |
3.12e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGeCHV-VMGPNGGGKTSLLRSILG--------LTPFSGQIDIQWASQELANKsgv 84
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAG-CMVgLIGPDGVGKSSLLSLIAGarkiqqgrVEVLGGDMADARHRRAVCPR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYVPQ---KAMFeaslP-LTV---MDFillnqtrFP-LFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:NF033858 78 IAYMPQglgKNLY----PtLSVfenLDF-------FGrLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170 180
....*....|....*....|..
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMD 178
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-212 |
3.28e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 8 SVLGPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQIDIQwASQELANKS----- 82
Cdd:PRK14258 2 SKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVE-GRVEFFNQNiyerr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 --------GVIGYVPQKAMFeaslPLTVMDFILLNQTRfpLFWRKRGKEQQNALAQLERVGMASRADRRMGQ----LSGG 150
Cdd:PRK14258 81 vnlnrlrrQVSMVHPKPNLF----PMSVYDNVAYGVKI--VGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 151 EQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEC-VKEGKTVLAVHHDVTAVRRL 212
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQVSRL 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-241 |
3.33e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.04 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-----ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI----------QWASQE 77
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQPTSGTVTIgervitagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 78 LANKSGVIGYVPQKAMFEAslplTVMDFILLNQTRFPLfwrKRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQQRVL 156
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLFEE----TVEKDICFGPMNFGV---SEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDSGRHQDILV 234
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKgTVFLQGTPREIFA 235
|
....*...
gi 1055853272 235 -PEKIERI 241
Cdd:PRK13634 236 dPDELEAI 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-228 |
3.49e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY-GENTILTDINHRFSAGECHVVMGPNGGGKTSLLrSIL--GLTPFSGQI-----DIQWASQELANKSgvI 85
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLqrVFDPQSGRIlidgtDIRTVTRASLRRN--I 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAMFeasLPLTVMDFILLNQTRFPLFWRKRGKEQQNALAQLER--VGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:PRK13657 412 AVVFQDAGL---FNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 164 DPALLVLDEPTTGMD-EQGVRYLECLikECVKEGKTVLAVHHDVTAVRRLDahvhvvnRILV-DSGR 228
Cdd:PRK13657 489 DPPILILDEATSALDvETEAKVKAAL--DELMKGRTTFIIAHRLSTVRNAD-------RILVfDNGR 546
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-186 |
8.78e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwasqelaNKSGVIGYV---- 88
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQeQPDSGTIKI--------GETVKLAYVdqsr 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 ----PQKAMFEA-SLPLtvmDFILLNQT---------RFPLfwrkRGKEQQnalaqlervgmasradRRMGQLSGGEQQR 154
Cdd:PRK11819 397 daldPNKTVWEEiSGGL---DIIKVGNReipsrayvgRFNF----KGGDQQ----------------KKVGVLSGGERNR 453
|
170 180 190
....*....|....*....|....*....|..
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLE 186
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDVETLRALE 485
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-178 |
1.01e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQIDIqwaSQELAN-----KSGViG 86
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDItSGDLFI---GEKRMNdvppaERGV-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKAmfeASLP-LTVMDfillNQTrFPLFWRKRGKEQQNalaqlERVGMASRA-------DRRMGQLSGGEQQRVLFA 158
Cdd:PRK11000 79 MVFQSY---ALYPhLSVAE----NMS-FGLKLAGAKKEEIN-----QRVNQVAEVlqlahllDRKPKALSGGQRQRVAIG 145
|
170 180
....*....|....*....|
gi 1055853272 159 QALLDDPALLVLDEPTTGMD 178
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-223 |
1.19e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTI-LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWASQELANKSGVigyvpqK 91
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPVTAEQPEDY------R 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMFEAslplTVMDFILLNQTRFPlfwrkRGKEQQNALAQ--LERVGMASRADRRMG-----QLSGGEQQRVLFAQALLDD 164
Cdd:PRK10522 397 KLFSA----VFTDFHLFDQLLGP-----EGKPANPALVEkwLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 165 PALLVLDEPTTGMDEQGVR--YLECL--IKEcvkEGKTVLAVHHDvtavrrlDAHVHVVNRIL 223
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRRefYQVLLplLQE---MGKTIFAISHD-------DHYFIHADRLL 520
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-227 |
1.24e-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: 64.04 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 39 GECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWAsqelanksgvIGYVPQKamFEASLPLTVMDFIL-LNQTRFPLF 116
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGvLKPDEGEVDEDLK----------ISYKPQY--ISPDYDGTVEEFLRsANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 117 WRKrgKEQQNALaQLERVgmasrADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD-EQgvRYLEC-LIKECVK 194
Cdd:COG1245 434 YYK--TEIIKPL-GLEKL-----LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDvEQ--RLAVAkAIRRFAE 503
|
170 180 190
....*....|....*....|....*....|....
gi 1055853272 195 E-GKTVLAVHHDVTAvrrLDahvHVVNRILVDSG 227
Cdd:COG1245 504 NrGKTAMVVDHDIYL---ID---YISDRLMVFEG 531
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
132-219 |
1.30e-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: 64.04 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 132 ERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD-EQGVRYLEcLIKECVKEGKTVLAVHHDVTAVR 210
Cdd:COG1245 198 EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVAR-LIRELAEEGKYVLVVEHDLAILD 276
|
....*....
gi 1055853272 211 RLDAHVHVV 219
Cdd:COG1245 277 YLADYVHIL 285
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-202 |
1.35e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHYGENT---ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP--FSGQI-------DIQWASQELANKs 82
Cdd:PRK13549 261 EVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWEGEIfidgkpvKIRNPQQAIAQG- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 gvIGYVPQKAMFEASLP-LTVMDFILL-NQTRFPLFWR-KRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQQRVLFA 158
Cdd:PRK13549 340 --IAMVPEDRKRDGIVPvMGVGKNITLaALDRFTGGSRiDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLA 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055853272 159 QALLDDPALLVLDEPTTGMDeQGVRY-LECLIKECVKEGKTVLAV 202
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGID-VGAKYeIYKLINQLVQQGVAIIVI 461
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
14-229 |
1.36e-11 |
|
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: 62.66 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-----LTP----FSGQIDIQWASQELANKSGV 84
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsyeVTSgtilFKGQDLLELEPDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGyvpqkamFEASLP---LTVMDFI--LLNQTRfplfwRKRGKEQQNALA-------QLERVGM-ASRADRRMGQ-LSGG 150
Cdd:TIGR01978 81 LA-------FQYPEEipgVSNLEFLrsALNARR-----SARGEEPLDLLDfekllkeKLALLDMdEEFLNRSVNEgFSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 151 EQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDvtaVRRLDA----HVHVV--NRILV 224
Cdd:TIGR01978 149 EKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY---QRLLNYikpdYVHVLldGRIVK 225
|
....*
gi 1055853272 225 DSGRH 229
Cdd:TIGR01978 226 SGDVE 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-243 |
1.97e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.49 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 6 TSSVLGPSIELK--NLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLR---SILGLTP-FSGQIDIQWASQELa 79
Cdd:PRK14243 1 TSTLNGTETVLRteNLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPgFRVEGKVTFHGKNL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 80 NKSGV--------IGYVPQKAM-FEASLPLTV------------MDFILLNQTRFPLFWRK-RGKEQQNALAqlervgma 137
Cdd:PRK14243 80 YAPDVdpvevrrrIGMVFQKPNpFPKSIYDNIaygaringykgdMDELVERSLRQAALWDEvKDKLKQSGLS-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 138 sradrrmgqLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDVTAVRRLDAHVH 217
Cdd:PRK14243 152 ---------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE-LKEQYTIIIVTHNMQQAARVSDMTA 221
|
250 260
....*....|....*....|....*..
gi 1055853272 218 VVNRILVDSGRHQDILVP-EKIERIFN 243
Cdd:PRK14243 222 FFNVELTEGGGRYGYLVEfDRTEKIFN 248
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
13-218 |
2.30e-11 |
|
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: 60.45 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTILtdinhrFSAGECHVVMGPNGGGKTSLLRSI-LGLTpfsgqidiQWASQELANKSGVIGYvpQK 91
Cdd:cd03227 1 KIVLGRFPSYFVPNDVT------FGEGSLTIITGPNGSGKSTILDAIgLALG--------GAQSATRRRSGVKAGC--IV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMFEASLPLTVMdfillnqtrfplfwrkrgkeqqnalaqlervgmasradrrmgQLSGGEQQRV----LFAQALLDDPAL 167
Cdd:cd03227 65 AAVSAELIFTRL------------------------------------------QLSGGEKELSalalILALASLKPRPL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 168 LVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHV 218
Cdd:cd03227 103 YILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
38-224 |
2.51e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 38 AGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiQWASQELANKSGvigyvpqKAM----------FE---ASL-P-LT 101
Cdd:COG4608 43 RGETLGLVGESGCGKSTLGRLLLRLeEPTSGEI--LFDGQDITGLSG-------RELrplrrrmqmvFQdpyASLnPrMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 102 VMDFI---LLNQTRFPlfwrkRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGM 177
Cdd:COG4608 114 VGDIIaepLRIHGLAS-----KAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 178 D----EQGVRYLECLIKEcvkEGKTVLAVHHDVTAVRrldahvHVVNRILV 224
Cdd:COG4608 189 DvsiqAQVLNLLEDLQDE---LGLTYLFISHDLSVVR------HISDRVAV 230
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
12-233 |
2.63e-11 |
|
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: 62.16 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI---DIQWASQELANKSGV--- 84
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrLAPDHGTAtyiMRSGAELELYQLSEAerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ------IGYVPQKAMfeASLPLTVMDFILLNQTRFPLFWRKRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQQRVLF 157
Cdd:TIGR02323 82 rlmrteWGFVHQNPR--DGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 158 AQALLDDPALLVLDEPTTGMD-EQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDSGRHQDIL 233
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDvSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQgRVVESGLTDQVL 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
31-224 |
3.02e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 31 DINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQiDIQWASQELANKSGV--------IGYVPQKAMfeASL-P-L 100
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDG-EVAWLGKDLLGMKDDewravrsdIQMIFQDPL--ASLnPrM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 101 TVMDFI---LlnQTRFPLFWRKRGKEQQNALaqLERVGM-ASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTG 176
Cdd:PRK15079 116 TIGEIIaepL--RTYHPKLSRQEVKDRVKAM--MLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 177 MD----EQGVRYLECLIKECvkeGKTVLAVHHDVTAVRrldahvHVVNRILV 224
Cdd:PRK15079 192 LDvsiqAQVVNLLQQLQREM---GLSLIFIAHDLAVVK------HISDRVLV 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-221 |
3.46e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 25 ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWAS----------QELANKSGVIGYVPQKAM 93
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALlKPTTGTVTVDDITithktkdkyiRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 94 FEAslplTVMDFILLNQTRFPLFWRKRGKEQQNALAQL--ERVGMASRAdrrmGQLSGGEQQRVLFAQALLDDPALLVLD 171
Cdd:PRK13646 99 FED----TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLgfSRDVMSQSP----FQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055853272 172 EPTTGMDEQGVRYLECLIKEC-VKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-205 |
3.96e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLHYGENTILTDinhrFSA----GECHVVMGPNGGGKTSLLRSILG-LTPFSGQIdiqwasqelanKSGV---IG 86
Cdd:PRK11147 321 EMENVNYQIDGKQLVKD----FSAqvqrGDKIALIGPNGCGKTTLLKLMLGqLQADSGRI-----------HCGTkleVA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQkamFEASLPL--TVMD-------FILLN-QTR--------FpLFWRKRGKEQQNALaqlervgmasradrrmgqlS 148
Cdd:PRK11147 386 YFDQ---HRAELDPekTVMDnlaegkqEVMVNgRPRhvlgylqdF-LFHPKRAMTPVKAL-------------------S 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 149 GGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcvKEGkTVLAVHHD 205
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS--YQG-TVLLVSHD 496
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-204 |
6.29e-11 |
|
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: 62.34 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 32 INHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQwASQELANKSgvIGYVPQ-KAMFEAslpLTVMD 104
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLlPPTSGTVlvggkDIE-TNLDAVRQS--LGMCPQhNILFHH---LTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 105 FILLnqtrfplFWRKRGKEQQNAL----AQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQ 180
Cdd:TIGR01257 1023 HILF-------YAQLKGRSWEEAQlemeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180
....*....|....*....|....*.
gi 1055853272 181 GVRYL-ECLIKecVKEGKT-VLAVHH 204
Cdd:TIGR01257 1096 SRRSIwDLLLK--YRSGRTiIMSTHH 1119
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
12-178 |
9.82e-11 |
|
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: 60.64 E-value: 9.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYgeNTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIdiqwasqelaNKSGVIGYVPQ 90
Cdd:cd03291 38 NNLFFSNLCLVG--APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKI----------KHSGRISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 kamFEASLPLTVMDFILLNQTrfplFWRKRGKEQQNAlAQLER--VGMASRADRRMGQ----LSGGEQQRVLFAQALLDD 164
Cdd:cd03291 106 ---FSWIMPGTIKENIIFGVS----YDEYRYKSVVKA-CQLEEdiTKFPEKDNTVLGEggitLSGGQRARISLARAVYKD 177
|
170
....*....|....
gi 1055853272 165 PALLVLDEPTTGMD 178
Cdd:cd03291 178 ADLYLLDSPFGYLD 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-243 |
1.33e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHY--GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFS---GQIDIQ---------WasqEL 78
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDnpnSKITVDgitltaktvW---DI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 79 ANKSGVIGYVPQKAMFEAslplTVMDfillnQTRFPLFWRKRGKEQQNALAQ--LERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:PRK13640 83 REKVGIVFQNPDNQFVGA----TVGD-----DVAFGLENRAVPRPEMIKIVRdvLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDvtavrrLDAHVHVVNRILVDSGRhqdILVP 235
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHD------IDEANMADQVLVLDDGK---LLAQ 224
|
....*...
gi 1055853272 236 EKIERIFN 243
Cdd:PRK13640 225 GSPVEIFS 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
131-219 |
2.39e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 131 LERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD-EQGVRYLEcLIKEcVKEGKTVLAVHHDVTAV 209
Cdd:PRK13409 197 VERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDiRQRLNVAR-LIRE-LAEGKYVLVVEHDLAVL 274
|
90
....*....|
gi 1055853272 210 RRLDAHVHVV 219
Cdd:PRK13409 275 DYLADNVHIA 284
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-219 |
2.39e-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: 60.22 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT---ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP--FSG-------QIDIQWASQELANK 81
Cdd:TIGR02633 258 LEARNLTCWDVINPhrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkFEGnvfingkPVDIRNPAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 SGVI-------GYVPQKAMFEaSLPLTVMDfillnqtRFPLFWR-KRGKEQQNALAQLERVGM-ASRADRRMGQLSGGEQ 152
Cdd:TIGR02633 338 IAMVpedrkrhGIVPILGVGK-NITLSVLK-------SFCFKMRiDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 153 QRVLFAQALLDDPALLVLDEPTTGMDeQGVRY-LECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVV 219
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVD-VGAKYeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
38-224 |
2.50e-10 |
|
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: 60.08 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 38 AGECHVVMGPNGGGKTSLLRSILGLTPFSGQIdiQWASQELANKSGvigyvpqKAM----------FE---ASL-P-LTV 102
Cdd:COG4172 311 RGETLGLVGESGSGKSTLGLALLRLIPSEGEI--RFDGQDLDGLSR-------RALrplrrrmqvvFQdpfGSLsPrMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 103 MDFI---LLnqtrfpLFWRKRGKEQQNALAQ--LERVGM-ASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTG 176
Cdd:COG4172 382 GQIIaegLR------VHGPGLSAAERRARVAeaLEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055853272 177 MDE--QgVRYLECLIKECVKEGKTVLAVHHDVTAVRRLdAHvhvvnRILV 224
Cdd:COG4172 456 LDVsvQ-AQILDLLRDLQREHGLAYLFISHDLAVVRAL-AH-----RVMV 498
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-178 |
2.50e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 1 MKKVTTSSVLgpsIELKNLNLHY----GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQID--IQWA 74
Cdd:PRK09473 3 PLAQQQADAL---LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGgsATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 75 SQELANksgvigyVPQKAMF-----EASL----PLT-----------VMDFILLNqtrfplfwRKRGKEQ--QNALAQLE 132
Cdd:PRK09473 80 GREILN-------LPEKELNklraeQISMifqdPMTslnpymrvgeqLMEVLMLH--------KGMSKAEafEESVRMLD 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055853272 133 RVGMaSRADRRMG----QLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD 178
Cdd:PRK09473 145 AVKM-PEARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-228 |
2.58e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.23 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQWAS----QELANKSGVIGY 87
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLlRPQKGKVLVSGIDtgdfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 88 VPQ--KAMFEASLPLTVMDFILLNQTRFPLFWRKRgkeQQNALAQlerVGMASRADRRMGQLSGGEQQRVLFAQALLDDP 165
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKR---VDRALAE---IGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 166 ALLVLDEPTTGMD-EQGVRYLEcLIKECVKEGKTVLAVHHDVtavrrldAHVHVVNRILV-DSGR 228
Cdd:PRK13644 156 ECLIFDEVTSMLDpDSGIAVLE-RIKKLHEKGKTIVYITHNL-------EELHDADRIIVmDRGK 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-202 |
3.28e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 15 ELKNLNLH-YGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwASQELANKS-------GVi 85
Cdd:COG3845 259 EVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLrPPASGSIRL--DGEDITGLSprerrrlGV- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAMFEASLP-LTVMD-FILLNQTRFPL---FWRKRGKEQQNALAQLERVG-MASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:COG3845 336 AYIPEDRLGRGLVPdMSVAEnLILGRYRRPPFsrgGFLDRKAIRAFAEELIEEFDvRTPGPDTPARSLSGGNQQKVILAR 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQGVRYL-ECLIKECvKEGKTVLAV 202
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIhQRLLELR-DAGAAVLLI 458
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-233 |
3.35e-10 |
|
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: 60.34 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 1 MKKVTTSSVLGPSIELKNLNLHY--GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQwasqe 77
Cdd:TIGR00957 624 IERRTIKPGEGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVHMK----- 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 78 lanksGVIGYVPQKAMFEASlplTVMDFILLNQTRFPlfwrKRGKEQQNALAQLERVGMASRADR-RMGQ----LSGGEQ 152
Cdd:TIGR00957 699 -----GSVAYVPQQAWIQND---SLRENILFGKALNE----KYYQQVLEACALLPDLEILPSGDRtEIGEkgvnLSGGQK 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 153 QRVLFAQALLDDPALLVLDEPTTGMDEQ-GVRYLECLI-KECVKEGKTVLAVHHDVTAVRRLDAHVHVVNRILVDSGRHQ 230
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQ 846
|
...
gi 1055853272 231 DIL 233
Cdd:TIGR00957 847 ELL 849
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
141-213 |
4.02e-10 |
|
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: 57.33 E-value: 4.02e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 141 DRRMGQLSGGEQQRVLFAQALLDDP--ALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLD 213
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSAD 156
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-221 |
5.34e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.98 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 1 MKKVTTSSVLGPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGG--KTSLLRSILGltPFSGQID---IQWAS 75
Cdd:NF000106 1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G--PDAGRRPwrf*TWCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 76 QELANKSGVIGYVPQKAMFEASLPLTVMDFILlnqTRFPLFWRKRGKEQQNALaqLERVGMASRADRRMGQLSGGEQQRV 155
Cdd:NF000106 79 NRRALRRTIG*HRPVR*GRRESFSGRENLYMI---GR*LDLSRKDARARADEL--LERFSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDR 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-204 |
5.43e-10 |
|
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: 57.25 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 20 NLHY------GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRsILGLTPFSGQI--DIQWASQEL-ANKSGVIGYVPQ 90
Cdd:cd03232 8 NLNYtvpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLD-VLAGRKTAGVItgEILINGRPLdKNFQRSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 KAMFEASLplTVmdfillnqtrfplfwrkrgkeqqnalaqleRVGMASRADRRmgQLSGGEQQRVLFAQALLDDPALLVL 170
Cdd:cd03232 87 QDVHSPNL--TV------------------------------REALRFSALLR--GLSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190
....*....|....*....|....*....|....
gi 1055853272 171 DEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHH 204
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
14-232 |
6.50e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTI----LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQI----------DIQWASQEla 79
Cdd:PRK11022 4 LNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmaeklefngqDLQRISEK-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 80 NKSGVIG----YVPQKAMFEASLPLTV----MDFILLNQTRfplfwrKRGKEQQNALAQLERVGM---ASRADRRMGQLS 148
Cdd:PRK11022 82 ERRNLVGaevaMIFQDPMTSLNPCYTVgfqiMEAIKVHQGG------NKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 149 GGEQQRVLFAQALLDDPALLVLDEPTTGMDEQ-GVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR-ILVDS 226
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTiQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAgQVVET 235
|
....*.
gi 1055853272 227 GRHQDI 232
Cdd:PRK11022 236 GKAHDI 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-221 |
7.22e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 18 NLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIdiQWASQELA-NKSGVIGYVPQKAMF- 94
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLlRPQKGAV--LWQGKPLDySKRGLLALRQQVATVf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 95 ---EASLPLTVMDfillNQTRFPLfwRKRGKEQQNALAQLERVGMASRADRRMGQ----LSGGEQQRVLFAQALLDDPAL 167
Cdd:PRK13638 84 qdpEQQIFYTDID----SDIAFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055853272 168 LVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQ 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-212 |
7.24e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSI--LG-LTP---FSGQIDIQWASQELANKSGV- 84
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPevtITGSIVYNGHNIYSPRTDTVd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 ----IGYVPQKAmfeASLPLTVMDFILLNqtrfplfWRKRGKEQQNALAQLERVGMASRA----------DRRMGqLSGG 150
Cdd:PRK14239 84 lrkeIGMVFQQP---NPFPMSIYENVVYG-------LRLKGIKDKQVLDEAVEKSLKGASiwdevkdrlhDSALG-LSGG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 151 EQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKEcVKEGKTVLAVHHDVTAVRRL 212
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRI 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-204 |
7.91e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.18 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGEN------TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIQ----------Wasq 76
Cdd:PRK13633 5 IKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlIPSEGKVYVDgldtsdeenlW--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 77 ELANKSGVIGYVPQKAMFEASLPLTVMdFILLNQTRFPLFWRKRGKEQqnalaqLERVGMASRADRRMGQLSGGEQQRVL 156
Cdd:PRK13633 82 DIRNKAGMVFQNPDNQIVATIVEEDVA-FGPENLGIPPEEIRERVDES------LKKVGMYEYRRHAPHLLSGGQKQRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055853272 157 FAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHH 204
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITH 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-202 |
7.92e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHYG---ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF--SGQIDIQwasqelanksGVIG 86
Cdd:PLN03232 613 PAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIR----------GSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKA-MFEAslplTVMDFILLNQTRFP-LFWRK-RGKEQQNALAQLERVGMASRADRRMgQLSGGEQQRVLFAQALLD 163
Cdd:PLN03232 683 YVPQVSwIFNA----TVRENILFGSDFESeRYWRAiDVTALQHDLDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYS 757
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYlecLIKECVKE---GKTVLAV 202
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQ---VFDSCMKDelkGKTRVLV 796
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
37-233 |
1.66e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.22 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 37 SAGECHVVMGPNGGGKTSLLRSILGLTPFSGQID---IQWASQELANKSGV---------IGYVPQKAMfeASL-P-LTV 102
Cdd:COG4170 31 NEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTadrFRWNGIDLLKLSPRerrkiigreIAMIFQEPS--SCLdPsAKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 103 MDFIL--LNQTRFP-LFWRKRGKEQQNALAQLERVG-------MASRADrrmgQLSGGEQQRVLFAQALLDDPALLVLDE 172
Cdd:COG4170 109 GDQLIeaIPSWTFKgKWWQRFKWRKKRAIELLHRVGikdhkdiMNSYPH----ELTEGECQKVMIAMAIANQPRLLIADE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 173 PTTGMDE----QGVRYLECLIKecvKEGKTVLAVHHDVTAVRRLdahvhvVNRI-------LVDSGRHQDIL 233
Cdd:COG4170 185 PTNAMESttqaQIFRLLARLNQ---LQGTSILLISHDLESISQW------ADTItvlycgqTVESGPTEQIL 247
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-221 |
2.01e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 28 ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILgltpfsGQIDIQwASQELANKSgvIGYVPQKAMFeasLPLTVMDFIL 107
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLL------SQFEIS-EGRVWAERS--IAYVPQQAWI---MNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 108 lnqtrfpLFWRKRGKEQQNAL--AQLER------VGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDE 179
Cdd:PTZ00243 743 -------FFDEEDAARLADAVrvSQLEAdlaqlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055853272 180 Q-GVRYLEclikECVK---EGKT-VLAVHhdvtavrrldaHVHVVNR 221
Cdd:PTZ00243 816 HvGERVVE----ECFLgalAGKTrVLATH-----------QVHVVPR 847
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-178 |
2.34e-09 |
|
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: 57.61 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 18 NLNLHYgeNTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIdiqwasqelaNKSGVIGYVPQkamFEA 96
Cdd:TIGR01271 433 NFSLYV--TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKI----------KHSGRISFSPQ---TSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 97 SLPLTVMDFILLNQTrfplFWRKRGKEQQNALAQLERVGMASRADRR-MGQ----LSGGEQQRVLFAQALLDDPALLVLD 171
Cdd:TIGR01271 498 IMPGTIKDNIIFGLS----YDEYRYTSVIKACQLEEDIALFPEKDKTvLGEggitLSGGQRARISLARAVYKDADLYLLD 573
|
....*..
gi 1055853272 172 EPTTGMD 178
Cdd:TIGR01271 574 SPFTHLD 580
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-204 |
2.36e-09 |
|
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: 57.45 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILT-DINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP-FSGQIDIqwasqelaNKSGVIGYVPQK 91
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIeSLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPvYGGRLTK--------PAKGKLFYVPQR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 92 AMFEASlplTVMDFILLNQTRFPLFwrKRGKEQQNALAQLERVGMASRADRRMG---------QLSGGEQQRVLFAQALL 162
Cdd:TIGR00954 524 PYMTLG---TLRDQIIYPDSSEDMK--RRGLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055853272 163 DDPALLVLDEPTTGM--DEQGVRYlecliKECVKEGKTVLAVHH 204
Cdd:TIGR00954 599 HKPQFAILDECTSAVsvDVEGYMY-----RLCREFGITLFSVSH 637
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
44-221 |
2.37e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.81 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 44 VMGPNGGGKTSLLRSILGLT-PFSGQI--------DIQWASQELANKSGvIGYVPQkamfEASLpltvmdfillnqtrFP 114
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTrPQKGRIvlngrvlfDAEKGICLPPEKRR-IGYVFQ----DARL--------------FP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 115 lFWRKRG----------KEQQNALAQLerVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVR- 183
Cdd:PRK11144 90 -HYKVRGnlrygmaksmVAQFDKIVAL--LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRe 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055853272 184 ---YLECLIKEcVKegKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:PRK11144 167 llpYLERLARE-IN--IPILYVSHSLDEILRLADRVVVLEQ 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-202 |
2.93e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 1 MKKVTTSSVLGPSIELKNLNLHygENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPF-SGQI-----DIQWA 74
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRaGGEIrlngkDISPR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 75 SQELANKSGvIGYVPQK-------AMFEASLPLTVMDFILLNQTRFPLFWRKRGKEQQNALAQLERVGM-ASRADRRMGQ 146
Cdd:PRK09700 331 SPLDAVKKG-MAYITESrrdngffPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALkCHSVNQNITE 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 147 LSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAV 202
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-228 |
2.98e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.74 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 35 RFS----AGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQWASQELANKSgvigYVPQKAMF-EASL--PLTVMDFI 106
Cdd:PRK10771 17 RFDltveRGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQDHTTTPPS----RRPVSMLFqENNLfsHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 107 LLNQTrfPLFwrKRGKEQQNALAQL-ERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYL 185
Cdd:PRK10771 93 GLGLN--PGL--KLNAAQREKLHAIaRQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055853272 186 ECLIKE-CVKEGKTVLAVHHDVTavrrlDAHVHVVNRILVDSGR 228
Cdd:PRK10771 169 LTLVSQvCQERQLTLLMVSHSLE-----DAARIAPRSLVVADGR 207
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-203 |
3.05e-09 |
|
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: 57.23 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHYGE--NTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQIDI---QWASQELANKSGVI 85
Cdd:TIGR01271 1215 GGQMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIdgvSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 86 GYVPQKAmfeaslpltvmdFILLNQTRFPLFWRKRGKEQQnALAQLERVGMASRADRRMGQ-----------LSGGEQQR 154
Cdd:TIGR01271 1295 GVIPQKV------------FIFSGTFRKNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQL 1361
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVH 203
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
147-233 |
3.60e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 147 LSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEgKTVLAVHHDVTAVRRLDAHVHVVNRILVDS 226
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
....*..
gi 1055853272 227 GRHQDIL 233
Cdd:PRK11176 560 GTHAELL 566
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-213 |
6.35e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 18 NLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDI--QWASQELANKSGVIGYVPQKAMF 94
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLlNPEKGEILFerQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 95 EASLPLTVMDFILLNQTRFPLfwrkrGKEQQNALAQLERVgmasrADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPT 174
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAV-----GITELCRLFSLEHL-----IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055853272 175 TGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLD 213
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-178 |
8.22e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENT-ILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQIDIqwasqelANKsgVIGYVPQ 90
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLeRITSGEIWI-------GGR--VVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 K----AM-FE--ASLP-LTV---MDFILLNqtrfplfwRKRGKEQQNalaqlERVGMASRA-------DRRMGQLSGGEQ 152
Cdd:PRK11650 74 AdrdiAMvFQnyALYPhMSVrenMAYGLKI--------RGMPKAEIE-----ERVAEAARIlelepllDRKPRELSGGQR 140
|
170 180
....*....|....*....|....*.
gi 1055853272 153 QRVLFAQALLDDPALLVLDEPTTGMD 178
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-211 |
9.56e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 29 LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTP---FSGQI----------DIQwAS---------QELAnksgvig 86
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsYEGEIlfdgevcrfkDIR-DSealgiviihQELA------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQkamfeaslpLTVMDFILLN--QTRFPLF-WRKRGKEqqnALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:NF040905 89 LIPY---------LSIAENIFLGneRAKRGVIdWNETNRR---ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055853272 164 DPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRR 211
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-213 |
9.71e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 9.71e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 147 LSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECV-KEGKTVLAVHHDVTAVRRLD 213
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKRSD 1426
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
29-204 |
9.90e-09 |
|
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: 54.26 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 29 LTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI-------DIQWASQELANKSGVIGYVPQKAMFeasLPL 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVhwsnkneSEPSFEATRSRNRYSVAYAAQKPWL---LNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 101 TVMDFILLNQTrfplFWRKRGKEQQNALAQLERVGMASRADR-----RMGQLSGGEQQRVLFAQALLDDPALLVLDEPTT 175
Cdd:cd03290 94 TVEENITFGSP----FNKQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|.
gi 1055853272 176 GMDEQGVRYL--ECLIKECVKEGKTVLAVHH 204
Cdd:cd03290 170 ALDIHLSDHLmqEGILKFLQDDKRTLVLVTH 200
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
118-228 |
1.13e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.32 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 118 RKRGKEQQNA--LAQLERVGMASRA---DRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD--EQgVRYLECLIK 190
Cdd:PRK10418 107 LALGKPADDAtlTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDvvAQ-ARILDLLES 185
|
90 100 110
....*....|....*....|....*....|....*...
gi 1055853272 191 ECVKEGKTVLAVHHDVTAVRRLDAHVHVvnrilVDSGR 228
Cdd:PRK10418 186 IVQKRALGMLLVTHDMGVVARLADDVAV-----MSHGR 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-238 |
1.39e-08 |
|
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: 54.81 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHY-----GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDI----QWASQelaNK 81
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLePTSGEVNVrvgdEWVDM---TK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 82 SGVIG---YVPQKAMFEASLPLTVMDFILLNQTR-----FPLFWRKRgkeqqNALAQLERVGMASRA-----DRRMGQLS 148
Cdd:TIGR03269 355 PGPDGrgrAKRYIGILHQEYDLYPHRTVLDNLTEaigleLPDELARM-----KAVITLKMVGFDEEKaeeilDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 149 GGEQQRVLFAQALLDDPALLVLDEPTTGMDE-QGVRYLECLIKECVKEGKTVLAVHHDVTAVRrldahvHVVNRI-LVDS 226
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVL------DVCDRAaLMRD 503
|
250
....*....|..
gi 1055853272 227 GRHQDILVPEKI 238
Cdd:TIGR03269 504 GKIVKIGDPEEI 515
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
145-200 |
1.60e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 1.60e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 145 GQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDeQGVRY-LECLIKECVKEGKTVL 200
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID-VGAKYeIYTIINELAAEGKGVI 458
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
141-219 |
1.68e-08 |
|
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: 53.91 E-value: 1.68e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055853272 141 DRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVV 219
Cdd:cd03236 134 DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-210 |
1.72e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 38 AGECHVVMGPNGGGKTSLLRSILGL--------------TPFSGQIDIQWAS-----QELanksgviGYVPQkamfeasl 98
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIytrdagsilylgkeVTFNGPKSSQEAGigiihQEL-------NLIPQ-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 99 pLTVMDFILLNQ---TRF-PLFWRKRGKEqqnALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPT 174
Cdd:PRK10762 94 -LTIAENIFLGRefvNRFgRIDWKKMYAE---ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055853272 175 TGMDEQGVRYLECLIKECVKEGKTVLAVHH----------DVTAVR 210
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVYISHrlkeifeicdDVTVFR 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
39-233 |
2.09e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.27 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 39 GECHVVMGPNGGGKTSLLRSILGLT-PFSGQIDIQWASQELANKSGVIGYVPQK-AMFEASLPLtVMDFILLNQTRF--P 114
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKISDAELREVRRKKiAMVFQSFAL-MPHMTVLDNTAFgmE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 115 LFWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQ-GVRYLECLIKECV 193
Cdd:PRK10070 133 LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLiRTEMQDELVKLQA 212
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055853272 194 KEGKTVLAVHHDVTAVRRLDAHVHVV-NRILVDSGRHQDIL 233
Cdd:PRK10070 213 KHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEIL 253
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-204 |
3.25e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 29 LTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSGQI-----DIQWASQELANKSGVigyvpqkAMFEASLPL-- 100
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSIlfqgkEIDFKSSKEALENGI-------SMVHQELNLvl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 101 --TVMDFILLNqtRFPL--FWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTG 176
Cdd:PRK10982 87 qrSVMDNMWLG--RYPTkgMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180
....*....|....*....|....*...
gi 1055853272 177 MDEQGVRYLECLIKECVKEGKTVLAVHH 204
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-205 |
3.76e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIeLKNLNlhYGentilTDINHRFSagechvVMGPNGGGKTSLLRSILGltpfsgqidiqwasqELANKSGVIGYVPQ 90
Cdd:PLN03073 521 GPLL-FKNLN--FG-----IDLDSRIA------MVGPNGIGKSTILKLISG---------------ELQPSSGTVFRSAK 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 91 KAMfeASLPLTVMDFILLNQTrfPLFWRKR---GKEQQNALAQLERVGMA-SRADRRMGQLSGGEQQRVLFAQALLDDPA 166
Cdd:PLN03073 572 VRM--AVFSQHHVDGLDLSSN--PLLYMMRcfpGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPH 647
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055853272 167 LLVLDEPTTGMDEQGVrylECLIKECVKEGKTVLAVHHD 205
Cdd:PLN03073 648 ILLLDEPSNHLDLDAV---EALIQGLVLFQGGVLMVSHD 683
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
49-224 |
3.85e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 49 GGGKTSLLRSILGLT-PFSGQID-----IQWASQELANKSGVIgYVPQKAMFEASLPL-TVMDFILLNQTRFPLFWR--- 118
Cdd:PRK11288 289 GAGRSELMKLLYGATrRTAGQVYldgkpIDIRSPRDAIRAGIM-LCPEDRKAEGIIPVhSVADNINISARRHHLRAGcli 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 119 KRGKEQQNALAQLERVGMASR-ADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGK 197
Cdd:PRK11288 368 NNRWEAENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGV 447
|
170 180
....*....|....*....|....*..
gi 1055853272 198 TVLAVHHDVTAVrrldahVHVVNRILV 224
Cdd:PRK11288 448 AVLFVSSDLPEV------LGVADRIVV 468
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-202 |
4.80e-08 |
|
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: 51.88 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 4 VTTSSVLGPSIELKNLNLHYgentILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFSGQI--DIQW---ASQEL 78
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIP----ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVegDIHYngiPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 79 ANK-SGVIGYVPQKAMFEAslPLTV---MDFILLnqtrfplfwrkrgkeqqnalaqlervgmaSRADRRMGQLSGGEQQR 154
Cdd:cd03233 78 AEKyPGEIIYVSEEDVHFP--TLTVretLDFALR-----------------------------CKGNEFVRGISGGERKR 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVryLECL--IKECVKEGKTVLAV 202
Cdd:cd03233 127 VSIAEALVSRASVLCWDNSTRGLDSSTA--LEILkcIRTMADVLKTTTFV 174
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-198 |
5.13e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 12 PSIELKNLNLHY---GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFS-GQIDIQwasqelanksGVIG 86
Cdd:PLN03130 613 PAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSdASVVIR----------GTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKA-MFEAslplTVMDFILL----NQTRfplFWRK-RGKEQQNALAQLERvGMASRADRRMGQLSGGEQQRVLFAQA 160
Cdd:PLN03130 683 YVPQVSwIFNA----TVRDNILFgspfDPER---YERAiDVTALQHDLDLLPG-GDLTEIGERGVNISGGQKQRVSMARA 754
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055853272 161 LLDDPALLVLDEPTTGMDEQGVRYlecLIKECVKE---GKT 198
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQ---VFDKCIKDelrGKT 792
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-219 |
8.31e-08 |
|
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: 51.03 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 36 FSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGqiDIQWASQELAnksgvigYVPQKAmfeaslpltvmdfillnqtrfp 114
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGqLIPNGD--NDEWDGITPV-------YKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 115 lfwrkrgkeqqnalaqlervgmasradrrmgQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVK 194
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180
....*....|....*....|....*.
gi 1055853272 195 EG-KTVLAVHHDVTAVRRLDAHVHVV 219
Cdd:cd03222 120 EGkKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-206 |
9.77e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDIN---HRFSAGECHVVMGPNGGGKTSLLRSILGL-TPFSG--QIDIQWASQE----LANKSG 83
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGkvKIDGELLTAEnvwnLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 VIGYVPQKAMFEASLPLTVMdFILLNQtrfplfwrkrGKEQQNALAQLER----VGMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:PRK13642 85 MVFQNPDNQFVGATVEDDVA-FGMENQ----------GIPREEMIKRVDEallaVNMLDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055853272 160 ALLDDPALLVLDEPTTGMDEQGVRYLECLIKECV-KEGKTVLAVHHDV 206
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDL 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-228 |
1.12e-07 |
|
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: 50.87 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGEN--TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQI---DIQWASQELANKSGVIG 86
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRfLEAEEGKIeidGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQKamfeaslPLTVMDFILLNQTRFplfwrkrgKEQQNalaqlERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPA 166
Cdd:cd03369 86 IIPQD-------PTLFSGTIRSNLDPF--------DEYSD-----EEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 167 LLVLDEPTTGMDEQGvrylECLIKECVKE---GKTVLAVHHDVTAVRRLDahvhvvnRILV-DSGR 228
Cdd:cd03369 146 VLVLDEATASIDYAT----DALIQKTIREeftNSTILTIAHRLRTIIDYD-------KILVmDAGE 200
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
141-224 |
1.21e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 141 DRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVrrldahVHVVN 220
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEV------LGMSD 463
|
....
gi 1055853272 221 RILV 224
Cdd:PRK10762 464 RILV 467
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-244 |
2.18e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 24 GENTILTDINHRFSAGECHVVMGPNGGGKTS----LLRSIL--GLTPFSGQIDIQWASQELANKSGVIGYVPQKAMFEAS 97
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 98 LPLTVMDFIL--LNQTRFPLFWRKRgkeQQNALAQLERVGM--ASRaDRRMGQLSGGEQQRVLFAQALLDDPALLVLDEP 173
Cdd:PRK15134 377 PRLNVLQIIEegLRVHQPTLSAAQR---EQQVIAVMEEVGLdpETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 174 TTGMDEQ-GVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDAHVHVVnrilvdsgRHQDILVPEKIERIFNH 244
Cdd:PRK15134 453 TSSLDKTvQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL--------RQGEVVEQGDCERVFAA 516
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
14-178 |
3.13e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGL---------TPFSGQIDIQWASQELANKSGV 84
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedyevtggtVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 85 IGYvpqkaMFEASLPLTVMDFILlnQTRFPLFWRKRGKEqqnalaQLERVGMASRADRRMGQL---------------SG 149
Cdd:PRK09580 82 MAF-----QYPVEIPGVSNQFFL--QTALNAVRSYRGQE------PLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSG 148
|
170 180
....*....|....*....|....*....
gi 1055853272 150 GEQQRVLFAQALLDDPALLVLDEPTTGMD 178
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
126-219 |
4.84e-07 |
|
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: 49.18 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 126 NALAQLERVGMAS-RADRRMGQLSGGEQQRVLFAQAL---LDDpALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLA 201
Cdd:cd03270 116 ERLGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIgsgLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLV 194
|
90
....*....|....*...
gi 1055853272 202 VHHDVTAVRRLDahvHVV 219
Cdd:cd03270 195 VEHDEDTIRAAD---HVI 209
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-213 |
5.32e-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: 50.40 E-value: 5.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 143 RMGQ----LSGGEQQRVLFAQALL---DDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLD 213
Cdd:TIGR00630 822 RLGQpattLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTAD 899
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-213 |
5.44e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 5.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 142 RRMGQLSGGEQQRVLFAQALL---DDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLD 213
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVAD 879
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
46-228 |
8.38e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 46 GPNGGGKTSLLRSILG-LTPFSGQIDiqwasqelanksgVIGYVP----------------QKAMFEASLPltVMD-FIL 107
Cdd:COG4586 55 GPNGAGKSTTIKMLTGiLVPTSGEVR-------------VLGYVPfkrrkefarrigvvfgQRSQLWWDLP--AIDsFRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 108 L------NQTRFplfwRKRgkeqqnaLAQL-ERVGMASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD-- 178
Cdd:COG4586 120 LkaiyriPDAEY----KKR-------LDELvELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvv 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 179 -EQGVRylECLIKECVKEGKTVLAVHHDVTAVRRLdahvhvVNRILV-DSGR 228
Cdd:COG4586 189 sKEAIR--EFLKEYNRERGTTILLTSHDMDDIEAL------CDRVIViDHGR 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-238 |
9.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.85 E-value: 9.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 14 IELKNLNLHYGENT-----ILTDINHRFSAGECHVVMGPNGGGKTSLLR------------SILGLTPFSGQIDIQWASQ 76
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 77 ELANKSGVIGYVPQKAMFEaslpltvmDFILLNQTRFPLFWRKRGKEQQNALAQLERVGMASR--ADRRMGQLSGGEQQR 154
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQ--------ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 155 VLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVRRLDAHVhvvnrILVDSGRHQDIL 233
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEV-----IVMHEGKVISIG 233
|
....*
gi 1055853272 234 VPEKI 238
Cdd:PRK13645 234 SPFEI 238
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
143-213 |
9.94e-07 |
|
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: 48.76 E-value: 9.94e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055853272 143 RMGQ----LSGGEQQRVLFAQALL---DDPALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLD 213
Cdd:cd03271 162 KLGQpattLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCAD 239
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
144-226 |
1.03e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 144 MGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDeQGVRY-LECLIKECVKEGKTVLAVHHDVTAVrrldahVHVVNRI 222
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID-VGAKFeIYQLIAELAKKDKGIIIISSEMPEL------LGITDRI 461
|
....
gi 1055853272 223 LVDS 226
Cdd:PRK10982 462 LVMS 465
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
117-219 |
1.39e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 117 WRKRgkeqqNALAQLERVGMASRADRrMG----QLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD----EQGVRYLECL 188
Cdd:PRK15093 131 WRKR-----RAIELLHRVGIKDHKDA-MRsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEpttqAQIFRLLTRL 204
|
90 100 110
....*....|....*....|....*....|.
gi 1055853272 189 IKecvKEGKTVLAVHHDVTAVRRLDAHVHVV 219
Cdd:PRK15093 205 NQ---NNNTTILLISHDLQMLSQWADKINVL 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-212 |
1.77e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.77 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 22 HYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILG-LTPFSGQIDIQwasqelanksgviGYVPqkAMFEASLP- 99
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTSGRVEVN-------------GRVS--ALLELGAGf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 100 ---LTVMDFILLNqtrfplfwrkrG------KEQQNAL-------AQLERVgmasrADRRMGQLSGGEQQRVLFAQALLD 163
Cdd:COG1134 100 hpeLTGRENIYLN-----------GrllglsRKEIDEKfdeivefAELGDF-----IDQPVKTYSSGMRARLAFAVATAV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 164 DPALLVLDEPTTGMDEqgvRYLE-CL--IKECVKEGKTVLAVHHDVTAVRRL 212
Cdd:COG1134 164 DPDILLVDEVLAVGDA---AFQKkCLarIRELRESGRTVIFVSHSMGAVRRL 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
142-204 |
2.27e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 142 RRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIkecVKEGKTVLAVHH 204
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL---LKWPKTFIVVSH 399
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
144-186 |
2.66e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.66e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1055853272 144 MGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLE 186
Cdd:PRK15064 153 MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLE 195
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
135-185 |
3.39e-06 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 44.15 E-value: 3.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055853272 135 GMASRADRRMGQLSGGEQQrVLFAQALL--------------DDPALLVLDEPTTGMDEQGVRYL 185
Cdd:pfam13558 21 GSEVETYRRSGGLSGGEKQ-LLAYLPLAaalaaqygsaegrpPAPRLVFLDEAFAKLDEENIRTA 84
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
127-178 |
3.57e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 3.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 127 ALAQLERVGM-ASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD 178
Cdd:PRK11308 134 ALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
140-191 |
4.30e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 4.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 140 ADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKE 191
Cdd:PRK11147 150 PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
146-230 |
1.65e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 146 QLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGvrylECLIKECV-----KEGKTVLAVHHDVTAVRrldahvhVVN 220
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS----EYLVQKTInnlkgNENRITIIIAHRLSTIR-------YAN 647
|
90
....*....|
gi 1055853272 221 RILVDSGRHQ 230
Cdd:PTZ00265 648 TIFVLSNRER 657
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
146-224 |
1.78e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 146 QLSGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKE-GKTVLAVHHDVTAVrrldahVHVVNRILV 224
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVV------AEIADRVLV 241
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
18-59 |
2.19e-05 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 44.16 E-value: 2.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1055853272 18 NLNLHYGENTILTDINhrFSAGECHVVMGPNGGGKTSLLRSI 59
Cdd:cd03243 10 LLALTKGETFVPNDIN--LGSGRLLLITGPNMGGKSTYLRSI 49
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-205 |
3.65e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 3.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055853272 141 DRRMGQLSGGEQQRVLFAQALLDDPA--LLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHD 205
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-209 |
4.62e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 28 ILTDINHRFSAGECHVVMGPNGGGKTSLL-----RSILGLTPFSGQIDIQWASQELANKSgvIGYVPQKAMFEASLplTV 102
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVITGGDRLVNGRPLDSSFQRS--IGYVQQQDLHLPTS--TV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 103 MDFIllnqtRFPLFWR---KRGKEQQNALAQ--LERVGMASRADRRMGQLSGG---EQ-QRVLFAQALLDDPALLV-LDE 172
Cdd:TIGR00956 854 RESL-----RFSAYLRqpkSVSKSEKMEYVEevIKLLEMESYADAVVGVPGEGlnvEQrKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055853272 173 PTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAV 209
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAI 965
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
44-220 |
4.96e-05 |
|
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: 42.36 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 44 VMGPNGGGKTSLLRSILGLtpfsgqidiqwasqelanksgvigyvpqkamfeasLPLTVMDFILLNQTRFPLFWRKRGKE 123
Cdd:smart00382 7 IVGPPGSGKTTLARALARE-----------------------------------LGPPGGGVIYIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 124 QQNalaqlervgmasraDRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPT------TGMDEQGVRYLECLIKECVKEGK 197
Cdd:smart00382 52 IIV--------------GGKKASGSGELRLRLALALARKLKPDVLILDEITslldaeQEALLLLLEELRLLLLLKSEKNL 117
|
170 180
....*....|....*....|....*....
gi 1055853272 198 TVLAVHHDVT------AVRRLDAHVHVVN 220
Cdd:smart00382 118 TVILTTNDEKdlgpalLRRRFDRRIVLLL 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-178 |
7.63e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 11 GPSIELKNLNLHYGENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFS-------GQ-IDiqwaSQELANKS 82
Cdd:NF033858 264 EPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASegeawlfGQpVD----AGDIATRR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 83 GViGYVPQKamFeaSL--PLTVMDFILLNQTRFPLfwrkRGKEQQNALAQL-ERVGMASRADRRMGQLSGGEQQRVLFAQ 159
Cdd:NF033858 340 RV-GYMSQA--F--SLygELTVRQNLELHARLFHL----PAAEIAARVAEMlERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170
....*....|....*....
gi 1055853272 160 ALLDDPALLVLDEPTTGMD 178
Cdd:NF033858 411 AVIHKPELLILDEPTSGVD 429
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-219 |
7.85e-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: 43.85 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 141 DRRMGQLSGGEQQRVLFAQAL---LDDpALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHHDVTAVRRLDahvH 217
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIgsgLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAAD---Y 558
|
..
gi 1055853272 218 VV 219
Cdd:TIGR00630 559 VI 560
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
13-183 |
1.05e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGENTIltdinhRFSAGeCHVVMGPNGGGKTSLLRSI-LGLT-PFSGQIDIQwasQELANKSGVIGYV-- 88
Cdd:COG0419 4 RLRLENFRSYRDTETI------DFDDG-LNLIVGPNGAGKSTILEAIrYALYgKARSRSKLR---SDLINVGSEEASVel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 89 -------------PQKAM--FEASLPLTVMDFI--LLNQTRFPLFWRKRGKEQQNALAQLERVGMASRADRR-------- 143
Cdd:COG0419 74 efehggkryrierRQGEFaeFLEAKPSERKEALkrLLGLEIYEELKERLKELEEALESALEELAELQKLKQEilaqlsgl 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055853272 144 --MGQLSGGEQQRVLFAQALlddpaLLVLDepTTGMDEQGVR 183
Cdd:COG0419 154 dpIETLSGGERLRLALADLL-----SLILD--FGSLDEERLE 188
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
43-218 |
1.78e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 43 VVMGPNGGGKTSLLRSIL-GLTP-FSGQIDIQWASQELANKSGVIGYVpqKAMFEASLPLTVMDFILLNQTRFPLFWRKr 120
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyALTGeLPPNSKGGAHDPKLIREGEVRAQV--KLAFENANGKKYTITRSLAILENVIFCHQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 121 gkEQQNALAQLERvgmasradrrmGQLSGGeqQRVLF--------AQALLDDPALLVLDEPTTGMDEQGVR-YLECLIKE 191
Cdd:cd03240 103 --GESNWPLLDMR-----------GRCSGG--EKVLAsliirlalAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEE 167
|
170 180
....*....|....*....|....*...
gi 1055853272 192 C-VKEGKTVLAVHHDVTAVRRLDAHVHV 218
Cdd:cd03240 168 RkSQKNFQLIVITHDEELVDAADHIYRV 195
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-233 |
2.09e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 25 ENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGltpfsgQIDIQwasqelankSGVIGYvpqkamfeASLPLTVMD 104
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQR------HFDVS---------EGDIRF--------HDIPLTKLQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 105 -------FILLNQTRFpLFWRKRG-----------KEQQNALAQLERV---------GMASRADRRMGQLSGGEQQRVLF 157
Cdd:PRK10789 384 ldswrsrLAVVSQTPF-LFSDTVAnnialgrpdatQQEIEHVARLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 158 AQALLDDPALLVLDEPTTGMDEQgvryLECLIKECVK---EGKTVLAVHHDVTAVRRLD-----AHVHVVNRilvdsGRH 229
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGR----TEHQILHNLRqwgEGRTVIISAHRLSALTEASeilvmQHGHIAQR-----GNH 533
|
....
gi 1055853272 230 QDIL 233
Cdd:PRK10789 534 DQLA 537
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
143-206 |
3.08e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 3.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055853272 143 RMGQ----LSGGEQQRVLFAQALLDDP---ALLVLDEPTTGMDEQGVRYLECLIKECVKEGKTVLAVHH--DV 206
Cdd:PRK00349 823 KLGQpattLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHnlDV 895
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-206 |
4.66e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 4.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055853272 143 RMGQ----LSGGEQQRVLFAQALLD---DPALLVLDEPTTGM---DEQgvRYLECLiKECVKEGKTVLAVHH--DV 206
Cdd:COG0178 819 KLGQpattLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLhfhDIR--KLLEVL-HRLVDKGNTVVVIEHnlDV 891
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
121-221 |
6.74e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 121 GKEQQNALAQL-ERVGM-ASRADRRMGQLSGGEQQRVLFAQALLDDPALLVLDEPTTGMD----EQGVRYLECLIKECvk 194
Cdd:PRK10261 436 GKAAAARVAWLlERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvsirGQIINLLLDLQRDF-- 513
|
90 100
....*....|....*....|....*..
gi 1055853272 195 eGKTVLAVHHDVTAVRRLDAHVHVVNR 221
Cdd:PRK10261 514 -GIAYLFISHDMAVVERISHRVAVMYL 539
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
133-204 |
1.11e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 133 RVGMASRADrrmgQLSGGEQQ------RVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIKECVKEG----KTVLAV 202
Cdd:PRK01156 792 RGGMVEGID----SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSsdipQVIMIS 867
|
..
gi 1055853272 203 HH 204
Cdd:PRK01156 868 HH 869
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-238 |
3.45e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 38.80 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 10 LGPSIELKNLNLHY--GENTILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLTPFS-GQI---DIQWASQELANKSG 83
Cdd:PLN03232 1231 SRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRImidDCDVAKFGLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 84 VIGYVPQK-AMFEASLPLTVMDFILLNQTRFplfWRKRGKEQQNALAQLERVGMASRADRRMGQLSGGEQQRVLFAQALL 162
Cdd:PLN03232 1311 VLSIIPQSpVLFSGTVRFNIDPFSEHNDADL---WEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 163 DDPALLVLDEPTTGMDeqgVRyLECLIKECVKE---GKTVLAVHHDVTAVRRLDahvhvvnRILV-DSGRHQDILVPEKI 238
Cdd:PLN03232 1388 RRSKILVLDEATASVD---VR-TDSLIQRTIREefkSCTMLVIAHRLNTIIDCD-------KILVlSSGQVLEYDSPQEL 1456
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-238 |
5.30e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.18 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 13 SIELKNLNLHYGEN--TILTDINHRFSAGECHVVMGPNGGGKTSLLRSILGLT-PFSGQI---DIQWASQELANKSGVIG 86
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVeLERGRIlidGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 87 YVPQK-AMFEASLpltvmdfillnqtRFPL--FWRKRGKEQQNAL--AQLERV------GMASRADRRMGQLSGGEQQRV 155
Cdd:PLN03130 1317 IIPQApVLFSGTV-------------RFNLdpFNEHNDADLWESLerAHLKDVirrnslGLDAEVSEAGENFSVGQRQLL 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055853272 156 LFAQALLDDPALLVLDEPTTGMDeqgVRyLECLIKECVKE---GKTVLAVHHDVTAVRRLDahvhvvnRILV-DSGRHQD 231
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD---VR-TDALIQKTIREefkSCTMLIIAHRLNTIIDCD-------RILVlDAGRVVE 1452
|
....*..
gi 1055853272 232 ILVPEKI 238
Cdd:PLN03130 1453 FDTPENL 1459
|
|
| AAA_27 |
pfam13514 |
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain ... |
16-62 |
7.70e-03 |
|
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain contains a P-loop motif.
Pssm-ID: 433272 [Multi-domain] Cd Length: 207 Bit Score: 36.76 E-value: 7.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1055853272 16 LKNLNLH-YG--ENTILTdinhrFSAGEC--HVVMGPNGGGKTSLLRSILGL 62
Cdd:pfam13514 3 IRRLDLErYGpfTDRSLD-----FPAGGPdlHLIYGPNEAGKSTALRAISDL 49
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
148-190 |
7.89e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 7.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1055853272 148 SGGEQQRVLFAQALLDDPALLVLDEPTTGMDEQGVRYLECLIK 190
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK 193
|
|
| |
