|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-251 |
2.82e-96 |
|
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: 282.32 E-value: 2.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAY 84
Cdd:COG1120 1 MLEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQSHTAAFPYSVRRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKAL 164
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSL 243
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEA 239
|
....*...
gi 2035452788 244 KQVDHEGS 251
Cdd:COG1120 240 RVIEDPVT 247
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-249 |
1.31e-74 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 227.28 E-value: 1.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAysassVAQ 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 81 QLAYVPQSHT--AAFPYSVRRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALA 158
Cdd:COG1121 76 RIGYVPQRAEvdWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 159 QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLdDGHIVADGLPQNVVTAEHMSRL 238
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRA 234
|
250
....*....|.
gi 2035452788 239 YGVSLKQVDHE 249
Cdd:COG1121 235 YGGPVALLAHG 245
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-248 |
1.74e-71 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 219.60 E-value: 1.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAY 84
Cdd:COG4559 1 MLEAENLSVRLGGR-TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQSHTAAFPYSVRRMIELGRVPHTGlgsaLRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQ----- 159
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRAPHGS----SAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 160 --EAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLIL-------LTShrpeeLFapASRVLVLDDGHIVADGLPQNVV 230
Cdd:COG4559 156 dgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVavlhdlnLAA-----QY--ADRILLLHQGRLVAQGTPEEVL 228
|
250
....*....|....*...
gi 2035452788 231 TAEHMSRLYGVSLKQVDH 248
Cdd:COG4559 229 TDELLERVYGADLRVLAH 246
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-248 |
8.59e-69 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 212.71 E-value: 8.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAY 84
Cdd:PRK13548 2 MLEARNLSVRLGGR-TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQSHTAAFPYSVRRMIELGRVPHTGlgsaLRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQ----- 159
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGL----SRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 160 -EAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL----IL----LTSHRpeelfapASRVLVLDDGHIVADGLPQNVV 230
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLavivVLhdlnLAARY-------ADRIVLLHQGRLVADGTPAEVL 229
|
250
....*....|....*...
gi 2035452788 231 TAEHMSRLYGVSLKQVDH 248
Cdd:PRK13548 230 TPETLRRVYGADVLVQPH 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-241 |
2.57e-61 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 193.69 E-value: 2.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFPYSVRR 99
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQL 179
Cdd:PRK11231 96 LVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 180 RLMSLLGEFAAEGRLILLTSHRPEElfapASR----VLVLDDGHIVADGLPQNVVTAEHMSRLYGV 241
Cdd:PRK11231 176 ELMRLMRELNTQGKTVVTVLHDLNQ----ASRycdhLVVLANGHVMAQGTPEEVMTPGLLRTVFDV 237
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-224 |
3.95e-61 |
|
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: 190.34 E-value: 3.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 7 ACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVP 86
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 87 QshtaafpysvrrmielgrvphtglgsalraedhaavdhAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLL 166
Cdd:cd03214 80 Q--------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 167 DEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-224 |
4.74e-61 |
|
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: 191.59 E-value: 4.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 8 CEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAssvaqQLAYVPQ 87
Cdd:cd03235 2 VEDLTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 SHTA--AFPYSVRRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALL 165
Cdd:cd03235 76 RRSIdrDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLdDGHIVADG 224
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-241 |
5.43e-57 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 186.97 E-value: 5.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFPYSVRR 99
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQL 179
Cdd:PRK09536 97 VVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 180 RLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGV 241
Cdd:PRK09536 177 RTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDA 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-233 |
4.34e-53 |
|
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: 171.75 E-value: 4.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYV 85
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQshtaaFP------YSVRRMIELGrvP-HTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALA 158
Cdd:COG1122 81 FQ-----NPddqlfaPTVEEDVAFG--PeNLGLP---REEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 159 QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAE 233
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-250 |
3.66e-52 |
|
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: 169.88 E-value: 3.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRG-HVLLEGKPLGAYSASSVAQQLA 83
Cdd:COG1119 3 LLELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 84 YVPQSHTAAFPY--SVRRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:COG1119 82 LVSPALQLRFPRdeTVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYG 240
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFG 241
|
250
....*....|
gi 2035452788 241 VSLkQVDHEG 250
Cdd:COG1119 242 LPV-EVERRD 250
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-242 |
7.21e-51 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 165.79 E-value: 7.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 27 VSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSassvaQQLAYVPQSHTAA--FPYSVRRMIELG 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGW-----RHIGYVPQRHEFAwdFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 105 RVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSL 184
Cdd:TIGR03771 76 RTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 185 LGEFAAEGRLILLTSHRPEELFAPASRVLVLdDGHIVADGLPQNVVTAEHMSRLYGVS 242
Cdd:TIGR03771 156 FIELAGAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-253 |
1.95e-50 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 165.64 E-value: 1.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQS 88
Cdd:COG4604 5 KNVSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 89 HTAAFPYSVRRMIELGRVPHTGlgSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDE 168
Cdd:COG4604 84 NHINSRLTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 169 PMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHrpeEL-FAP--ASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSLK 244
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH---DInFAScyADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIE 238
|
....*....
gi 2035452788 245 QVDHEGSRF 253
Cdd:COG4604 239 VEEIDGKRI 247
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-229 |
3.97e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.08 E-value: 3.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAsSVAQQLAYV 85
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQsHTAAFPY-SVRRMIELgrvpHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKAL 164
Cdd:COG1131 79 PQ-EPALYPDlTVRENLRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-254 |
2.48e-48 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 160.01 E-value: 2.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLkPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFPYSVRRMI 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 ELGRVPHTglgsalraeDHAAVDHAMA----RLGLQEMAERPVTQLSGGERQRVVLARALAQ-------EAKALLLDEPM 170
Cdd:COG4138 91 ALHQPAGA---------SSEAVEQLLAqlaeALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 171 TGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSLKQVDHEG 250
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVEG 241
|
....
gi 2035452788 251 SRFF 254
Cdd:COG4138 242 HRWL 245
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-240 |
2.70e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.53 E-value: 2.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQ---Q 81
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 82 LAYVPQSHtaafpYSVRRM--IE---LGRVPHTGLGSALR----AEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVV 152
Cdd:COG3638 82 IGMIFQQF-----NLVPRLsvLTnvlAGRLGRTSTWRSLLglfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 153 LARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNvVT 231
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LT 235
|
....*....
gi 2035452788 232 AEHMSRLYG 240
Cdd:COG3638 236 DAVLREIYG 244
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-219 |
3.59e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 155.70 E-value: 3.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGT-VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:cd03225 3 KNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 -SHTAAFPYSVRRMIELGrVPHTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLL 166
Cdd:cd03225 83 nPDDQFFGPTVEEEVAFG-LENLGLP---EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 167 DEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGH 219
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
20-239 |
7.96e-47 |
|
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: 156.17 E-value: 7.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQLAYVPQSHtaAFPY--SV 97
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQIGVLPDER--GLYDrlTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIELgrvphtgLGSA---LRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:COG4555 92 RENIRY-------FAELyglFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 175 YGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLY 239
Cdd:COG4555 165 VMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-247 |
5.65e-46 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 154.76 E-value: 5.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFPYSVRR 99
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQL 179
Cdd:PRK10253 101 LVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 180 RLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSLKQVD 247
Cdd:PRK10253 181 DLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIID 249
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-247 |
6.44e-45 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 151.90 E-value: 6.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILL----GLLKPD----RGHVLLEGKPLGAYSAS 76
Cdd:PRK13547 1 MLTADHLHVARRHR-AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltGGGAPRgarvTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 77 SVAQQLAYVPQSHTAAFPYSVRRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARA 156
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 157 LAQ---------EAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLP 226
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
250 260
....*....|....*....|.
gi 2035452788 227 QNVVTAEHMSRLYGVSLKQVD 247
Cdd:PRK13547 240 ADVLTPAHIARCYGFAVRLVD 260
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
13-252 |
1.43e-42 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 145.08 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 13 LRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLkPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAA 92
Cdd:PRK03695 3 LNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 93 FPYSVRRMIELGRVPHTGLgsalrAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQ-------EAKALL 165
Cdd:PRK03695 82 FAMPVFQYLTLHQPDKTRT-----EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSLKQ 245
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRR 236
|
....*..
gi 2035452788 246 VDHEGSR 252
Cdd:PRK03695 237 LDVEGHP 243
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-215 |
1.90e-42 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 143.14 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGkplgaysassvAQQLAYVPQ--SHTAAFPYSV 97
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrsEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH 177
Cdd:NF040873 75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 2035452788 178 QLRLMSLLGEFAAEGRLILLTSHRPEELfAPASRVLVL 215
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-220 |
7.33e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.26 E-value: 7.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYV 85
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQsHTAAFPYSVRRMIELGrvphtgLGSALRAEDHAAVDHAMARLGLQE-MAERPVTQLSGGERQRVVLARALAQEAKAL 164
Cdd:COG4619 80 PQ-EPALWGGTVRDNLPFP------FQLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHI 220
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-229 |
3.77e-41 |
|
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: 147.74 E-value: 3.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRG----TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSV-- 78
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 79 -AQQLAYVPQSHTAAF--PYSVRRMIELGRVPHTGLGsalRAEDHAAVDHAMARLGLQ-EMAERPVTQLSGGERQRVVLA 154
Cdd:COG1123 340 lRRRVQMVFQDPYSSLnpRMTVGDIIAEPLRLHGLLS---RAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 155 RALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-231 |
4.82e-41 |
|
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: 141.04 E-value: 4.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGsrG-TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LA 83
Cdd:cd03219 1 LEVRGLTKRFG--GlVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 84 YVPQsHTAAFP-YSVRRMIELGRVPHTGLGSAL------RAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARA 156
Cdd:cd03219 79 RTFQ-IPRLFPeLTVLENVMVAAQARTGSGLLLararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 157 LAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVT 231
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-250 |
1.66e-40 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 140.31 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFPYSVRR 99
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRVP-HTGLGSaLRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:PRK10575 105 LVAIGRYPwHGALGR-FGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLV-LDDGHIVADGLPQNVVTAEHMSRLYGVSLKQVDHEG 250
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVaLRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPA 256
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-217 |
1.99e-40 |
|
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: 138.38 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAySASSVAQQLAY 84
Cdd:COG4133 2 MLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQsHTAAFPY-SVRRMIELgrvpHTGLGSalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKA 163
Cdd:COG4133 80 LGH-ADGLKPElTVRENLRF----WAALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 164 LLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELfaPASRVLVLDD 217
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-239 |
3.25e-40 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 138.85 E-value: 3.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS---SVAQQL 82
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYVPQSHTAAFPYSVRRMIELGRVPHTGLGSALR----AEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALA 158
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 159 QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNvVTAEHMSR 237
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDE 239
|
..
gi 2035452788 238 LY 239
Cdd:cd03256 240 IY 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-220 |
4.42e-40 |
|
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: 136.37 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAsSVAQQLAYV 85
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQshtaafpysvrrmielgrvpHTGLGSALRAEDHAavdhamarlglqemaerpvtQLSGGERQRVVLARALAQEAKALL 165
Cdd:cd03230 79 PE--------------------EPSLYENLTVRENL--------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHI 220
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-227 |
1.47e-39 |
|
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: 144.13 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYV 85
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQsHTAAFPYSVRRMIELGRvphtglgsalRAEDHAAVDHAMARLGLQEMAER-------PV----TQLSGGERQRVVLA 154
Cdd:COG4988 417 PQ-NPYLFAGTIRENLRLGR----------PDASDEELEAALEAAGLDEFVAAlpdgldtPLgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 155 RALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEfAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADGLPQ 227
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHE 556
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-229 |
1.66e-39 |
|
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: 137.48 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LA 83
Cdd:COG0411 4 LLEVRGLTKRFGGL-VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 84 YVPQsHTAAFP-YSVRRMIELGRVPHTGLG--------SALRAEDHAAVDHAMA---RLGLQEMAERPVTQLSGGERQRV 151
Cdd:COG0411 83 RTFQ-NPRLFPeLTVLENVLVAAHARLGRGllaallrlPRARREEREARERAEElleRVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 152 VLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-220 |
8.20e-39 |
|
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: 134.54 E-value: 8.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGT---VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYS----ASSV 78
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 79 AQQLAYVPQSHTAaFPY-SVRRMIELGRVphtgLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARAL 157
Cdd:cd03255 81 RRHIGFVFQSFNL-LPDlTALENVELPLL----LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 158 AQEAKALLLDEPmTG-LDYGHQLRLMSLLGEFAAE-GRLILLTSHRPeELFAPASRVLVLDDGHI 220
Cdd:cd03255 156 ANDPKIILADEP-TGnLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-221 |
8.64e-39 |
|
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: 134.31 E-value: 8.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAqqlAYVPQ- 87
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI---GYVMQd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 SHTAAFPYSVRRmiELGrvphtgLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLD 167
Cdd:cd03226 80 VDYQLFTDSVRE--ELL------LGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 168 EPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-224 |
1.22e-38 |
|
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: 133.80 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSrGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaysASSVAQQ--LAYVP 86
Cdd:cd03259 4 KGLSKTYGS-VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERrnIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 87 QSHtAAFPY-SVRRMI----ELGRVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:cd03259 79 QDY-ALFPHlTVAENIafglKLRGVP--------KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGE-FAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-229 |
2.37e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.82 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaYSASSVAQ-QLAYVPQsHTAAFPY-SV 97
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRErRVGFVFQ-HYALFPHmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIELG-RVPHTGlgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:COG1118 93 AENIAFGlRVRPPS-----KAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 177 --HQLR--LMSLLGEFaaeGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:COG1118 168 vrKELRrwLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-232 |
1.26e-37 |
|
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: 138.11 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 3 ADLLACEGVCLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPD---RGHVLLEGKPLGAYSASSV 78
Cdd:COG1123 2 TPLLEVRDLSVRyPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 79 AQQLAYVPQSHTAAF-PYSVRRMIELGRVphtgLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARAL 157
Cdd:COG1123 82 GRRIGMVFQDPMTQLnPVTVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 158 AQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTA 232
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
1.32e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 135.23 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaysASSVAQ 80
Cdd:COG3842 1 MAMPALELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 81 Q--LAYVPQSHtAAFPY-SVRRMIELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVL 153
Cdd:COG3842 76 KrnVGMVFQDY-ALFPHlTVAENVAFGlrmrGVP--------KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 154 ARALAQEAKALLLDEPMTGLDYghQLR------LMSLLGEFaaeGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQ 227
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDA--KLReemreeLRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPE 221
|
..
gi 2035452788 228 NV 229
Cdd:COG3842 222 EI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-223 |
1.38e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.70 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNAdLLACEGVCLRRGSRG---TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASS 77
Cdd:COG1136 1 MSP-LLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 78 VA----QQLAYVPQSHTaAFPY-SVRRMIELGRVphtgLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVV 152
Cdd:COG1136 80 LArlrrRHIGFVFQFFN-LLPElTALENVALPLL----LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 153 LARALAQEAKALLLDEPmTG-LDYGHQLRLMSLLGEFAAE-GRLILLTSHRPeELFAPASRVLVLDDGHIVAD 223
Cdd:COG1136 155 IARALVNRPKLILADEP-TGnLDSKTGEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDGRIVSD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-219 |
2.29e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 128.90 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQs 88
Cdd:cd00267 3 ENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 89 htaafpysvrrmielgrvphtglgsalraedhaavdhamarlglqemaerpvtqLSGGERQRVVLARALAQEAKALLLDE 168
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 169 PMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGH 219
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-224 |
9.21e-37 |
|
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: 130.31 E-value: 9.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRG---TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ 81
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 82 LAYVPQSHTAAF-P-YSVRRMIElgrvphTGLGSALRAEDHAAVDHAMARLGL-QEMAERPVTQLSGGERQRVVLARALA 158
Cdd:COG1124 81 VQMVFQDPYASLhPrHTVDRILA------EPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 159 QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLtYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-233 |
3.34e-36 |
|
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: 135.73 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGT-VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAY 84
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQsHTAAFPYSVRRMIELGRvPHTGLGSALRAEDHAAVDHAMARL--GLQ-EMAERpVTQLSGGERQRVVLARALAQEA 161
Cdd:COG2274 554 VLQ-DVFLFSGTIRENITLGD-PDATDEEIIEAARLAGLHDFIEALpmGYDtVVGEG-GSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGEFAAeGRLILLTSHRPeELFAPASRVLVLDDGHIVADGLPQNVVTAE 233
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-224 |
3.50e-36 |
|
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: 127.71 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQsHTAAFPYSVRRM 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ-DVTLFYGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRVPHTGlGSALRAEDHAAVDHAMARL--GLQ-EMAERPVtQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH 177
Cdd:cd03245 98 ITLGAPLADD-ERILRAAELAGVTDFVNKHpnGLDlQIGERGR-GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2035452788 178 QLRLMSLLGEFAAEGRLILLTsHRPeELFAPASRVLVLDDGHIVADG 224
Cdd:cd03245 176 EERLKERLRQLLGDKTLIIIT-HRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
6.92e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 128.28 E-value: 6.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLR---RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAss 77
Cdd:COG1116 3 AAAPALELRGVSKRfptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 78 vaqQLAYVPQSHtAAFPY-SVRRMIELGrVPHTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARA 156
Cdd:COG1116 81 ---DRGVVFQEP-ALLPWlTVLDNVALG-LELRGVP---KAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 157 LAQEAKALLLDEPMTGLDYGHQLRLMSLLGE-FAAEGRLILLTSHRPEELFAPASRVLVLDD--GHIVAD 223
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-224 |
9.11e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.18 E-value: 9.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 26 SVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASsvAQQLAYVPQSHTAaFPY-SVRRMIELG 104
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSMLFQENNL-FPHlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 105 RvpHTGLgsALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGhqLR--LM 182
Cdd:COG3840 96 L--RPGL--KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA--LRqeML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2035452788 183 SLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:COG3840 170 DLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADG 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-251 |
1.11e-35 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 128.08 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGaysaSSVAQQL-AYVPQSHTA--AFPYS 96
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLvAYVPQSEEVdwSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK15056 97 VEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 177 HQLRLMSLLGEFAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSLKQVDHEGS 251
Cdd:PRK15056 177 TEARIISLLRELRDEGKTMLVSTHNLGSV-TEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVLRHVALNGS 250
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-224 |
1.78e-35 |
|
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: 125.77 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGsRGTVLDNVSVSLRAGeLVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSaSSVAQQLAYV 85
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQSHTAAFPYSVRRMIE----LGRVPHTglgsalraEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLDyiawLKGIPSK--------EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGEfAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-240 |
2.67e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 126.26 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS---SVAQQLAYVPQSHTAAFPYS 96
Cdd:TIGR02315 16 QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrKLRRRIGMIFQHYNLIERLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGRVPHTG-----LGSALRAEDHAAVDhAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:TIGR02315 96 VLENVLHGRLGYKPtwrslLGRFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPqNVVTAEHMSRLYG 240
Cdd:TIGR02315 175 SLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP-SELDDEVLRHIYG 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-224 |
3.80e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.16 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA---QQLAYV 85
Cdd:COG2884 5 ENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQSH------TA----AFPysvrrMIELGRvphtglgsaLRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLAR 155
Cdd:COG2884 85 FQDFrllpdrTVyenvALP-----LRVTGK---------SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 156 ALAQEAKALLLDEPmTG-LDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:COG2884 151 ALVNRPELLLADEP-TGnLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-169 |
1.50e-34 |
|
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: 121.60 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQsHTAAFP-YSVRRM 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQ-DPQLFPrLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 101 IELGRVphtgLGSALRAEDHAAVDHAMARLGLQEMAERPV----TQLSGGERQRVVLARALAQEAKALLLDEP 169
Cdd:pfam00005 80 LRLGLL----LKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-239 |
2.07e-34 |
|
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: 123.42 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LAY 84
Cdd:cd03218 1 LRAENLSKRYGKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQSHTAAFPYSVRRMI----ELGRVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENIlavlEIRGLS--------KKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 161 AKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLY 239
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-228 |
2.30e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 129.89 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAY 84
Cdd:COG4987 334 LELEDVSFRyPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQsHTAAFPYSVRRMIELGRvphtglgsaLRAEDHAAVDhAMARLGLQEMAER-------PV----TQLSGGERQRVVL 153
Cdd:COG4987 414 VPQ-RPHLFDTTLRENLRLAR---------PDATDEELWA-ALERVGLGDWLAAlpdgldtWLgeggRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 154 ARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEfAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADGLPQN 228
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEE 555
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-223 |
6.88e-34 |
|
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: 121.81 E-value: 6.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRG---TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaysaSSVAQQL 82
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYVPQSHtAAFPY-SVRRMIELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARAL 157
Cdd:cd03293 76 GYVFQQD-ALLPWlTVLDNVALGlelqGVP--------KAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 158 AQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLD--DGHIVAD 223
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKtVLLVTHDIDEAVFLADRVVVLSarPGRIVAE 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-224 |
1.02e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 121.25 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 32 GELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSA----SSVAQQLAYVPQSHtAAFPY-SVRRMIELGrv 106
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKkinlPPQQRKIGLVFQQY-ALFPHlNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 107 phtgLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLG 186
Cdd:cd03297 100 ----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2035452788 187 EFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03297 176 QIKKNLNIpVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-224 |
2.22e-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: 120.46 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAysasSVAQQLAYVPQSHTAAFPYSVR- 98
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEERGLYPKMKVId 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELGRVphTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:cd03269 90 QLVYLAQL--KGLK---KEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03269 165 ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-223 |
2.60e-33 |
|
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: 118.69 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSrGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGaysassvaqqlayv 85
Cdd:cd03216 1 LELRGITKRFGG-VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 pqshtaafPYSVRRMIELGrvphtglgsalraedhaavdhamarLGLqemaerpVTQLSGGERQRVVLARALAQEAKALL 165
Cdd:cd03216 66 --------FASPRDARRAG-------------------------IAM-------VYQLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVAD 223
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-219 |
3.54e-33 |
|
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: 118.64 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGT-VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:cd03228 4 KNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 sHTAAFPYSVRRMIelgrvphtglgsalraedhaavdhamarlglqemaerpvtqLSGGERQRVVLARALAQEAKALLLD 167
Cdd:cd03228 84 -DPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 168 EPMTGLDYGHQLRLMSLLGEFaAEGRLILLTSHRPEELFApASRVLVLDDGH 219
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-229 |
4.00e-33 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 120.52 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 13 LRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSvaQQLAYVPQSHtAA 92
Cdd:cd03299 6 LSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNY-AL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 93 FPY-SVRRMIELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLD 167
Cdd:cd03299 83 FPHmTVYKNIAYGlkkrKVD--------KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 168 EPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVtVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-224 |
1.51e-32 |
|
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: 118.76 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 14 RRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA---QQLAYVPQSHT 90
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrKEIQMVFQDPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 AAFP--YSVRRMIELGRVPHTGLGSALRAEdhAAVDHAMARLGL-QEMAERPVTQLSGGERQRVVLARALAQEAKALLLD 167
Cdd:cd03257 93 SSLNprMTIGEQIAEPLRIHGKLSKKEARK--EAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 168 EPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03257 171 EPTSALDVSVQAQILDLLKKLQEELGLtLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-224 |
1.81e-32 |
|
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: 117.98 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 26 SVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAysASSVAQQLAYVPQSHTAAFPYSVRRMIELGR 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 106 VPhtglGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLL 185
Cdd:cd03298 96 SP----GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2035452788 186 GEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03298 172 LDLHAETKMtVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-224 |
6.21e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.05 E-value: 6.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQL--AYVPQsHTAAFPY-S 96
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQAAgiAIIHQ-ELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGRVPHTGlGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:COG1129 96 VAENIFLGREPRRG-GLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 177 HQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:COG1129 175 EVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-251 |
2.72e-31 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 118.28 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 11 VCLRRGsrGTVLDnVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaYSASSV------AQQLAY 84
Cdd:COG4148 7 FRLRRG--GFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGiflpphRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQSHtAAFP-YSVRRMIELG--RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:COG4148 82 VFQEA-RLFPhLSVRGNLLYGrkRAP--------RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVvtaehMSRLYG 240
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV-----LSRPDL 227
|
250
....*....|.
gi 2035452788 241 VSLKQVDHEGS 251
Cdd:COG4148 228 LPLAGGEEAGS 238
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-224 |
5.82e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.36 E-value: 5.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGA---------------YSASSVAQQLAY 84
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigylpeerglYPKMKVGEQLVY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 vpqshtaafpysvrrmieLGRVphTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKAL 164
Cdd:COG4152 95 ------------------LARL--KGLS---KAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHR---PEELfapASRVLVLDDGHIVADG 224
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmelVEEL---CDRIVIINKGRKVLSG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-234 |
1.37e-30 |
|
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: 113.92 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS---S 77
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 78 VAQQLAYVPQShTA-----------AFPysvrrMIElgrvpHTGLGSALRAEdhaAVDHAMARLGLQEMAERPVTQLSGG 146
Cdd:COG1127 80 LRRRIGMLFQG-GAlfdsltvfenvAFP-----LRE-----HTDLSEAEIRE---LVLEKLELVGLPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 147 ERQRVVLARALAQEAKALLLDEPMTGLDyghqlRLMSllGEFAaegRLIL-------LTS----HRPEELFAPASRVLVL 215
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLD-----PITS--AVID---ELIRelrdelgLTSvvvtHDLDSAFAIADRVAVL 215
|
250
....*....|....*....
gi 2035452788 216 DDGHIVADGLPQNVVTAEH 234
Cdd:COG1127 216 ADGKIIAEGTPEELLASDD 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-234 |
1.49e-30 |
|
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: 113.75 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 8 CEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS---SVAQQLAY 84
Cdd:cd03261 3 LRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQShTAAF-PYSVRRMIELGRVPHTGLGSALRAEdhaAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKA 163
Cdd:cd03261 82 LFQS-GALFdSLTVFENVAFPLREHTRLSEEEIRE---IVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 164 LLLDEPMTGLD---YGHQLRLMSLLGEfaAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEH 234
Cdd:cd03261 158 LLYDEPTAGLDpiaSGVIDDLIRSLKK--ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-229 |
1.82e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.94 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaySASSVAQ-QLAYVPQ 87
Cdd:COG3839 7 ENVSKSYGGV-EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDrNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 SHtAAFP-YSVRRMIELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAK 162
Cdd:COG3839 83 SY-ALYPhMTVYENIAFPlklrKVP--------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 163 ALLLDEPMTGLDYghQLRlMSLLGEFAaegRL-------ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:COG3839 154 VFLLDEPLSNLDA--KLR-VEMRAEIK---RLhrrlgttTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-233 |
8.27e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 8.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 17 SRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYS-ASSVAQQLAYVPQS--HTAAF 93
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPEDrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 PY-SVRRMIELGRVPHTGLGSAL-RAEDHAAVDHAMARLGLQeMA--ERPVTQLSGGERQRVVLARALAQEAKALLLDEP 169
Cdd:COG1129 343 LDlSIRENITLASLDRLSRGGLLdRRRERALAEEYIKRLRIK-TPspEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 170 MTGLDYG-----HQlrlmsLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADgLPQNVVTAE 233
Cdd:COG1129 422 TRGIDVGakaeiYR-----LIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGE-LDREEATEE 484
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-220 |
2.12e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 109.06 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 17 SRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS-SVAQQLAYVPQ--SHTAAF 93
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdAIRAGIAYVPEdrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 P-YSVRRMIELGRvphtglgsalraedhaavdhamarlglqemaerpvtQLSGGERQRVVLARALAQEAKALLLDEPMTG 172
Cdd:cd03215 91 LdLSVAENIALSS------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 173 LDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHI 220
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-229 |
2.20e-29 |
|
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: 110.22 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LAYVPQSHtAAFPY-SVR 98
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGR-RIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELGRVPHTglgsalRAEDHAAVDHAMARL-GLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH 177
Cdd:cd03224 94 ENLLLGAYARR------RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 178 QLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:cd03224 168 VEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-239 |
2.49e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.50 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LAY 84
Cdd:COG1137 4 LEAENLVKSYGKR-TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQSHtaafpySV-RRM---------IELGRVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLA 154
Cdd:COG1137 83 LPQEA------SIfRKLtvednilavLELRKLS--------KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 155 RALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEH 234
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
....*
gi 2035452788 235 MSRLY 239
Cdd:COG1137 229 VRKVY 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-229 |
2.53e-29 |
|
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: 110.40 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSrGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKP---LGAYSassvaQQLAYV 85
Cdd:cd03300 4 ENVSKFYGG-FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHK-----RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQSHtAAFPY-SVRRMIELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQE 160
Cdd:cd03300 78 FQNY-ALFPHlTVFENIAFGlrlkKLP--------KAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 161 AKALLLDEPMTGLDY----GHQLRLMSLLGEFaaeGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:cd03300 149 PKVLLLDEPLGALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-239 |
3.02e-29 |
|
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: 110.44 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LAY 84
Cdd:TIGR04406 2 LVAENLIKSYKKR-KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQSHTAAFPYSVRRMIELGRVPHTGLGSALRAEDhaaVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKAL 164
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDRAEREER---LEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLY 239
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-239 |
3.21e-29 |
|
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: 110.07 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGsRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LA 83
Cdd:COG0410 3 MLEVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 84 YVPQSHtAAFPY-SVRRMIELGRVPHTGlgsalRAEDHAAVDHAMARL-GLQEMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:COG0410 82 YVPEGR-RIFPSlTVEENLLLGAYARRD-----RAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 162 KALLLDEPMTGL-----DyghqlRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMS 236
Cdd:COG0410 156 KLLLLDEPSLGLaplivE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
...
gi 2035452788 237 RLY 239
Cdd:COG0410 231 EAY 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-227 |
3.24e-29 |
|
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: 109.52 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQLAYVPQsHTAAFPY-SVR 98
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQ-FDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELgrvpHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDygHQ 178
Cdd:cd03263 94 EHLRF----YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD--PA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 179 LR--LMSLLgEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQ 227
Cdd:cd03263 168 SRraIWDLI-LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-224 |
3.39e-29 |
|
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: 109.76 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQLAYVPQShTAAFPY-SVRR 99
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDS-TGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELgrvpHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQL 179
Cdd:cd03266 98 NLEY----FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2035452788 180 RLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03266 174 ALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-229 |
3.42e-29 |
|
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: 110.12 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGsRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSvaQQLAYVPQs 88
Cdd:cd03296 6 RNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 89 HTAAFPY-SVRRMIELG-RVPHTGLGSAlRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLL 166
Cdd:cd03296 82 HYALFRHmTVFDNVAFGlRVKPRSERPP-EAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 167 DEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-219 |
4.19e-29 |
|
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: 108.04 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA--QQLAYVPQSHtAAFPY-S 96
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGMVFQDF-ALFPHlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGrvphtglgsalraedhaavdhamarlglqemaerpvtqLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:cd03229 93 VLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2035452788 177 HQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGH 219
Cdd:cd03229 135 TRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-234 |
6.87e-29 |
|
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: 109.31 E-value: 6.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQS 88
Cdd:cd03295 4 ENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 89 hTAAFPY-SVRRMIELgrVPHtgLGSALRAEDHAAVDHAMARLGL--QEMAERPVTQLSGGERQRVVLARALAQEAKALL 165
Cdd:cd03295 84 -IGLFPHmTVEENIAL--VPK--LLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEH 234
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-222 |
9.84e-29 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 113.47 E-value: 9.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPL-----GAYSASSVA---QQLAYVPQshtaaf 93
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfastTAALAAGVAiiyQELHLVPE------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 pYSVRRMIELGRVPHTGlGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:PRK11288 94 -MTVAENLYLGQLPHKG-GIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2035452788 174 DYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVA 222
Cdd:PRK11288 172 SAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-215 |
1.72e-28 |
|
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: 113.15 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYV 85
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQsHTAAFPYSVRRMIELGRvphtglgsalRAEDHAAVDHAMARLGLQEM-AERPV----------TQLSGGERQRVVLA 154
Cdd:TIGR02857 402 PQ-HPFLFAGTIAENIRLAR----------PDASDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 155 RALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFaAEGRLILLTSHRPeELFAPASRVLVL 215
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-229 |
4.56e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.04 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASsvAQQLAYVPQSHtAAFPY-SVR 98
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSY-ALFPHmTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELG----RVPHtglgsalrAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK09452 105 ENVAFGlrmqKTPA--------AEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 175 YghQLRL-MSLlgEFAAEGRLILLT----SHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK09452 177 Y--KLRKqMQN--ELKALQRKLGITfvfvTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-222 |
8.23e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.26 E-value: 8.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSvaqqlAYVPQSHtAAFPY-SVRR 99
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-----GVVFQKD-ALLPWlNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:COG4525 96 NVAFGlrlrGVP--------KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2035452788 176 GHQLRLMSLLGE-FAAEGRLILLTSHRPEELFAPASRVLVLDD--GHIVA 222
Cdd:COG4525 168 LTREQMQELLLDvWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVE 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
22-256 |
9.59e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 107.86 E-value: 9.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQLAYVPQSHTAAFPYSVRRMI 101
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV-VREPRKVRRSIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 ELgrvpHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRL 181
Cdd:TIGR01188 88 EM----MGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 182 MSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV---VTAEHMsRLYGVSLKQVDHEGSRFFTM 256
Cdd:TIGR01188 164 WDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELkrrLGKDTL-ESRPRDIQSLKVEVSMLIAE 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-221 |
1.00e-27 |
|
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: 105.82 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKST---LLRILLGLLKPDRGHVLLEGKPLgaySASSVAQQLAYVPQSHTAAFPYSV 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 R---RMIELGRVPHTGLGSALRAEDhaaVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:cd03234 99 RetlTYTAILRLPRKSSDAIRKKRV---EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 175 YGHQLRLMSLLGEFAAEGRLILLTSHRP-EELFAPASRVLVLDDGHIV 221
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPrSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-231 |
1.05e-27 |
|
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: 106.96 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 24 NVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSV----AQQLAYVPQsHTAAFPY-SVR 98
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQ-SFALLPHrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELG-RVPHTGlgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD--- 174
Cdd:cd03294 121 ENVAFGlEVQGVP-----RAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpli 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 175 -YGHQLRLMSLLGEFaaeGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVT 231
Cdd:cd03294 196 rREMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-233 |
2.08e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.20 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAySASSVAQ 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 81 QLAYVPQSHTAAFPYSVRR-MIELGRvpHTGLGSalrAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQ 159
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVREnLLVFGR--YFGLSA---AAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 160 EAKALLLDEPMTGLD--YGHQL--RLMSLLgefaAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAE 233
Cdd:PRK13537 156 DPDVLVLDEPTTGLDpqARHLMweRLRSLL----ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-248 |
2.20e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASS---VAQQLAYVPQ-SHTAAFPYS 96
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSlleVRKTVGIVFQnPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGRVpHTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK13639 96 VEEDVAFGPL-NLGLS---KEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 177 HQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSLKQVDH 248
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRLPRVAH 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-220 |
2.39e-27 |
|
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: 103.45 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGT-VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAY 84
Cdd:cd03246 1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQSHTaAFPYSVRRMIelgrvphtglgsalraedhaavdhamarlglqemaerpvtqLSGGERQRVVLARALAQEAKAL 164
Cdd:cd03246 81 LPQDDE-LFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELfAPASRVLVLDDGHI 220
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-224 |
4.67e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 103.84 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 19 GTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplGAYSASSVAQQLAYVPQSHtAAFPYsvr 98
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAP-GFYPN--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 rmieLGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD-YG- 176
Cdd:cd03268 87 ----LTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpDGi 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 177 HQLRlmSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03268 163 KELR--ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-230 |
5.34e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.45 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAySASSVAQQLAYVPQSHTAAFPYSVRR- 99
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEFTVREn 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRVphtgLGSALRaEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD-YGHQ 178
Cdd:PRK13536 135 LLVFGRY----FGMSTR-EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDpHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 179 L---RLMSLLgefaAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVV 230
Cdd:PRK13536 210 LiweRLRSLL----ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-239 |
7.27e-27 |
|
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: 104.11 E-value: 7.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:cd03252 4 EHVRFRyKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 SHTaAFPYSVRRMIELGRVP---HTGLGSALRAEDHAAVdhAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKAL 164
Cdd:cd03252 84 ENV-LFNRSIRDNIALADPGmsmERVIEAAKLAGAHDFI--SELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAeGRLILLTSHRPEELFApASRVLVLDDGHIVADGLPQNVVTAEHM-SRLY 239
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLyAYLY 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-248 |
1.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.54 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGaYSASSVA- 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 80 --QQLAYVPQS-HTAAFPYSVRRMIELGRVpHTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARA 156
Cdd:PRK13636 80 lrESVGMVFQDpDNQLFSASVYQDVSFGAV-NLKLP---EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 157 LAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHM 235
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
250
....*....|...
gi 2035452788 236 SRLYGVSLKQVDH 248
Cdd:PRK13636 236 LRKVNLRLPRIGH 248
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-224 |
1.20e-26 |
|
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: 101.62 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASsVAQQLAYVPQShtaAFPYSVRR 99
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVLNQR---PYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRvphtglgsalraedhaavdhamarlglqemaerpvtQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQL 179
Cdd:cd03247 92 RNNLGR------------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2035452788 180 RLMSLLGEFaAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:cd03247 136 QLLSLIFEV-LKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-224 |
1.26e-26 |
|
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: 103.04 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 15 RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSV---AQQLAYVPQ---- 87
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQhfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 --SHTA----AFPysvrrmIELGRVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:cd03258 94 lsSRTVfenvALP------LEIAGVP--------KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLtIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-223 |
1.35e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 104.00 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 13 LRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAssvAQQLAY------VP 86
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR---AQRKAFrrdiqmVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 87 QSHTAAF--PYSVRRMIelgRVPHTGLGSALRAEDHAAVDHAMARLGLQ-EMAERPVTQLSGGERQRVVLARALAQEAKA 163
Cdd:PRK10419 96 QDSISAVnpRKTVREII---REPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 164 LLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSH--RPEELFapASRVLVLDDGHIVAD 223
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHdlRLVERF--CQRVMVMDNGQIVET 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-233 |
1.36e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.12 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 26 SVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPlgaYSASSVAQQ-LAYVPQSHTAaFPY-SVRRMIEL 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSRRpVSMLFQENNL-FSHlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 104 GRVPhtglGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMS 183
Cdd:PRK10771 95 GLNP----GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 184 LLGEFAAEGRLILL-TSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAE 233
Cdd:PRK10771 171 LVSQVCQERQLTLLmVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
21-200 |
1.47e-26 |
|
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: 102.12 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGaYSASS---VAQQLAYVPQS-HTAAFPYS 96
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGlleRRQRVGLVFQDpDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGRVpHTGLGSAlraEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:TIGR01166 86 VDQDVAFGPL-NLGLSEA---EVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....
gi 2035452788 177 HQLRLMSLLGEFAAEGRLILLTSH 200
Cdd:TIGR01166 162 GREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-228 |
1.67e-26 |
|
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: 102.45 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGkplgaYSASS----VAQQLAYVPQSHTAAFPY 95
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-----HDVVRepreVRRRIGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIEL-GRVphTGLGSALRAEdhaAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:cd03265 89 TGWENLYIhARL--YGVPGAERRE---RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 175 YGHQLRLMSLLGEF-AAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQN 228
Cdd:cd03265 164 PQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-228 |
2.42e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.19 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSrGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaySASSVAQ 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 81 Q-LAYVPQSHtAAFPY-SVRRMIELGrVPHTGLGSALRAEdhaAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALA 158
Cdd:PRK11432 78 RdICMVFQSY-ALFPHmSLGENVGYG-LKMLGVPKEERKQ---RVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 159 QEAKALLLDEPMTGLDygHQLR------LMSLLGEFaaeGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQN 228
Cdd:PRK11432 153 LKPKVLLFDEPLSNLD--ANLRrsmrekIRELQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-229 |
1.39e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.45 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS--SVAQQL 82
Cdd:COG1126 1 MIEIENLHKSFGDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYVPQSHtAAFP-YSVRRMIELGRVPHTGLGsalRAEdhaAVDHAMA---RLGLQEMAERPVTQLSGGERQRVVLARALA 158
Cdd:COG1126 80 GMVFQQF-NLFPhLTVLENVTLAPIKVKKMS---KAE---AEERAMElleRVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 159 QEAKALLLDEPMTGLD---YGHQLRLMSLLgefAAEGRLILLTSHrpeEL-FAP--ASRVLVLDDGHIVADGLPQNV 229
Cdd:COG1126 153 MEPKVMLFDEPTSALDpelVGEVLDVMRDL---AKEGMTMVVVTH---EMgFARevADRVVFMDGGRIVEEGPPEEF 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-221 |
1.46e-25 |
|
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: 101.42 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 10 GVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAY---SASSVAQQLAYVP 86
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 87 QSHTAAF--PYSVRRMIelgRVPHTGLGSALRAEDHAAVDHAMARLGLQ-EMAERPVTQLSGGERQRVVLARALAQEAKA 163
Cdd:TIGR02769 95 QDSPSAVnpRMTVRQII---GEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 164 LLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-229 |
1.55e-25 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 104.83 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 16 GSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPY 95
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQD-VELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVR----RMIElgrvphtglgsalrAEDHAAVDHAMArLGLQEMAER-------PV----TQLSGGERQRVVLARALAQE 160
Cdd:COG4618 421 TIAeniaRFGD--------------ADPEKVVAAAKL-AGVHEMILRlpdgydtRIgeggARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 161 AKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPeELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-229 |
1.96e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGkplgaysassvaQQLAYVP----------QSHt 90
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG------------VDLSHVPpyqrpinmmfQSY- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 AAFPY-SVRRMIELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALL 165
Cdd:PRK11607 101 ALFPHmTVEQNIAFGlkqdKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 166 LDEPMTGLDYG----HQLRLMSLLGEFaaeGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK11607 173 LDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-224 |
3.14e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 104.09 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQs 88
Cdd:COG1132 343 ENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 89 HTAAFPYSVRRMIELGRVPHT--GLGSALRAedhAAVDHAMARL--GLQEM-AERPVTqLSGGERQRVVLARALAQEAKA 163
Cdd:COG1132 422 DTFLFSGTIRENIRYGRPDATdeEVEEAAKA---AQAHEFIEALpdGYDTVvGERGVN-LSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 164 LLLDEPMTGLDYGHQLRLMSLLGEFAAeGRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQG 556
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-220 |
4.16e-25 |
|
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: 99.08 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTaAFPYSVRRM 100
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPV-LFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELgrvphtGLGSALRAEDHAAVDHAMARLGLQEMAERPVT-------QLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:cd03248 108 IAY------GLQSCSFECVKEAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2035452788 174 DYGHQLRLMSLLGEfAAEGRLILLTSHRPeELFAPASRVLVLDDGHI 220
Cdd:cd03248 182 DAESEQQVQQALYD-WPERRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-238 |
4.26e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQL--AYVPQsHtaaF----PY 95
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDAIALgiGMVHQ-H---FmlvpNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELGRVPHTGLGSALRAEdHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLDRKAA-RARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 176 GHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNvVTAEHMSRL 238
Cdd:COG3845 175 QEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE-TSEEELAEL 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-227 |
5.10e-25 |
|
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: 98.84 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRRM 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQD-TFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRvPHTGLGSALRAEDHAAVDHAMARL--GLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:cd03254 97 IRLGR-PNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2035452788 179 LRLMSLLGEFaAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADGLPQ 227
Cdd:cd03254 176 KLIQEALEKL-MKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHD 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-174 |
5.64e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 2 NADLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ 81
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 82 LAYVPQSHT---------AAFPYSVRRmielgrvphtglgsalRAEDHAAVDHAMARLGL-QEMAERPVTQLSGGERQRV 151
Cdd:PRK10247 83 VSYCAQTPTlfgdtvydnLIFPWQIRN----------------QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRI 146
|
170 180
....*....|....*....|...
gi 2035452788 152 VLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALD 169
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-238 |
9.24e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYS---------ASSVAQQLAYVPQShT 90
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvderlirqeAGMVFQQFYLFPHL-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 A----AF-PYSVRRmielgrvphtglgsALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALL 165
Cdd:PRK09493 94 AlenvMFgPLRVRG--------------ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 166 LDEPMTGLD--YGHQ-LRLMSLLGEfaaEGRLILLTSHrpEELFAP--ASRVLVLDDGHIVADGLPQNVVTAEHMSRL 238
Cdd:PRK09493 160 FDEPTSALDpeLRHEvLKVMQDLAE---EGMTMVIVTH--EIGFAEkvASRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-224 |
9.64e-25 |
|
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: 98.02 E-value: 9.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTL-----LRILLGLLKPDRGHVLLEGKPLGA--YSASSVAQQ 81
Cdd:cd03260 4 RDLNVYYGDK-HALKDISLDIPKGEITALIGPSGCGKSTLlrllnRLNDLIPGAPDEGEVLLDGKDIYDldVDVLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 82 LAYVPQsHTAAFPYSVRRMIELGRVPHtglGSALRAEDHAAVDHAMARLGL-QEMAERP-VTQLSGGERQRVVLARALAQ 159
Cdd:cd03260 83 VGMVFQ-KPNPFPGSIYDNVAYGLRLH---GIKLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 160 EAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEgRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-220 |
9.70e-25 |
|
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: 97.60 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGA--YSASSVAQQLAYVPQSHTAaFPY-SV 97
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNL-FPHlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIELGRVphtglgSALRAEDHAAVDHAM---ARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:cd03262 94 LENITLAPI------KVKGMSKAEAEERALellEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 175 ---YGHQLRLMSLLgefAAEGRLILLTSHrpEELFAP--ASRVLVLDDGHI 220
Cdd:cd03262 168 pelVGEVLDVMKDL---AEEGMTMVVVTH--EMGFARevADRVIFMDDGRI 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-229 |
1.39e-24 |
|
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: 98.66 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGkpLGAYSASSVaqqlayvpqshtaafpYSVRRM 100
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENL----------------WEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IelGRV---PHTGLGSALRAEDHA---------------AVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAK 162
Cdd:TIGR04520 79 V--GMVfqnPDNQFVGATVEDDVAfglenlgvpreemrkRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 163 ALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELfAPASRVLVLDDGHIVADGLPQNV 229
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREI 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-224 |
1.43e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 97.79 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFPYSVRR 99
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGR----VPHtglgsalrAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:cd03267 115 SFYLLAaiydLPP--------ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2035452788 176 GHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03267 187 VAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-231 |
2.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSA-SSVAQQLAYVPQSHTAAFpysVRRM 100
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPETQF---VGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IE--LGRVPHTGLGSALraEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:PRK13644 95 VEedLAFGPENLCLPPI--EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPEELFApASRVLVLDDGHIVADGLPQNVVT 231
Cdd:PRK13644 173 IAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
2.84e-24 |
|
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: 97.15 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAqqlayVPQSHtAAFPY-SVRRM 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNY-SLLPWlTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELG--RVPHTglgsALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:TIGR01184 75 IALAvdRVLPD----LSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2035452788 179 LRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDG 218
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVtVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-229 |
3.31e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.77 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGaYSAS---SVAQQLAYVPQSHTAAFPYSv 97
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRgllALRQQVATVFQDPEQQIFYT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 rrMIElgrvphTGLGSALR----AEDHAA--VDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:PRK13638 94 --DID------SDIAFSLRnlgvPEAEITrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-223 |
6.86e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 99.69 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYS--ASSVA------QQLAYVPQshtaaf 93
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpkSSQEAgigiihQELNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 pYSVRRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:PRK10762 94 -LTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2035452788 174 DYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVAD 223
Cdd:PRK10762 173 TDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-221 |
6.86e-24 |
|
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: 95.40 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSvaQQLAYVPQS 88
Cdd:cd03301 4 ENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 89 HtAAFP-YSVRRMIELG-RVPHTGlgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLL 166
Cdd:cd03301 81 Y-ALYPhMTVYDNIAFGlKLRKVP-----KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 167 DEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-238 |
7.55e-24 |
|
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: 98.26 E-value: 7.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 11 VCLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSA----SSVAQQLAYV 85
Cdd:TIGR02142 1 LSARfSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiflPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQSHTAaFP-YSVRRMIELGRVPHTGlgsalrAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKAL 164
Cdd:TIGR02142 81 FQEARL-FPhLSVRGNLRYGMKRARP------SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRL 238
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
22-218 |
8.51e-24 |
|
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: 95.39 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA---QQLAYVPQSH------TA- 91
Cdd:TIGR02673 18 LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllrRRIGVVFQDFrllpdrTVy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 92 ---AFPYSVRRmielgrvphtglgsALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDE 168
Cdd:TIGR02673 98 envALPLEVRG--------------KKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2035452788 169 PMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDG 218
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-224 |
8.87e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.90 E-value: 8.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ-----SHT----- 90
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQrvhlfSATlrdnl 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 --AAFPYSVRRMIE-LGRVphtGLGSALraEDHAAVDHAMARLGlqemaerpvTQLSGGERQRVVLARALAQEAKALLLD 167
Cdd:PRK11160 435 llAAPNASDEALIEvLQQV---GLEKLL--EDDKGLNAWLGEGG---------RQLSGGEQRRLGIARALLHDAPLLLLD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 168 EPMTGLDYGHQLRLMSLLGEFAAEGRLILLTsHRpeeLFAPAS--RVLVLDDGHIVADG 224
Cdd:PRK11160 501 EPTEGLDAETERQILELLAEHAQNKTVLMIT-HR---LTGLEQfdRICVMDNGQIIEQG 555
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-245 |
1.03e-23 |
|
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: 99.41 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGT-VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:TIGR02203 334 RNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 sHTAAFPYSVRRMIELGRvphtgLGSALRAEDHAAVDHAMAR-------LGLQEMAERPVTQLSGGERQRVVLARALAQE 160
Cdd:TIGR02203 414 -DVVLFNDTIANNIAYGR-----TEQADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 161 AKALLLDEPMTGLDYGHQlRLMSLLGEFAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADGLPQNVVTAE-HMSRLY 239
Cdd:TIGR02203 488 APILILDEATSALDNESE-RLVQAALERLMQGRTTLVIAHRLSTI-EKADRIVVMDDGRIVERGTHNELLARNgLYAQLH 565
|
....*.
gi 2035452788 240 GVSLKQ 245
Cdd:TIGR02203 566 NMQFRE 571
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-220 |
1.16e-23 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 94.93 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 26 SVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSvaQQLAYVPQSHTAAFPYSVRRMIELGR 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 106 VPhtglGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLL 185
Cdd:TIGR01277 96 HP----GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 2035452788 186 GEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHI 220
Cdd:TIGR01277 172 KQLCSERQRtLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-231 |
1.53e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS----SVAQQLAYVPQ-SHTAAFPYS 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkKLRKKVSLVFQfPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGrvPHTGLGSALRAEDHAAvdHAMARLGLQE-MAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:PRK13641 103 VLKDVEFG--PKNFGFSEDEAKEKAL--KWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 176 GHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVT 231
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-174 |
2.19e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 8 CEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassvaQQLAYVPQ 87
Cdd:COG0488 1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 SHTAAFPYSVRRMIELGrvpHTGLGSALR-------------------AEDHAAVDHA------------MARLGL-QEM 135
Cdd:COG0488 69 EPPLDDDLTVLDTVLDG---DAELRALEAeleeleaklaepdedlerlAELQEEFEALggweaearaeeiLSGLGFpEED 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 2035452788 136 AERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-239 |
2.37e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.96 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LAYVPQSHTAAFPYSVR 98
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELGRVPHTGLGSALRaEDHAavDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEQR-EDRA--NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLY 239
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-224 |
3.53e-23 |
|
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: 93.00 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 14 RRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKST--LLRILLGLLKPDRGHVLLEGKPLgaySASSVAQQLAYVPQsHTA 91
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQ-DDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 92 AFPY-SVRRMIelgrvphtglgsalraeDHAAvdhamarlGLQemaerpvtQLSGGERQRVVLARALAQEAKALLLDEPM 170
Cdd:cd03213 93 LHPTlTVRETL-----------------MFAA--------KLR--------GLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 171 TGLDYGHQLRLMSLLGEFAAEGRLILLTSHRP-EELFAPASRVLVLDDGHIVADG 224
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-234 |
9.44e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKsTLLRILLGLLKPDR--GHVLLEGKPLGAYS-ASSVAQQLAYVPQSHtaafpysv 97
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGR-TELVQCLFGAYPGRweGEIFIDGKPVKIRNpQQAIAQGIAMVPEDR-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMielGRVPHTGLG-----SALR----------AEDHAAVDHAMARLGLQ-EMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:PRK13549 348 KRD---GIVPVMGVGknitlAALDrftggsriddAAELKTILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGEFAAEG-RLILLTSHRPEELfAPASRVLVLDDGHIVADgLPQNVVTAEH 234
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELPEVL-GLSDRVLVMHEGKLKGD-LINHNLTQEQ 496
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-222 |
9.56e-23 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 92.80 E-value: 9.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVC--LRRGSRGT-VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA-- 79
Cdd:TIGR02211 1 LLKCENLGkrYQEGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 80 --QQLAYVPQSHTAAFPYSVrrmieLGRVPHTGLGSALRAEDHAAVDHAM-ARLGLQEMAERPVTQLSGGERQRVVLARA 156
Cdd:TIGR02211 81 rnKKLGFIYQFHHLLPDFTA-----LENVAMPLLIGKKSVKEAKERAYEMlEKVGLEHRINHRPSELSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 157 LAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPeELFAPASRVLVLDDGHIVA 222
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRElNTSFLVVTHDL-ELAKKLDRVLEMKDGQLFN 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-223 |
9.58e-23 |
|
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: 92.88 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRG---TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYS--- 74
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 75 -ASSVAQQLAYVPQSH------TA----AFPysvrrmIELGRVPHtglgsalrAEDHAAvdHAMARLGLQEMAERPVTQL 143
Cdd:COG4181 84 rARLRARHVGFVFQSFqllptlTAlenvMLP------LELAGRRD--------ARARAR--ALLERVGLGHRLDHYPAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 144 SGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPeELFAPASRVLVLDDGHIVA 222
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDP-ALAARCDRVLRLRAGRLVE 226
|
.
gi 2035452788 223 D 223
Cdd:COG4181 227 D 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-229 |
1.02e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.15 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 18 RGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSvaQQLAYVPQsHTAAFpysv 97
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQ-HYALF---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIELGRVPHtGLGSALRAE--DHAAVDHAMARL----GLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:PRK10851 87 RHMTVFDNIAF-GLTVLPRRErpNAAAIKAKVTQLlemvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAEGRLI-LLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-215 |
1.02e-22 |
|
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: 92.17 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 3 ADLLACEgvclrRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGaYSASSVAQQL 82
Cdd:cd03231 3 ADELTCE-----RDGR-ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-FQRDSIARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYVPQSHTAAFPYSVRRMIELGRVPHtglgsalraeDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAK 162
Cdd:cd03231 76 LYLGHAPGIKTTLSVLENLRFWHADH----------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 163 ALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVL 215
Cdd:cd03231 146 LWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-224 |
1.64e-22 |
|
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: 92.29 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGT-VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:cd03251 4 KNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 ShTAAFPYSVRRMIELGRvphtglgsalRAEDHAAVDHAmARL------------GLQEM-AERPVtQLSGGERQRVVLA 154
Cdd:cd03251 84 D-VFLFNDTVAENIAYGR----------PGATREEVEEA-ARAanahefimelpeGYDTViGERGV-KLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 155 RALAQEAKALLLDEPMTGLDYGHQlRLMSLLGEFAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESE-RLVQAALERLMKNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERG 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-237 |
1.93e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.48 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 3 ADLLACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ- 81
Cdd:COG3845 255 EVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 82 LAYVPQ--SHTAAFP-YSVRRMIELGRVPHTGLGSALRAEDHAAVDHAmarlglQEMAER----------PVTQLSGGER 148
Cdd:COG3845 335 VAYIPEdrLGRGLVPdMSVAENLILGRYRRPPFSRGGFLDRKAIRAFA------EELIEEfdvrtpgpdtPARSLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 149 QRVVLARALAQEAKALLLDEPMTGLDYG-----HQlRLMSLlgefAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVAd 223
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGaiefiHQ-RLLEL----RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVG- 482
|
250
....*....|....
gi 2035452788 224 glpqnVVTAEHMSR 237
Cdd:COG3845 483 -----EVPAAEATR 491
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-232 |
2.02e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 95.66 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKsTLLRILLGLLKPDR--GHVLLEGKPLGAYS-ASSVAQQLAYVPQS---HTAAFPY 95
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGR-TELVQALFGAYPGKfeGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELGRV-PHTGLGSALRAEDHAAVDHAMARLGLQEMA-ERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:TIGR02633 355 GVGKNITLSVLkSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 174 DYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVAD----GLPQNVVTA 232
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDfvnhALTQEQVLA 497
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-220 |
2.68e-22 |
|
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: 91.32 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASsvaqQLAYVPQSHTAAFPYSvrR 99
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR----AIPYLRRKIGVVFQDF--R 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIeLGRVPHTGLGSALRAEDHAA------VDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:cd03292 89 LL-PDRNVYENVAFALEVTGVPPreirkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2035452788 174 DYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHI 220
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-206 |
2.78e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGkplGAYSASSVAQQLAYV 85
Cdd:PRK13539 3 LEGEDLACVRGGR-VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 pqSHTAAF--PYSVRRMIELGRvphtglgsALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKA 163
Cdd:PRK13539 79 --GHRNAMkpALTVAENLEFWA--------AFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2035452788 164 LLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELF 206
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLP 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-229 |
3.72e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 91.71 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 4 DLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassvaQQLA 83
Cdd:PRK09544 3 SLVSLENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-----------LRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 84 YVPQ--SHTAAFPYSVRRMIELgrvpHTGLGSalraedhAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:PRK09544 71 YVPQklYLDTTLPLTVNRFLRL----RPGTKK-------EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLdDGHIVADGLPQNV 229
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVV 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-229 |
8.37e-22 |
|
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: 92.17 E-value: 8.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 37 LLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaySASSVAQQLAYVP---QSHtAAFPY-SVRRMIELG-RVPHTGl 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE-----DVTNVPPHLRHINmvfQSY-ALFPHmTVEENVAFGlKMRKVP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 112 gsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG----HQLRLMSLLGE 187
Cdd:TIGR01187 74 ----RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2035452788 188 FaaeGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:TIGR01187 150 L---GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-216 |
8.87e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 3 ADLLACEgvclrRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAySASSVAQQL 82
Cdd:PRK13538 4 ARNLACE-----RDER-ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYvpqshtaafpysvrrmieLGRvpHTGLGSALRAE-------------DHAAVDHAMARLGLQEMAERPVTQLSGGERQ 149
Cdd:PRK13538 77 LY------------------LGH--QPGIKTELTALenlrfyqrlhgpgDDEALWEALAQVGLAGFEDVPVRQLSAGQQR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 150 RVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLD 216
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRLG 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-246 |
9.88e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.30 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 2 NADLLACEGVCLR-----RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEG--------- 67
Cdd:PRK13633 1 MNEMIKCKNVSYKyesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 68 ------------KPLGAYSASSVAQQLAYVPQShtaafpysvrrmieLGRVPHtglgsalraEDHAAVDHAMARLGLQEM 135
Cdd:PRK13633 81 wdirnkagmvfqNPDNQIVATIVEEDVAFGPEN--------------LGIPPE---------EIRERVDESLKKVGMYEY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 136 AERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELfAPASRVLV 214
Cdd:PRK13633 138 RRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIV 216
|
250 260 270
....*....|....*....|....*....|..
gi 2035452788 215 LDDGHIVADGLPQNVVTAEHMSRLYGVSLKQV 246
Cdd:PRK13633 217 MDSGKVVMEGTPKEIFKEVEMMKKIGLDVPQV 248
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-203 |
1.23e-21 |
|
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: 89.21 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQ----QLAYVPQSHTAAFPY 95
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfrreKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELGRVPHTGLGSalraEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKK----EKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDP 167
|
170 180
....*....|....*....|....*...
gi 2035452788 176 GHQLRLMSLLGEFAAEGRLILLTSHRPE 203
Cdd:TIGR03608 168 KNRDEVLDLLLELNDEGKTIIIVTHDPE 195
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
21-224 |
1.44e-21 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 93.65 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRRM 100
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQE-NVLFSRSIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRvPHTGLGSALRAEDHAAVDHAMARL--GLQ-EMAERPVTqLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH 177
Cdd:TIGR01846 551 IALCN-PGAPFEHVIHAAKLAGAHDFISELpqGYNtEVGEKGAN-LSGGQRQRIAIARALVGNPRILIFDEATSALDYES 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2035452788 178 QLRLMSLLGEFAAeGRLILLTSHRPEELFApASRVLVLDDGHIVADG 224
Cdd:TIGR01846 629 EALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-224 |
1.50e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 89.91 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRRM 100
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRVPHTgLGSALRAEDHAAVDHAMARL--GLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:cd03249 97 IRYGKPDAT-DEEVEEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 179 LRLMSLLGEfAAEGRLILLTSHRpeeLFAP--ASRVLVLDDGHIVADG 224
Cdd:cd03249 176 KLVQEALDR-AMKGRTTIVIAHR---LSTIrnADLIAVLQNGQVVEQG 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-229 |
2.14e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.49 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSA--SSVAQQLAYVPQ-SHTAAFPYSVR 98
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklSDIRKKVGLVFQyPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELGRVpHTGLGsalRAEDHAAVDHAMARLGL--QEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK13637 103 KDIAFGPI-NLGLS---EEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 177 HQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMtIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-202 |
2.39e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 92.81 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYV 85
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQ-SHTaaFPYSVRRMIELGRVPHTG--LGSALRA---EDHAAVDHAMARLGLQEMAERpvtqLSGGERQRVVLARALAQ 159
Cdd:TIGR02868 415 AQdAHL--FDTTVRENLRLARPDATDeeLWAALERvglADWLRALPDGLDTVLGEGGAR----LSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2035452788 160 EAKALLLDEPMTGLDYGHQLRLMSLLgeFAA-EGRLILLTSHRP 202
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDL--LAAlSGRTVVLITHHL 530
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-200 |
3.18e-21 |
|
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: 90.50 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 15 RGSRGTV--LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKP---DRGHVLLEGKPLGAYSASSVAQ----QLAYV 85
Cdd:COG0444 12 PTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQSHTAAF-P-YSVRRMIELGRVPHTGLGsalRAEDHAAVDHAMARLGLQEMAER----PVtQLSGGERQRVVLARALAQ 159
Cdd:COG0444 92 FQDPMTSLnPvMTVGDQIAEPLRIHGGLS---KAEARERAIELLERVGLPDPERRldryPH-ELSGGMRQRVMIARALAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2035452788 160 EAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSH 200
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLaILFITH 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-221 |
4.00e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 4 DLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLeGKPLgaysassvaqQLA 83
Cdd:COG0488 314 KVLELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 84 YVPQsHTAAFPYSvRRMIElgrvphtglgsALRAEDHAAVD-HAMARLGL----QEMAERPVTQLSGGERQRVVLARALA 158
Cdd:COG0488 382 YFDQ-HQEELDPD-KTVLD-----------ELRDGAPGGTEqEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 159 QEAKALLLDEPMTGLDyghqlrLMSL------LGEFaaEGRLIlLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:COG0488 449 SPPNVLLLDEPTNHLD------IETLealeeaLDDF--PGTVL-LVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-228 |
4.66e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.09 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQ----QLAYVPQSHTAAFPYS 96
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGRVpHTGLGSALRAEDHAAVdhaMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK10535 103 AAQNVEVPAV-YAGLERKQRLLRAQEL---LQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 177 HQLRLMSLLGEFAAEGRLILLTSHRPeELFAPASRVLVLDDGHIVADGLPQN 228
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVIIVTHDP-QVAAQAERVIEIRDGEIVRNPPAQE 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-218 |
4.99e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.99 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASS--VAQQL 82
Cdd:PRK11248 1 MLQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYVPQSHTAAfpySVRRMIELGRVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAK 162
Cdd:PRK11248 80 GLLPWRNVQD---NVAFGLQLAGVE--------KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 163 ALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDG 218
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-235 |
5.75e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.30 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFPYS-VRRM 100
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPDNQFVGAtVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK13635 103 VAFGleniGVP--------REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 177 HQLRLMSLLGEFAAEGRLILLT-SHRPEELfAPASRVLVLDDGHIVADGLPQNVVTAEHM 235
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-217 |
7.13e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.54 E-value: 7.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPD---RGHVLLEGKPLGAYSASsvAQQL 82
Cdd:COG4136 2 LSLENLTITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYVPQSHTAaFPY-SVRRMIELGRVPHTGlgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEA 161
Cdd:COG4136 79 GILFQDDLL-FPHlSVGENLAFALPPTIG-----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 162 KALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLI-LLTSHRPEELfAPASRVLVLDD 217
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPaLLVTHDEEDA-PAAGRVLDLGN 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
22-227 |
9.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.64 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQS-HTAAFPYSVRRM 100
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpDDQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRVpHTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLR 180
Cdd:PRK13647 101 VAFGPV-NMGLD---KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2035452788 181 LMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQ 227
Cdd:PRK13647 177 LMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-223 |
1.07e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 25 VSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYS-ASSVAQQLAYVPQSHTAA--FP-YSVRRM 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAGIMLCPEDRKAEgiIPvHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELG-RVPHTGLGSAL--RAEDHAAvDHAMARLGLQE-MAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK11288 352 INISaRRHHLRAGCLInnRWEAENA-DRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2035452788 177 HQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVAD 223
Cdd:PRK11288 431 AKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
9-230 |
1.19e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPD---RGHVLLEGKPLGAYSASSVAqqlAYV 85
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS---AYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQ------SHTAAFPYSVRRMIELGRvphtglgSALRAEDHAAVDHAMARLGLQEMA------ERPVTQLSGGERQRVVL 153
Cdd:TIGR00955 105 QQddlfipTLTVREHLMFQAHLRMPR-------RVTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 154 ARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPE-ELFAPASRVLVLDDGHIVADGLPQNVV 230
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-223 |
1.58e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.18 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLR--RGSRGT-VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASS 77
Cdd:PRK11629 1 MNKILLQCDNLCKRyqEGSVQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 78 VA----QQLAYVPQSHTAAFPYSVRRMIELGRVphtgLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVL 153
Cdd:PRK11629 81 KAelrnQKLGFIYQFHHLLPDFTALENVAMPLL----IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 154 ARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEF-AAEGRLILLTSHrPEELFAPASRVLVLDDGHIVAD 223
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTH-DLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-220 |
2.07e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLkPD---RGHVLLEGKPLGAYS-----ASSVA---QQLAYVPQsht 90
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNirdteRAGIAiihQELALVKE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 aafpYSVRRMIELGRVPHTGlGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPM 170
Cdd:PRK13549 97 ----LSVLENIFLGNEITPG-GIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 171 TGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDG-HI 220
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGrHI 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-235 |
3.13e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 15 RGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ-SHTAAF 93
Cdd:PRK13652 14 SGSK-EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 PYSVRRMIELGRvphTGLGSALRAEDHAaVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:PRK13652 93 SPTVEQDIAFGP---INLGLDEETVAHR-VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 174 DYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHM 235
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-202 |
3.34e-20 |
|
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: 85.49 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQLAYV 85
Cdd:TIGR01189 1 LAARNLACSRGER-MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 pqSHTAAFP--YSVRrmiELGRVPHTGLGSALRAedhaaVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKA 163
Cdd:TIGR01189 79 --GHLPGLKpeLSAL---ENLHFWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 2035452788 164 LLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRP 202
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-226 |
3.44e-20 |
|
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: 85.54 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSR-GTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:cd03369 10 ENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 SHTaAFPYSVRrmielgrvphtglgSALRAEDHAAVDHAMARLGLQEMAErpvtQLSGGERQRVVLARALAQEAKALLLD 167
Cdd:cd03369 90 DPT-LFSGTIR--------------SNLDPFDEYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 168 EPMTGLDYGHQLRLM-SLLGEFAaeGRLILLTSHRPEELfAPASRVLVLDDGHIVADGLP 226
Cdd:cd03369 151 EATASIDYATDALIQkTIREEFT--NSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
20-224 |
6.59e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.06 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA---QQLAYVPQ------SHT 90
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGMIFQhfnllsSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 A----AFPysvrrmIELGRVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLL 166
Cdd:COG1135 99 VaenvALP------LEIAGVP--------KAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 167 DEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPE---ELfapASRVLVLDDGHIVADG 224
Cdd:COG1135 165 DEATSALDPETTRSILDLLKDINRELGLtIVLITHEMDvvrRI---CDRVAVLENGRIVEQG 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-224 |
8.50e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 8.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLrillgllK-------PDRGHVLLEGkplgaysassvaqqlaYVPQSHTAAFp 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTI-------KmltgilvPTSGEVRVLG----------------YVPFKRRKEF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 ysVRRM----------------IE----LG---RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRV 151
Cdd:COG4586 94 --ARRIgvvfgqrsqlwwdlpaIDsfrlLKaiyRIP--------DAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRC 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 152 VLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-232 |
9.46e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.17 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 16 GSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPY 95
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQD-VELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIElgrvphtglgsalRAEDHAAVDH--AMARL-GLQEM------------AERPVTqLSGGERQRVVLARALAQE 160
Cdd:TIGR01842 407 TVAENIA-------------RFGENADPEKiiEAAKLaGVHELilrlpdgydtviGPGGAT-LSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 161 AKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPeELFAPASRVLVLDDGHIVADGLPQNVVTA 232
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-224 |
1.14e-19 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 84.59 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRRM 100
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD-TVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRVphtglgSALRAEDHAAVDHAMARLGLQEMAERPVTQ-------LSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:cd03253 95 IRYGRP------DATDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 174 DYGHQLRLMSLLGEfAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:cd03253 169 DTHTEREIQAALRD-VSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERG 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-224 |
1.23e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.39 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA---QQLAYVPQ------SHT 90
Cdd:PRK11153 19 HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarRQIGMIFQhfnllsSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 A----AFPysvrrmIELGRVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLL 166
Cdd:PRK11153 99 VfdnvALP------LELAGTP--------KAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 167 DEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-223 |
2.35e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 19 GTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS-SVAQQLAYVPQSHTA---AFP 94
Cdd:PRK10762 265 GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRKRdglVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 YSVRRMIELGRVPH--TGLGSALRAEDHAAVDHAMARLGLQE-MAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:PRK10762 345 MSVKENMSLTALRYfsRAGGSLKHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVAD 223
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-238 |
2.75e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 24 NVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYS-ASSVAQQLAYVP---QSHTAAFPYSVRR 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIelGRVPHTGLGSALR-AEDHAAVDHAMARLGLQ-EMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH 177
Cdd:PRK15439 361 NV--CALTHNRRGFWIKpARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 178 QLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIvADGLPQNVVTAEHMSRL 238
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI-SGALTGAAINVDTIMRL 498
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-224 |
2.91e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQLA--YVPQsHTAAFP-YSV 97
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARLTPAKAHQLGiyLVPQ-EPLLFPnLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIeLGRVPHtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH 177
Cdd:PRK15439 104 KENI-LFGLPK-------RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2035452788 178 QLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-224 |
3.67e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 16 GSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPY 95
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD-AGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELGRVPHTGLGSALRAEDHAAVDHAMAR-LGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK13657 424 SIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2035452788 175 YGHQLRLMSLLGEfAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:PRK13657 504 VETEAKVKAALDE-LMKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESG 551
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-189 |
3.99e-19 |
|
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: 83.61 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 28 SLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGkplgaysassvaQQLAYVPQSHTAAFPYSVRRMIElGRVP 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL------------DTVSYKPQYIKADYEGTVRDLLS-SITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 108 HTGLGSALRAEdhaavdhAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGE 187
Cdd:cd03237 88 DFYTHPYFKTE-------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
..
gi 2035452788 188 FA 189
Cdd:cd03237 161 FA 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-174 |
5.08e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 86.02 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 29 LRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassvaqqLAYVPQSHTAAFPYSVRRMieLGRVPH 108
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISYKPQYIKPDYDGTVEDL--LRSITD 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 109 TGLGSALRAEdhaavdhAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK13409 427 DLGSSYYKSE-------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-223 |
8.43e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAysassvAQQlayv 85
Cdd:PRK11247 13 LLLNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------ARE---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 pqshtaafpySVRRMIELGR-------VPHTGLGsaLRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALA 158
Cdd:PRK11247 82 ----------DTRLMFQDARllpwkkvIDNVGLG--LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 159 QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVAD 223
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-240 |
8.86e-19 |
|
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: 85.45 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 16 GSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgAYSASSVAQQLAYVPQshtaafpY 95
Cdd:TIGR01257 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQ-------F 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELGRvPHTGLGSALRA----EDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:TIGR01257 2021 DAIDDLLTGR-EHLYLYARLRGvpaeEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLvlddghIVADGLPQNVVTAEHMSRLYG 240
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLA------IMVKGAFQCLGTIQHLKSKFG 2162
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-224 |
1.07e-18 |
|
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: 85.18 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRRM 100
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQE-PYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRVPHTGLGSALRAEDHAAVDHAMAR--LGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:TIGR01193 568 LLLGAKENVSQDEIWAACEIAEIKDDIENmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2035452788 179 LRLMSLLgeFAAEGRLILLTSHRpEELFAPASRVLVLDDGHIVADG 224
Cdd:TIGR01193 648 KKIVNNL--LNLQDKTIIFVAHR-LSVAKQSDKIIVLDHGKIIEQG 690
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
24-224 |
1.08e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 84.94 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 24 NVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRRMIEL 103
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQD-AGLFNRSIRENIRL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 104 GRVPHTGLGSALRAEDHAAVDHAMARLG--LQEMAERPvTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRL 181
Cdd:TIGR01192 432 GREGATDEEVYEAAKAAAAHDFILKRSNgyDTLVGERG-NRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARV 510
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2035452788 182 MSLLgEFAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:TIGR01192 511 KNAI-DALRKNRTTFIIAHRLSTV-RNADLVLFLDQGRLIEKG 551
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-222 |
1.21e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 24 NVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSA-SSVAQQLAYVPQSH--TAAFP-YSVRR 99
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESRrdNGFFPnFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGR-VPHTGLGSAL----RAEDHAAVDHAMARLGLQ-EMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:PRK09700 361 NMAISRsLKDGGYKGAMglfhEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2035452788 174 DYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVA 222
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-229 |
1.32e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRGTVlDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQ 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 81 QLAYVPQSHTAAFpysvRRM--IE-LGRVPHTGLGSAL-----------RAEDhAAVDHA---MARLGLQEMAERPVTQL 143
Cdd:PRK11300 80 MGVVRTFQHVRLF----REMtvIEnLLVAQHQQLKTGLfsgllktpafrRAES-EALDRAatwLERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 144 SGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVA 222
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
....*..
gi 2035452788 223 DGLPQNV 229
Cdd:PRK11300 235 NGTPEEI 241
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-223 |
1.83e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.06 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYV---PQSHTAAfpys 96
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVfqdPMMGTAP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 vrRM-IE------LGRVPHTGLGSALRAEDHAAVDHAMARL--GLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLD 167
Cdd:COG1101 96 --SMtIEenlalaYRRGKRRGLRRGLTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 168 EPMTGLDYGHQLRLMSLLGEFAAEGRLI-LLTSHRPEELFAPASRVLVLDDGHIVAD 223
Cdd:COG1101 174 EHTAALDPKTAALVLELTEKIVEENNLTtLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-224 |
2.79e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.00 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRRM 100
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE-PVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELgrvphtGLGSALRAEDHAAVDHAMARLGLQEMAERPVT-------QLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:TIGR00958 575 IAY------GLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 174 DyghqLRLMSLLGEF-AAEGRLILLTSHRpEELFAPASRVLVLDDGHIVADG 224
Cdd:TIGR00958 649 D----AECEQLLQESrSRASRTVLLIAHR-LSTVERADQILVLKKGSVVEMG 695
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-232 |
2.94e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 10 GVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLkPDRGHVLLEGKPLGAYSASS---VAQQLAYVP 86
Cdd:PRK15134 290 GILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 87 QSHTAAFP--YSVRRMIELG-RVPHTGLGSALRaedHAAVDHAMARLGLQ-EMAERPVTQLSGGERQRVVLARALAQEAK 162
Cdd:PRK15134 369 QDPNSSLNprLNVLQIIEEGlRVHQPTLSAAQR---EQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 163 ALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTA 232
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLaYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-229 |
3.46e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 24 NVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaysaSSVAQQL---------AYVPQSHTAaFP 94
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL-----FDAEKGIclppekrriGYVFQDARL-FP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 -YSVRRMIELGrvphtglgsaLRAEDHAAVDHAMARLGLQEMAER-PVTqLSGGERQRVVLARALAQEAKALLLDEPMTG 172
Cdd:PRK11144 90 hYKVRGNLRYG----------MAKSMVAQFDKIVALLGIEPLLDRyPGS-LSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 173 LDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK11144 159 LDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-224 |
3.66e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.22 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 16 GSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPY 95
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT-PFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELGRvPHTGLGSALRAEDHAAVDHAMARL--GLQ-EMAERPVtQLSGGERQRVVLARALAQEAKALLLDEPMTG 172
Cdd:PRK10789 404 TVANNIALGR-PDATQQEIEHVARLASVHDDILRLpqGYDtEVGERGV-MLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 173 LDYGHQLRLMSLLGEFaAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:PRK10789 482 VDGRTEHQILHNLRQW-GEGRTVIISAHRLSAL-TEASEILVMQHGHIAQRG 531
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-221 |
5.62e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.92 E-value: 5.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA---QQLAYVPQSHTAAFPYSVR 98
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELGRVPHTGLGSALRAEDHAAVDhamaRLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALD----KVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:PRK10908 174 EGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-224 |
5.87e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 82.76 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQS-HTaaFPYSVRRM 100
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNvHL--FNDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRvphTGLGSALRAEDHAAVDHAMARL-----GLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:PRK11176 437 IAYAR---TEQYSREQIEEAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2035452788 176 GHQLRLMSLLGEFAAEgRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:PRK11176 514 ESERAIQAALDELQKN-RTSLVIAHRLSTI-EKADEILVVEDGEIVERG 560
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
13-174 |
6.19e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 81.70 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 13 LRRGSRGTV--LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA---QQLAYVPQ 87
Cdd:COG4608 23 LFGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 ShtaafPYS-------VRRMIELGRVPHtGLGSalRAEDHAAVDHAMARLGL-QEMAERPVTQLSGGERQRVVLARALAQ 159
Cdd:COG4608 103 D-----PYAslnprmtVGDIIAEPLRIH-GLAS--KAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALAL 174
|
170
....*....|....*
gi 2035452788 160 EAKALLLDEPMTGLD 174
Cdd:COG4608 175 NPKLIVCDEPVSALD 189
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-232 |
6.56e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassVAQQLAYvpqshTAAF-P-YSV 97
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VSALLEL-----GAGFhPeLTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIEL-GRVphtgLGsALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPM-TGlDY 175
Cdd:COG1134 106 RENIYLnGRL----LG-LSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 176 GHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTA 232
Cdd:COG1134 180 AFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-258 |
9.16e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVllegkPLGAYSASSVAQQLAYVP--QSHTAAFPYSVRR 99
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-----TVGDIVVSSTSKQKEIKPvrKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRVPHTGLG------SALRAEDHAAVDHAMARLGlQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:PRK13643 97 LFEETVLKDVAFGpqnfgiPKEKAEKIAAEKLEMVGLA-DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 174 DYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSLKQVDH----- 248
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGVPKATHfadql 255
|
250
....*....|
gi 2035452788 249 EGSRFFTMEK 258
Cdd:PRK13643 256 QKTGAVTFEK 265
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-221 |
1.50e-17 |
|
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: 81.65 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVC----LRRGS-RGTV-----LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLkPDRGHVLLEGKPLGAYS 74
Cdd:COG4172 275 LLEARDLKvwfpIKRGLfRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 75 AS---SVAQQLAYVPQShtaafPYS-------VRRMIELG-RVPHTGLGsalRAEDHAAVDHAMARLGLQ-EMAERPVTQ 142
Cdd:COG4172 354 RRalrPLRRRMQVVFQD-----PFGslsprmtVGQIIAEGlRVHGPGLS---AAERRARVAEALEEVGLDpAARHRYPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 143 LSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSH-----RpeelfAPASRVLVLD 216
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLaYLFISHdlavvR-----ALAHRVMVMK 500
|
....*
gi 2035452788 217 DGHIV 221
Cdd:COG4172 501 DGKVV 505
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-224 |
1.53e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.43 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 19 GTVL-DNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLkPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAaFPYSV 97
Cdd:PRK11174 362 GKTLaGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQL-PHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIELGRVphtglgsalRAEDhAAVDHAMARLGLQEMAER-------PVTQ----LSGGERQRVVLARALAQEAKALLL 166
Cdd:PRK11174 440 RDNVLLGNP---------DASD-EQLQQALENAWVSEFLPLlpqgldtPIGDqaagLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 167 DEPMTGLDYGHQLRLMSLLGEfAAEGRLILLTSHRPEELfAPASRVLVLDDGHIVADG 224
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDL-AQWDQIWVMQDGQIVQQG 565
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-222 |
1.84e-17 |
|
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: 81.41 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPD--RGHVLLEGKPLGAYSASS--------VAQQLAYVPQsh 89
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDteragiviIHQELTLVPE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 90 taafpYSVRRMIELG-RVPHTGLGSALRAEDHAAvDHAMARLGLQEM-AERPVTQLSGGERQRVVLARALAQEAKALLLD 167
Cdd:TIGR02633 93 -----LSVAENIFLGnEITLPGGRMAYNAMYLRA-KNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 168 EPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVA 222
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-174 |
1.84e-17 |
|
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: 81.37 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 28 SLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassvaqqLAYVPQSHTAAFPYSVRRMIElGRVP 107
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------ISYKPQYISPDYDGTVEEFLR-SANT 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 108 HTGLGSALRAEdhaavdhAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:COG1245 428 DDFGSSYYKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-224 |
2.73e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEG------KPLGAYSASSVAQQLAYVPQSHTAAFP 94
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 YSVrrMIELGRVPHTGLGSAlraeDHAAVDHAM---ARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:COG4161 97 LTV--MENLIEAPCKVLGLS----KEQAREKAMkllARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEelFAP--ASRVLVLDDGHIVADG 224
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGITQVIVTHEVE--FARkvASQVVYMEKGRIIEQG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-224 |
2.82e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEG------KPLGAYSASSVAQQLAYVPQSHTAAFP 94
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 YSVRR-MIElgrVPHTGLGSAlRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:PRK11124 97 LTVQQnLIE---APCRVLGLS-KDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 174 DYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-218 |
3.80e-17 |
|
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: 77.12 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassvaqqLAYVPQShtaafPY----S 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQE-----PWiqngT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIeLGrvphtglGSALRAEDHAAVDHA------MARL--GLQ-EMAERPVTqLSGGERQRVVLARALAQEAKALLLD 167
Cdd:cd03250 82 IRENI-LF-------GKPFDEERYEKVIKAcalepdLEILpdGDLtEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 168 EPMTGLD--YGHQLrLMSLLGEFAAEGRLILLTSHRpEELFAPASRVLVLDDG 218
Cdd:cd03250 153 DPLSAVDahVGRHI-FENCILGLLLNNKTRILVTHQ-LQLLPHADQIVVLDNG 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-227 |
4.28e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.52 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDR---GHVLLEGKPLG-----AYSASSVAQQLAYVPQSHTAAF 93
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQregrlARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 PYSVRRMI---ELGRVP--HTGLGSALRAEDHAAVdHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDE 168
Cdd:PRK09984 100 RLSVLENVligALGSTPfwRTCFSWFTREQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 169 PMTGLDYGHQLRLMSLLGEF-AAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQ 227
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-226 |
4.39e-17 |
|
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: 77.53 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:cd03244 6 KNVSLRyRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 SHTaAFPYSVRRMIE-LGRVPHTGLGSALraEDHAAVDHAMARL-GLQEMAERPVTQLSGGERQRVVLARALAQEAKALL 165
Cdd:cd03244 86 DPV-LFSGTIRSNLDpFGEYSDEELWQAL--ERVGLKEFVESLPgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGE-FAaeGRLILLTSHRPEELfAPASRVLVLDDGHIVADGLP 226
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREaFK--DCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDSP 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-200 |
8.32e-17 |
|
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: 79.44 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 29 LRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHV--------LLE---GKPLGAYSASSVAQQL--AYVPQshtaafpy 95
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGTELQDYFKKLANGEIkvAHKPQ-------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 svrrMIELgrVP--HTGLGSAL--RAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:COG1245 168 ----YVDL--IPkvFKGTVRELleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180
....*....|....*....|....*....
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAEGRLILLTSH 200
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-256 |
1.13e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LAYVPQSHTAAFPYSVR 98
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELGRVPHT---GLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:PRK09700 99 ENLYIGRHLTKkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 176 GHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSLKqvdhegSRFFT 255
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRELQ------NRFNA 252
|
.
gi 2035452788 256 M 256
Cdd:PRK09700 253 M 253
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-238 |
1.52e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.55 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 14 RRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS------SVAQQLAYVPQ 87
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 SHTAAFP----YSVRRMIE-LGRVPHTGLGSAlRAEDHAAVDHAMARLGLQEMAER--PVtQLSGGERQRVVLARALAQE 160
Cdd:PRK10619 93 RLTMVFQhfnlWSHMTVLEnVMEAPIQVLGLS-KQEARERAVKYLAKVGIDERAQGkyPV-HLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 161 AKALLLDEPMTGLD---YGHQLRLMSLLGEfaaEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHMSR 237
Cdd:PRK10619 171 PEVLLFDEPTSALDpelVGEVLRIMQQLAE---EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPR 247
|
.
gi 2035452788 238 L 238
Cdd:PRK10619 248 L 248
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-235 |
2.03e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.20 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSvaQQLAYVPQ------------ 87
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNH--ELITNPYSkkiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 -SHTAAFP-Y-----SVRRMIELGRVphtGLGSAlRAEDHAAVDHAMARLGLQE-MAERPVTQLSGGERQRVVLARALAQ 159
Cdd:PRK13631 118 vSMVFQFPeYqlfkdTIEKDIMFGPV---ALGVK-KSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 160 EAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEHM 235
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-229 |
2.34e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAF-----PYS 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFvgsivKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGRVPHTglgsalraEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK13648 105 VAFGLENHAVPYD--------EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 177 HQLRLMSLLGEFAAEGRL-ILLTSHRPEELfAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNItIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
2.48e-16 |
|
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: 75.55 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNAdLLACEGVC------LRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLL--EGKPLGA 72
Cdd:COG4778 1 MTT-LLEVENLSktftlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 73 YSASSV------AQQLAYVPQshtaaFPYSVRR----------MIELGRvphtglgSALRAEDHAAvdHAMARLGLQema 136
Cdd:COG4778 80 AQASPReilalrRRTIGYVSQ-----FLRVIPRvsaldvvaepLLERGV-------DREEARARAR--ELLARLNLP--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 137 ER-----PVTqLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASR 211
Cdd:COG4778 143 ERlwdlpPAT-FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADR 221
|
....*..
gi 2035452788 212 VLVLDDG 218
Cdd:COG4778 222 VVDVTPF 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-246 |
4.31e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 24 NVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASsvaqQLAYVPQSHTAAFPYSVRRMIEL 103
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDA----ELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 104 GRVPHTGLGSAL----RAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQL 179
Cdd:PRK10070 122 TVLDNTAFGMELaginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 180 RLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVT--AEHMSRLY--GVSLKQV 246
Cdd:PRK10070 202 EMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNnpANDYVRTFfrGVDISQV 273
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-232 |
5.40e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILL-------GLLKPDrGHVLLEGKPLGAYSASSVAQQLAYVPQsHTAAF 93
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVD-GKVLYFGKDIFQIDAIKLRKEVGMVFQ-QPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 PY-SVRRMIELgrvPHTGLGSALRAEDHAAVDHAMARLGL-QEMAER---PVTQLSGGERQRVVLARALAQEAKALLLDE 168
Cdd:PRK14246 103 PHlSIYDNIAY---PLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 169 PMTGLDYGHQLRLMSLLGEFAAEgRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTA 232
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-201 |
6.03e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEG----KPLGAYSassvaQQLAYVPQsHTAAFPYS 96
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTYQ-----KQLCFVGH-RSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGRVpHTGLGSalraedhAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK13540 90 TLRENCLYDI-HFSPGA-------VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 2035452788 177 HQLRLMSLLGEFAAEGRLILLTSHR 201
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-229 |
8.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.78 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 19 GTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS----SVAQQLAYVPQ-SHTAAF 93
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQIRKKVGLVFQfPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 PYSVRRMIELGrvPHTGLGSALRAEDHAAVDHAMARLGlQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGL 173
Cdd:PRK13649 100 EETVLKDVAFG--PQNFGVSQEEAEALAREKLALVGIS-ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 174 DYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-230 |
1.29e-15 |
|
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: 75.99 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRIL--LGLLKPDRGHVLLE----------------GKPLGAYSASSVAQQL 82
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskvGEPCPVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYVPQSHTAAFPYSVRRMIELGRV-----PHTGLGSALRA------EDHAAVDHAMARLGLQEMAERPV---TQLSGGER 148
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTfalygDDTVLDNVLEAleeigyEGKEAVGRAVDLIEMVQLSHRIThiaRDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 149 QRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFA-AEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQ 227
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPD 254
|
...
gi 2035452788 228 NVV 230
Cdd:TIGR03269 255 EVV 257
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-224 |
1.60e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 73.34 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPlgaysASSVAQQLAYVPQshtaafpYSVRR 99
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-----SSLLGLGGGFNPE-------LTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIEL-GRVphtgLGsALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:cd03220 104 NIYLnGRL----LG-LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-243 |
1.65e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.07 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 17 SRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPD---RGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAF 93
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIREKVGIVFQNPDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 PYS-----VRRMIELGRVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDE 168
Cdd:PRK13640 98 VGAtvgddVAFGLENRAVP--------RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 169 PMTGLDYGHQLRLMSLLGEFAAEGRLILLT-SHRPEELfAPASRVLVLDDGHIVADGLPQNVVTAEHMSRLYGVSL 243
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDI 244
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-227 |
1.94e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.65 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 3 ADLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS---SVA 79
Cdd:PRK11831 5 ANLVDMRGVSFTRGNR-CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 80 QQLAYVPQSHTAAFPYSVRRMIELGRVPHTGLGSALRaedHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQ 159
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLL---HSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 160 EAKALLLDEPMTGLDYGHQLRLMSLLGEF-AAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQ 227
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-224 |
2.06e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.25 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLL------EGKPLGAYSA--SSVAQQLAYVPQSHTA 91
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGliRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 92 aFPY-SVRRMIELGRVPHTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPM 170
Cdd:PRK11264 97 -FPHrTVLENIIEGPVIVKGEP---KEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 171 TGLDYGHQLRLMSLLGEFAAEGRLILLTSHrpEELFAP--ASRVLVLDDGHIVADG 224
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTH--EMSFARdvADRAIFMDQGRIVEQG 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-200 |
2.57e-15 |
|
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: 73.17 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 30 RAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHvlLEGKP-----LGAYSASSVAQQLAYVPQSHTAAfpysVRRMIELG 104
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELQNYFTKLLEGDVKV----IVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 105 RVPHTGLGSAL----RAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLR 180
Cdd:cd03236 98 LIPKAVKGKVGellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|
gi 2035452788 181 LMSLLGEFAAEGRLILLTSH 200
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEH 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-233 |
2.63e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.49 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAF-PYSVRR 99
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDNQFiGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELG----RVPhtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:PRK13632 104 DIAFGlenkKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 176 GHQLRLMSLLGEFAAEGR--LILLTsHRPEELFApASRVLVLDDGHIVADGLPQNVVTAE 233
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKktLISIT-HDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-224 |
3.42e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILL--GLLKPDRGHVLLEGKPLGAYSASSVAQQ-LAYvpqshtaAFPYS 96
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERARAgIFL-------AFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VR----RMIELgrvphtgLGSALRA---------EDHAAVDHAMARLGL-QEMAERPVTQ-LSGGERQRVVLARALAQEA 161
Cdd:COG0396 87 VEipgvSVSNF-------LRTALNArrgeelsarEFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 162 KALLLDEPMTGLDYgHQLRLMS-LLGEFAAEGRLILLTSHRPEEL-FAPASRVLVLDDGHIVADG 224
Cdd:COG0396 160 KLAILDETDSGLDI-DALRIVAeGVNKLRSPDRGILIITHYQRILdYIKPDFVHVLVDGRIVKSG 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-222 |
3.65e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSA--------SSVAQQLAYVPQShtaaf 93
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkealengiSMVHQELNLVLQR----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 pySVRRMIELGRVPHTGLgsalraedhaAVDHA-MAR--------LGLQEMAERPVTQLSGGERQRVVLARALAQEAKAL 164
Cdd:PRK10982 89 --SVMDNMWLGRYPTKGM----------FVDQDkMYRdtkaifdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVA 222
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-221 |
4.98e-15 |
|
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: 74.09 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRR 99
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD-TVLFNDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRVphtglgSALRAEDHAAVDHA-----MARL--GLQEM-AERPVtQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:COG5265 451 NIAYGRP------DASEEEVEAAARAAqihdfIESLpdGYDTRvGERGL-KLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 172 GLDYGHQLRLMSLLGEfAAEGRLILLTSHRpeeL--FAPASRVLVLDDGHIV 221
Cdd:COG5265 524 ALDSRTERAIQAALRE-VARGRTTLVIAHR---LstIVDADEILVLEAGRIV 571
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-243 |
5.88e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.04 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRrgSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPD----RGHVLLEGKPLGAysASSVAQQ 81
Cdd:PRK10418 5 IELRNIALQ--AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAP--CALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 82 LAYVPQSHTAAFPySVRRMIELGRVPHTGLGsalRAEDHAAVDHAMARLGLQE---MAERPVTQLSGGERQRVVLARALA 158
Cdd:PRK10418 81 IATIMQNPRSAFN-PLHTMHTHARETCLALG---KPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 159 QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADG-------LPQNVV 230
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGdvetlfnAPKHAV 236
|
250
....*....|....*..
gi 2035452788 231 T----AEHMSrLYGVSL 243
Cdd:PRK10418 237 TrslvSAHLA-LYGMEL 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-235 |
6.27e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.43 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAF-PYSVRRM 100
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFvGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGrVPHTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLR 180
Cdd:PRK13642 103 VAFG-MENQGIP---REEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 181 LMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV-VTAEHM 235
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELfATSEDM 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-218 |
7.98e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.69 E-value: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 2 NADLLACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTllrillgllkpdrghvLL----------EGK--- 68
Cdd:COG4178 359 EDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKST----------------LLraiaglwpygSGRiar 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 69 PLGAysassvaqQLAYVPQShtaafPYsvrrmielgrVPHTGLGSAL------RAEDHAAVDHAMARLGLQEMAERPVTQ 142
Cdd:COG4178 423 PAGA--------RVLFLPQR-----PY----------LPLGTLREALlypataEAFSDAELREALEAVGLGHLAERLDEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 143 ------LSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLtSHRPeELFAPASRVLVLD 216
Cdd:COG4178 480 adwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISV-GHRS-TLAAFHDRVLELT 557
|
..
gi 2035452788 217 DG 218
Cdd:COG4178 558 GD 559
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
22-227 |
1.50e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.30 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAF-PYSVRRM 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQFvGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGrVPHTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLR 180
Cdd:PRK13650 103 VAFG-LENKGIP---HEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 181 LMSLLGEFAAEGRLILLT-SHRPEELfAPASRVLVLDDGHIVADGLPQ 227
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISiTHDLDEV-ALSDRVLVMKNGQVESTSTPR 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
1.72e-14 |
|
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: 72.41 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRG---TVLDNVSVSLRAGELVGLLGLNGAGKS-----TLLRILLGLLKPDrGHVLLEGKPLGA 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGgtvEAVKGVSFDIAAGETLALVGESGSGKSvtalsILRLLPDPAAHPS-GSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 73 YSASSVAQ----QLAYVPQS-HTAAFP-YSV-RRMIELGRVpHTGLGsalRAEDHAAVDHAMARLGLQEmAERPVT---- 141
Cdd:COG4172 81 LSERELRRirgnRIAMIFQEpMTSLNPlHTIgKQIAEVLRL-HRGLS---GAAARARALELLERVGIPD-PERRLDayph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 142 QLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHrpeEL-----FapASRVLVL 215
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITH---DLgvvrrF--ADRVAVM 230
|
....*.
gi 2035452788 216 DDGHIV 221
Cdd:COG4172 231 RQGEIV 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-189 |
2.65e-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: 71.89 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLegkplgaysASSVaqQLAYVPQS 88
Cdd:TIGR03719 326 ENLTKAFGDK-LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETV--KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 89 HTAAFP-YSVRRMIELGrvphtglgsalraedhaavdHAMARLGLQEMAER---------------PVTQLSGGERQRVV 152
Cdd:TIGR03719 394 RDALDPnKTVWEEISGG--------------------LDIIKLGKREIPSRayvgrfnfkgsdqqkKVGQLSGGERNRVH 453
|
170 180 190
....*....|....*....|....*....|....*...
gi 2035452788 153 LARALAQEAKALLLDEPMTGLDYgHQLR-LMSLLGEFA 189
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDV-ETLRaLEEALLNFA 490
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-218 |
3.21e-14 |
|
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: 69.19 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 16 GSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGllKPDRGHV----LLEGKPLGAysasSVAQQLAYVPQSHTA 91
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVItgeiLINGRPLDK----NFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 92 AFPYSVRRMIELgrvphtglgSA-LRAedhaavdhamarlglqemaerpvtqLSGGERQRVVLARALAQEAKALLLDEPM 170
Cdd:cd03232 91 SPNLTVREALRF---------SAlLRG-------------------------LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2035452788 171 TGLDYGHQLRLMSLLGEFAAEGRLILLTSHRP-EELFAPASRVLVLDDG 218
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQAILCTIHQPsASIFEKFDRLLLLKRG 185
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-224 |
3.54e-14 |
|
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: 69.98 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGllKPD----RGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFP-Y 95
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDERARAGLFLAFQYPEEIPgV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIelgrvpHTGLGSALRAEDHAAVD---------HAMARLGL-QEMAERPVTQ-LSGGERQRVVLARALAQEAKAL 164
Cdd:TIGR01978 93 SNLEFL------RSALNARRSARGEEPLDlldfekllkEKLALLDMdEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 165 LLDEPMTGLDYgHQLRLMS-LLGEFAAEGRLILLTSHRPE--ELFAPaSRVLVLDDGHIVADG 224
Cdd:TIGR01978 167 ILDEIDSGLDI-DALKIVAeGINRLREPDRSFLIITHYQRllNYIKP-DYVHVLLDGRIVKSG 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-226 |
4.39e-14 |
|
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: 71.97 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAySASSVAQQLAYVPQsHTAAFPYsvrrmi 101
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQ-HNILFHH------ 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 eLGRVPHTGLGSAL--RAEDHAAVD-HAMAR-LGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH 177
Cdd:TIGR01257 1018 -LTVAEHILFYAQLkgRSWEEAQLEmEAMLEdTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2035452788 178 QLRLMSLLGEFAAeGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLP 226
Cdd:TIGR01257 1097 RRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-221 |
5.02e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLrillgllkpdrgHVLLEGKPLGAYS---------------ASSVA------- 79
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLM------------KVLSGVYPHGSYEgeilfdgevcrfkdiRDSEAlgiviih 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 80 QQLAYVPQshtaafpYSVRRMIELGRVPHTGlGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQ 159
Cdd:NF040905 85 QELALIPY-------LSIAENIFLGNERAKR-GVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 160 EAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-219 |
6.74e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 67.09 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVllegkplgaysASSVAQQLAYV 85
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PqshtaafpysvrrmielgrvphtglgsalraedhaavdhamarlglqemaerpvtQLSGGERQRVVLARALAQEAKALL 165
Cdd:cd03221 69 E-------------------------------------------------------QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGEFAaegRLILLTSHRPEELFAPASRVLVLDDGH 219
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-200 |
1.02e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 29 LRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVllEGKP-----LGAYSAS--------------SVAQQLAYV---P 86
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEPswdevLKRFRGTelqnyfkklyngeiKVVHKPQYVdliP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 87 QshtaAFPYSVRRMIElgrvphtglgsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLL 166
Cdd:PRK13409 174 K----VFKGKVRELLK-------------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....
gi 2035452788 167 DEPMTGLDYGHQLRLMSLLGEFaAEGRLILLTSH 200
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEH 269
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-231 |
1.63e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLK--PD---RGHVLLEGKPLGAYSASSVAQQLAYVPQSHTAAFPY 95
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELGRVPHTGLGSalRAEDHAAVDHAMARLGL-QEMAER---PVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:PRK14247 98 SIFENVALGLKLNRLVKS--KKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAEGRLILLTsHRPEELFAPASRVLVLDDGHIVADGLPQNVVT 231
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVT-HFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
1.75e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.57 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHV---------LLEGKPLGAYSASSVAQ---------- 80
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknKKKTKEKEKVLEKLVIQktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 81 -----QLAYVPQ-SHTAAFPYSVRRMIELGRVphtGLG-SALRAEDHAAVDHAMarLGL-QEMAERPVTQLSGGERQRVV 152
Cdd:PRK13651 101 keirrRVGVVFQfAEYQLFEQTIEKDIIFGPV---SMGvSKEEAKKRAAKYIEL--VGLdESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 153 LARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-221 |
1.79e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQ-LAYVPQSHTAAFPYSVRR 99
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 100 MIELGRVPHTGLGSALRAEdhaAVDHAMARLgLQEMAERPVTqLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQL 179
Cdd:PRK11614 100 NLAMGGFFAERDQFQERIK---WVYELFPRL-HERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2035452788 180 RLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-223 |
2.16e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAG----------KSTLLRIllgllkpdRGHVLLEGKPLgaySASSVAQQ----LAYVP 86
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGrtelamsvfgRSYGRNI--------SGTVFKDGKEV---DVSTVSDAidagLAYVT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 87 QSHTAA---FPYSVRRMI---ELGRVPHTGLgsalraedhaaVDHAMARlglqEMAER--------------PVTQLSGG 146
Cdd:NF040905 344 EDRKGYglnLIDDIKRNItlaNLGKVSRRGV-----------IDENEEI----KVAEEyrkkmniktpsvfqKVGNLSGG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 147 ERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVAD 223
Cdd:NF040905 409 NQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-224 |
3.48e-13 |
|
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: 66.40 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILL--GLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVpqshtaAFPYSVR 98
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEERARLGIFL------AFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 rmielgrVPHTGLGSALRaedhaavdhamarlGLQEmaerpvtQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYgHQ 178
Cdd:cd03217 89 -------IPGVKNADFLR--------------YVNE-------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 179 LRLMS-LLGEFAAEGRLILLTSHRPEEL-FAPASRVLVLDDGHIVADG 224
Cdd:cd03217 140 LRLVAeVINKLREEGKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-229 |
5.56e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASS----VAQQLAYVPQ-SHTAAFPYS 96
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpVRKRIGMVFQfPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 VRRMIELGrvPHTgLGSALRAEDHAAVDHAMaRLGLQE--MAERPVtQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK13646 103 VEREIIFG--PKN-FKMNLDEVKNYAHRLLM-DLGFSRdvMSQSPF-QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 175 YGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-218 |
5.94e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPD--RGHVLLEGKPLgaysASSVAQQLAYVPQSHTAAFPYSV 97
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP----TKQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMI---ELGRVPHtglgSALRAEDHAAVDHAMARLGLQE-----MAERPVTQLSGGERQRVVLARALAQEAKALLLDEP 169
Cdd:PLN03211 158 RETLvfcSLLRLPK----SLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2035452788 170 MTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRP-EELFAPASRVLVLDDG 218
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPsSRVYQMFDSVLVLSEG 283
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-226 |
7.67e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGA-----YSASSVAQQLAYVPQ-SHTAAFPY 95
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRKEIGLVFQfPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELGRVpHTGlgsALRAEDHAAVDHAMARLGL-QEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK13645 107 TIEKDIAFGPV-NLG---ENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 175 YGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLP 226
Cdd:PRK13645 183 PKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
13-232 |
1.44e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 65.63 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 13 LRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ-SHTA 91
Cdd:COG4167 21 FRRQQF-EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQdPNTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 92 AFP-YSVRRMIELGRVPHTGLGSALRAEdhaAVDHAMARLGL-QEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEP 169
Cdd:COG4167 100 LNPrLNIGQILEEPLRLNTDLTAEEREE---RIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 170 MTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTA 232
Cdd:COG4167 177 LAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-174 |
1.46e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 23 DNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLegkplgaysASSVaqQLAYVPQSHTAAFP-YSVRRMI 101
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---------GETV--KLAYVDQSRDALDPnKTVWEEI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 ELGrvphtglgsalraedhaavdHAMARLGLQEMAER---------------PVTQLSGGERQRVVLARALAQEAKALLL 166
Cdd:PRK11819 410 SGG--------------------LDIIKVGNREIPSRayvgrfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLL 469
|
....*...
gi 2035452788 167 DEPMTGLD 174
Cdd:PRK11819 470 DEPTNDLD 477
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-174 |
1.51e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSA-SSVAQQLAYVPQ 87
Cdd:NF033858 5 EGVSHRYGKT-VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 S------HTaafpYSVRRMIEL-GRVphTGLGsalRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQE 160
Cdd:NF033858 84 GlgknlyPT----LSVFENLDFfGRL--FGQD---AAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170
....*....|....
gi 2035452788 161 AKALLLDEPMTGLD 174
Cdd:NF033858 155 PDLLILDEPTTGVD 168
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-185 |
1.61e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.14 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVA---QQLAYVPQShtaafPYS-- 96
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrQKIQIVFQN-----PYGsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 -----VRRMIELGRVPHTGLGSALRAEDHAAVdhaMARLGLQ-EMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPM 170
Cdd:PRK11308 106 nprkkVGQILEEPLLINTSLSAAERREKALAM---MAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170
....*....|....*
gi 2035452788 171 TGLDYGHQLRLMSLL 185
Cdd:PRK11308 183 SALDVSVQAQVLNLM 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-221 |
1.92e-12 |
|
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: 64.21 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKST----LLRILLGLLKPDrGHVLLEGKPlGAYSASSVAQQLAYVPQSHTAAFPY 95
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIP-YKEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIELgrvphtglgsALRAEDHAAVdhamarlglqemaeRPVtqlSGGERQRVVLARALAQEAKALLLDEPMTGLDY 175
Cdd:cd03233 99 TVRETLDF----------ALRCKGNEFV--------------RGI---SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 176 GHQLRLMSLLGEFAAEGRLILL--TSHRPEELFAPASRVLVLDDGHIV 221
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTFvsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-229 |
2.01e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.43 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS----SVAQQLAYVPQshtaaFPYS- 96
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkPLRKKVGIVFQ-----FPEHq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 97 -----VRRMIELGrvPhTGLGSAlRAEDHAAVDHAMARLGL-QEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPM 170
Cdd:PRK13634 98 lfeetVEKDICFG--P-MNFGVS-EEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 171 TGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNV 229
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLtTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-233 |
2.54e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.28 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVpQSHTAAFPYSVRRM 100
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV-QQDPVVLADTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGR-VPHTGLGSALRAEDHAAVDHAM-----ARLGLQEmaerpvTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK10790 435 VTLGRdISEEQVWQALETVQLAELARSLpdglyTPLGEQG------NNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 175 YGHQLRLMSLLGEFAAEGRLILLtSHRPEELfAPASRVLVLDDGHIVADGLPQNVVTAE 233
Cdd:PRK10790 509 SGTEQAIQQALAAVREHTTLVVI-AHRLSTI-VEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-256 |
4.46e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:PLN03232 1238 EDVHLRyRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 ShTAAFPYSVRRMIE-LGRVPHTGLGSAL-RAEDHAAVDHamARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALL 165
Cdd:PLN03232 1318 S-PVLFSGTVRFNIDpFSEHNDADLWEALeRAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 166 LDEPMTGLDyghqLRLMSLLG-----EFAAEGRLILltSHRPEELFaPASRVLVLDDGHIVADGLPQnvvtaEHMSRlyg 240
Cdd:PLN03232 1395 LDEATASVD----VRTDSLIQrtireEFKSCTMLVI--AHRLNTII-DCDKILVLSSGQVLEYDSPQ-----ELLSR--- 1459
|
250
....*....|....*.
gi 2035452788 241 vslkqvdhEGSRFFTM 256
Cdd:PLN03232 1460 --------DTSAFFRM 1467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-232 |
4.83e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.74 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 12 CLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShT 90
Cdd:TIGR00957 1291 CLRyREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQD-P 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 AAFPYSVRRMIE-LGRVPHTGLGSALR-AEDHAAVDHAMARLGLQ--EMAErpvtQLSGGERQRVVLARALAQEAKALLL 166
Cdd:TIGR00957 1370 VLFSGSLRMNLDpFSQYSDEEVWWALElAHLKTFVSALPDKLDHEcaEGGE----NLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 167 DEPMTGLDY-GHQLRLMSLLGEFaaEGRLILLTSHRPEELFaPASRVLVLDDGHIVADGLPQNVVTA 232
Cdd:TIGR00957 1446 DEATAAVDLeTDNLIQSTIRTQF--EDCTVLTIAHRLNTIM-DYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
22-224 |
7.26e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.37 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLkPDRGHvllegKPLGAYSASSVAQQLAYVPQSHTAAfpYSVRRMI 101
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGR-----RPWRF*TWCANRRALRRTIG*HRPV--R*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 ELGRVPHTGLGSAL---RAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:NF000106 101 FSGRENLYMIGR*LdlsRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:NF000106 181 NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-201 |
1.18e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.42 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 13 LRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassvaQQLAYVPQsHTAA 92
Cdd:PRK10636 9 IRRGVR-VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-----------WQLAWVNQ-ETPA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 93 FPYSVRRMIELGRVPHTGLGSALRAEDHAAVDHAMARL---------------------GL---QEMAERPVTQLSGGER 148
Cdd:PRK10636 76 LPQPALEYVIDGDREYRQLEAQLHDANERNDGHAIATIhgkldaidawtirsraasllhGLgfsNEQLERPVSDFSGGWR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 149 QRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFaaEGRLILLTSHR 201
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILISHDR 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-174 |
1.51e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGH-VLLEGKPLGaysassvaqqlaYVPQ------SHTaaf 93
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKVG------------YLPQepqldpEKT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 pysVRRMIELGRVPHTGLG------SALRAEDHAAVDHAMARLG-LQ---------------EMA---------ERPVTQ 142
Cdd:PRK11819 87 ---VRENVEEGVAEVKAALdrfneiYAAYAEPDADFDALAAEQGeLQeiidaadawdldsqlEIAmdalrcppwDAKVTK 163
|
170 180 190
....*....|....*....|....*....|..
gi 2035452788 143 LSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-174 |
1.73e-11 |
|
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: 63.80 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGhvllEGKPLGAYSASSVAQQlayvPQ---SHTaafpysV 97
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----EARPQPGIKVGYLPQE----PQldpTKT------V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIELGRVPHTGLG------SALRAEDHAAVDHAMARLG-LQ---------------EMA---------ERPVTQLSGG 146
Cdd:TIGR03719 86 RENVEEGVAEIKDALdrfneiSAKYAEPDADFDKLAAEQAeLQeiidaadawdldsqlEIAmdalrcppwDADVTKLSGG 165
|
170 180
....*....|....*....|....*...
gi 2035452788 147 ERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-218 |
1.86e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYS----ASSVAQQLAYVPQSHTAafpy 95
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSFML---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 svrrMIELGRVPHTGLGSALRAE-DHAAVDHA---MARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:PRK10584 100 ----IPTLNALENVELPALLRGEsSRQSRNGAkalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPeELFAPASRVLVLDDG 218
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREhGTTLILVTHDL-QLAARCDRRLRLVNG 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
128-248 |
2.42e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 128 ARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFA 207
Cdd:PRK10938 121 QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPD 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2035452788 208 PASRVLVLDDGHIVADG----LPQNVVTAE--HMSRLYGVSLKQVDH 248
Cdd:PRK10938 201 FVQFAGVLADCTLAETGereeILQQALVAQlaHSEQLEGVQLPEPDE 247
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-234 |
5.24e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 9 EGVCLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQ 87
Cdd:PLN03130 1241 EDVVLRyRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 ShTAAFPYSVRRMIE-LGRVPHTGLGSALraeDHAAVDHAMAR--LGLQ-EMAERPvTQLSGGERQRVVLARALAQEAKA 163
Cdd:PLN03130 1321 A-PVLFSGTVRFNLDpFNEHNDADLWESL---ERAHLKDVIRRnsLGLDaEVSEAG-ENFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 164 LLLDEPMTGLDYG-HQLRLMSLLGEFAAEGRLILltSHRPEELFaPASRVLVLDDGHIVADGLPQNVVTAEH 234
Cdd:PLN03130 1396 LVLDEATAAVDVRtDALIQKTIREEFKSCTMLII--AHRLNTII-DCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-221 |
5.35e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.65 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 23 DNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS---SVAQQLAYVPQSHTAAF-Pysvr 98
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDPLASLnP---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMI------ELGRVPHTGLGsalRAEDHAAVDHAMARLGLQE-MAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:PRK15079 114 RMTigeiiaEPLRTYHPKLS---RQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAEGRLILL-TSHRPEELFAPASRVLVLDDGHIV 221
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIfIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-221 |
7.19e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVL---------LEGKP-------LGAYSASSVAQQLAYV 85
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdlivarLQQDPprnvegtVYDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQ----SHTAAFPYSVRRMIELGRVP----HTGLgsaLRAEDHaaVDHAMARLGLQemAERPVTQLSGGERQRVVLARAL 157
Cdd:PRK11147 99 KRyhdiSHLVETDPSEKNLNELAKLQeqldHHNL---WQLENR--INEVLAQLGLD--PDAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 158 AQEAKALLLDEPMTGLDYGHQLRLMSLLGEFaaEGRLILLtSHRPEELFAPASRVLVLDDGHIV 221
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFI-SHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-220 |
7.54e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAysassvAQQLAYv 85
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA------EQPEDY- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 pQSHTAAFPYSVRRMIELgrvphtgLGSALRAEDHAAVDHAMARLGLQEMAERP-----VTQLSGGERQRVVLARALAQE 160
Cdd:PRK10522 396 -RKLFSAVFTDFHLFDQL-------LGPEGKPANPALVEKWLERLKMAHKLELEdgrisNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 161 AKALLLDEpmTGLDYGHQLR---LMSLLGEFAAEGRLILLTSHrPEELFAPASRVLVLDDGHI 220
Cdd:PRK10522 468 RDILLLDE--WAADQDPHFRrefYQVLLPLLQEMGKTIFAISH-DDHYFIHADRLLEMRNGQL 527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-201 |
1.05e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHV-LLEGKPLGAYsassvAQ-QL 82
Cdd:PRK10636 312 LLKMEKVSAGYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYF-----AQhQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 83 AYvpqshtaafpysvrrmielgrvphtglgsaLRAeDHAAVDHaMARLGLQEMAER-----------------PVTQLSG 145
Cdd:PRK10636 386 EF------------------------------LRA-DESPLQH-LARLAPQELEQKlrdylggfgfqgdkvteETRRFSG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 146 GERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFaaEGRLILLTSHR 201
Cdd:PRK10636 434 GEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDR 487
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-230 |
1.10e-10 |
|
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: 61.36 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 18 RGTV--LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHV----------LLEGKPLGAYSASS----VAQQ 81
Cdd:TIGR03269 294 RGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdMTKPGPDGRGRAKRyigiLHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 82 LAYVPQSH-----TAA----FPYSVRRMielgRVPHTgLGSALRAEDHAavdhamarlglQEMAERPVTQLSGGERQRVV 152
Cdd:TIGR03269 374 YDLYPHRTvldnlTEAigleLPDELARM----KAVIT-LKMVGFDEEKA-----------EEILDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 153 LARALAQEAKALLLDEPMTGLDYGHQLRLM-SLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVV 230
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-218 |
1.68e-10 |
|
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: 59.27 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 16 GSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYvPQSHTAAFPY 95
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRY-SVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 96 SVRRMIElgrvPHTGLGSALRAEDHAAVDHA--------MARLGLQ-EMAERPVtQLSGGERQRVVLARALAQEAKALLL 166
Cdd:cd03290 90 LLNATVE----ENITFGSPFNKQRYKAVTDAcslqpdidLLPFGDQtEIGERGI-NLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 167 DEPMTGLDYGHQLRLMS--LLGEFAAEGRLILLTSHRPEELfAPASRVLVLDDG 218
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-225 |
2.03e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.55 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 1 MNADLLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLL---EGKPLGAYSASS 77
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 78 VAQQL------AYVPQSHTAAFPYSV-------RRMIELGrVPHTGlgsALRAEdhaAVDHaMAR--LGLQEMAERPvTQ 142
Cdd:PRK11701 81 AERRRllrtewGFVHQHPRDGLRMQVsaggnigERLMAVG-ARHYG---DIRAT---AGDW-LERveIDAARIDDLP-TT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 143 LSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLaVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
....
gi 2035452788 222 ADGL 225
Cdd:PRK11701 232 ESGL 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-220 |
2.11e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQqlayvpqsHTAAFPYSVRRmi 101
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN--------HGFALVTEERR-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 elgrvpHTGLGSALRAEDH---AAVDHAMARLGL---QEMA-----------------ERPVTQLSGGERQRVVLARALA 158
Cdd:PRK10982 334 ------STGIYAYLDIGFNsliSNIRNYKNKVGLldnSRMKsdtqwvidsmrvktpghRTQIGSLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 159 QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHI 220
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-240 |
4.57e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.57 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGH-----VLLEGKPLGAYSASSVAQQLAYVPQSHTAAFP 94
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 YSVRRMIELGRVPHTGLGsalRAEDHAAVDHAMARLGLQE-----MAERPVtQLSGGERQRVVLARALAQEAKALLLDEP 169
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVP---RKEFRGVAQARLTEVGLWDavkdrLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 170 MTGLDYGHQLRLMSLLGEFAAEGRLILLTsHRPEELFAPASRVLVLDDGHIVADG-------LPQNVVTAEHMSRLYG 240
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVT-HNLAQAARISDRAALFFDGRLVEEGpteqlfsSPKHAETARYVAGLSG 267
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-224 |
5.03e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAS---SVAQQLAYVPQSHTAAFP---- 94
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDPYASLDprqt 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 --YSVrrmIELGRVPHTGLGSALRAEdhaaVDHAMARLGLQ-EMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMT 171
Cdd:PRK10261 420 vgDSI---MEPLRVHGLLPGKAAAAR----VAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 172 GLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIVADG 224
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-221 |
5.64e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.95 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 16 GSRGTVLDNVSVSLRAGELVGLLGLNGAGKS-TLLRILLGLLKPD----RGHVLLEGKPLGAYSASSVAQ----QLAYVP 86
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 87 QSHTAAFP--YSVRRMIELGRVPHTGLG-SALRAEDHAAVDHAMARLGLQEMAERPvTQLSGGERQRVVLARALAQEAKA 163
Cdd:PRK15134 99 QEPMVSLNplHTLEKQLYEVLSLHRGMRrEAARGEILNCLDRVGIRQAAKRLTDYP-HQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 164 LLLDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSHRPEELFAPASRVLVLDDGHIV 221
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-200 |
7.08e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKS-TLLRILLGLLKPDR--GHVLLEGKPLGAYSASSV----AQQLAYVPQS-HTA 91
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPEKELnklrAEQISMIFQDpMTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 92 AFPYsVRRMIELGRV--PHTGLGSALRAEDHA----AVDHAMARlglQEMAERPvTQLSGGERQRVVLARALAQEAKALL 165
Cdd:PRK09473 110 LNPY-MRVGEQLMEVlmLHKGMSKAEAFEESVrmldAVKMPEAR---KRMKMYP-HEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGEFAAE-GRLILLTSH 200
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-218 |
9.50e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKP---DRGHVLLEGKPLGaysaSSVAQQLAYVPQSHTAAFPYSV 97
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD----SSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 98 RRMIELG---RVPHtglgSALRAEDHAAVDHAMARLGLQEMAER----PVTQLSGGERQRVVLARALAQEAKALL-LDEP 169
Cdd:TIGR00956 854 RESLRFSaylRQPK----SVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2035452788 170 MTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPE-ELFAPASRVLVLDDG 218
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaILFEEFDRLLLLQKG 979
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-237 |
1.77e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDrGHVLLEGK----PLGAY----SASSVAQQLAYV-PQSHTa 91
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRveffNQNIYerrvNLNRLRRQVSMVhPKPNL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 92 aFPYSVRRMIELGrVPHTGLGSALRAED--HAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEP 169
Cdd:PRK14258 100 -FPMSVYDNVAYG-VKIVGWRPKLEIDDivESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 170 MTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEEL----------FAPASRVlvlddGHIVADGLPQNVVTAEHMSR 237
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELtMVIVSHNLHQVsrlsdftaffKGNENRI-----GQLVEFGLTKKIFNSPHDSR 251
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-219 |
2.07e-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: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassvaqqLAYVPQShTAAFPYSVRRM 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQT-SWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELG----RVPHTGLGSALRAEDHAAVdhaMARLGLQEMAERPVTqLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:TIGR01271 507 IIFGlsydEYRYTSVIKACQLEEDIAL---FPEKDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2035452788 177 HQLRLM-SLLGEFAAEGRLILLTSHRpeELFAPASRVLVLDDGH 219
Cdd:TIGR01271 583 TEKEIFeSCLCKLMSNKTRILVTSKL--EHLKKADKILLLHEGV 624
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
141-212 |
2.43e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 2.43e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 141 TQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTsHRPeelfAPASRV 212
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSP----AQAARV 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
111-226 |
3.44e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.58 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 111 LGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH--QLRL-MSLLGE 187
Cdd:PRK11000 102 LAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALrvQMRIeISRLHK 181
|
90 100 110
....*....|....*....|....*....|....*....
gi 2035452788 188 faAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLP 226
Cdd:PRK11000 182 --RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
140-213 |
5.47e-09 |
|
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: 53.90 E-value: 5.47e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 140 VTQLSGGERQRVVLARALAQEAKA----LLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPeELFAPASRVL 213
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKprplYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP-ELAELADKLI 151
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-214 |
6.04e-09 |
|
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: 56.49 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGkplgaysassvaqQLAYVPQSHTAAfPYSVRRMI 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQ-NDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 ELGRvphtglgsALRAEDHAAVDHAMARLGLQEM---------AERPVtQLSGGERQRVVLARALAQEAKALLLDEPMTG 172
Cdd:TIGR00957 720 LFGK--------ALNEKYYQQVLEACALLPDLEIlpsgdrteiGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2035452788 173 LDyghqlrlmsllgefAAEGRLILLTSHRPEELFAPASRVLV 214
Cdd:TIGR00957 791 VD--------------AHVGKHIFEHVIGPEGVLKNKTRILV 818
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
24-232 |
6.81e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 24 NVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPL--GAYSASSvaQQLAYVPQ-SHTAAFPYsvRRM 100
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDYSYRS--QRIRMIFQdPSTSLNPR--QRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRVP---HTGLGSALRAEdhaAVDHAMARLGL-QEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:PRK15112 107 SQILDFPlrlNTDLEPEQREK---QIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 177 HQLRLMSLLGEFAAEGRL--ILLTSHRpEELFAPASRVLVLDDGHIVADGLPQNVVTA 232
Cdd:PRK15112 184 MRSQLINLMLELQEKQGIsyIYVTQHL-GMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
116-174 |
7.25e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.62 E-value: 7.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 116 RAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PRK11650 108 KAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-174 |
8.39e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSAsSVAQQLAYVPQshtaAFP-Y--- 95
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDI-ATRRRVGYMSQ----AFSlYgel 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 96 SVRRMIELgrvpHTGLGSALRAEDHAAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:NF033858 355 TVRQNLEL----HARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-217 |
8.61e-09 |
|
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: 53.31 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVlleGKPLGAysassvaqQLAYV 85
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE--------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 86 PQShtaafPYsvrrmielgrvphtglgsalraedhaavdhaMARLGLQEMAERPVTQ-LSGGERQRVVLARALAQEAKAL 164
Cdd:cd03223 70 PQR-----PY-------------------------------LPLGTLREQLIYPWDDvLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 165 LLDEPMTGLDYGHQLRLMSLLGEfaaEGRLILLTSHRPeELFAPASRVLVLDD 217
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE---LGITVISVGHRP-SLWKFHDRVLDLDG 162
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-220 |
9.78e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.86 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDrGHVLLEGKPLGAYSASSVAQQLAYVPQS---HTAAF--- 93
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKvfiFSGTFrkn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 --PYSVRRMIELGRVP-HTGLGSalraedhaAVDHAMARLGLQEMAERPVtqLSGGERQRVVLARALAQEAKALLLDEPM 170
Cdd:cd03289 97 ldPYGKWSDEEIWKVAeEVGLKS--------VIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2035452788 171 TGLD-YGHQLRLMSLLGEFAaeGRLILLTSHRPEELFApASRVLVLDDGHI 220
Cdd:cd03289 167 AHLDpITYQVIRKTLKQAFA--DCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-203 |
1.24e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 10 GVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTllrillgllkpdrghvLLEgkplgaysasSVAQQLAYVPQSH 89
Cdd:COG2401 35 GVELRVVER-YVLRDLNLEIEPGEIVLIVGASGSGKST----------------LLR----------LLAGALKGTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 90 TAAFPYsvrrmIELGRVPhTGLGSALRAEDHAAVDHAMARLGLQEMA--ERPVTQLSGGERQRVVLARALAQEAKALLLD 167
Cdd:COG2401 88 CVDVPD-----NQFGREA-SLIDAIGRKGDFKDAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2035452788 168 EPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPE 203
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGItLVVATHHYD 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-221 |
1.46e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 19 GTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVllegkplgAYSASSvaqQLAYVPQSHTAAFPYSVR 98
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENA---NIGYYAQDHAYDFENDLT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 99 RMIELGRVPHTGlgsalraEDHAAVDHAMARLGL-QEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGH 177
Cdd:PRK15064 401 LFDWMSQWRQEG-------DDEQAVRGTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2035452788 178 QLRLMSLLGEFaaEGRLILLtSHRPEELFAPASRVLVLDDGHIV 221
Cdd:PRK15064 474 IESLNMALEKY--EGTLIFV-SHDREFVSSLATRIIEITPDGVV 514
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-174 |
1.80e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.89 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLrillgllkpdR---------------GHVLLEGKPL 70
Cdd:COG1117 12 IEVRNLNVYYGDK-QALKDINLDIPENKVTALIGPSGCGKSTLL----------RclnrmndlipgarveGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 71 gaYSAS----SVAQQLAYVPQSHTAaFPYSVRRMIELG-RVpHtglGSALRAEDHAAVDHAMARLGL-QEMAER---PVT 141
Cdd:COG1117 81 --YDPDvdvvELRRRVGMVFQKPNP-FPKSIYDNVAYGlRL-H---GIKSKSELDEIVEESLRKAALwDEVKDRlkkSAL 153
|
170 180 190
....*....|....*....|....*....|...
gi 2035452788 142 QLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-174 |
1.98e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKP-DRGHVLLEGKplgaysassvaqqLAYVPQShTAAFPYSVRRM 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT-------------VAYVPQV-SWIFNATVRDN 698
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 101 IELGrVPHTGlGSALRAEDHAAVDHAMARL---GLQEMAERPVtQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PLN03130 699 ILFG-SPFDP-ERYERAIDVTALQHDLDLLpggDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-206 |
3.09e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDrGHVLLEGKPLGAYSASSVAQQLAYVPQS---HTAAF--- 93
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKvfiFSGTFrkn 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 94 --PYSVRRMIELGRVP-HTGLGSALR----AEDHAAVDHAMArlglqemaerpvtqLSGGERQRVVLARALAQEAKALLL 166
Cdd:TIGR01271 1312 ldPYEQWSDEEIWKVAeEVGLKSVIEqfpdKLDFVLVDGGYV--------------LSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2035452788 167 DEPMTGLD-YGHQLRLMSLLGEFAaeGRLILLTSHRPEELF 206
Cdd:TIGR01271 1378 DEPSAHLDpVTLQIIRKTLKQSFS--NCTVILSEHRVEALL 1416
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-203 |
3.57e-08 |
|
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: 51.94 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTllrillgllkpdrghVLLEGkplgaysassVAQQLAYVPQSHTAAFPYSVRRMI 101
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEG----------LYASGKARLISFLPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 -ELGRVPHTGLGsalraedhaavdhaMARLGlqemaeRPVTQLSGGERQRVVLARALAQEAKALL--LDEPMTGLDYGHQ 178
Cdd:cd03238 66 dQLQFLIDVGLG--------------YLTLG------QKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQDI 125
|
170 180
....*....|....*....|....*
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPE 203
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-174 |
3.62e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 5 LLACEGVCLRRGSRgTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLgaySASSVAQQLAY 84
Cdd:PRK13543 11 LLAAHALAFSRNEE-PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VpqSHTAAFPYSVRRMIEL-------GRVPHTGLGSALraedhaavdhamARLGLQEMAERPVTQLSGGERQRVVLARAL 157
Cdd:PRK13543 87 L--GHLPGLKADLSTLENLhflcglhGRRAKQMPGSAL------------AIVGLAGYEDTLVRQLSAGQKKRLALARLW 152
|
170
....*....|....*..
gi 2035452788 158 AQEAKALLLDEPMTGLD 174
Cdd:PRK13543 153 LSPAPLWLLDEPYANLD 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-224 |
4.94e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEgkplgaysassvaQQLAYVPQsHTAAFPYSVRRM 100
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQ-QAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRVPHTG-LGSALRAEDHAAvDHAMARLGLQ-EMAERPVtQLSGGERQRVVLARALAQEAKALLLDEPMTGLD--YG 176
Cdd:PTZ00243 741 ILFFDEEDAArLADAVRVSQLEA-DLAQLGGGLEtEIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLSALDahVG 818
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2035452788 177 HQLRLMSLLGEFAAEGRliLLTSHRPeELFAPASRVLVLDDGHIVADG 224
Cdd:PTZ00243 819 ERVVEECFLGALAGKTR--VLATHQV-HVVPRADYVVALGDGRVEFSG 863
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-224 |
1.20e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKP-DRGHVLLEGkplgaysassvaqQLAYVPQShTAAFPYSVRRM 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG-------------SVAYVPQV-SWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGRVPHTGlgSALRAEDHAAVDHAMARLG---LQEMAERPVtQLSGGERQRVVLARALAQEAKALLLDEPMTGLD--Y 175
Cdd:PLN03232 699 ILFGSDFESE--RYWRAIDVTALQHDLDLLPgrdLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDahV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2035452788 176 GHQLRLMSLLGEFAAEGRlILLTShrpEELFAP-ASRVLVLDDGHIVADG 224
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTR-VLVTN---QLHFLPlMDRIILVSEGMIKEEG 821
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
129-173 |
1.54e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.95 E-value: 1.54e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2035452788 129 RLGlQemaerPVTQLSGGERQRVVLARALAQEA--KAL-LLDEPMTGL 173
Cdd:COG0178 819 KLG-Q-----PATTLSGGEAQRVKLASELSKRStgKTLyILDEPTTGL 860
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
142-232 |
3.54e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 142 QLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFA-AEGRLILLTSHRPEELFAPASRVLVLDDGHI 220
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
90
....*....|..
gi 2035452788 221 VADGLPQNVVTA 232
Cdd:PRK11022 233 VETGKAHDIFRA 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-174 |
3.74e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 59 DRGHVLLEGKPLGAYSASSVAQQLAYVPQsHTAAFPYSVRRMIELGRVPHTgLGSALRAEDHAAVDHAMARLGLQ-EMAE 137
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQ-EPMLFNMSIYENIKFGKEDAT-REDVKRACKFAAIDEFIESLPNKyDTNV 1352
|
90 100 110
....*....|....*....|....*....|....*...
gi 2035452788 138 RPVTQ-LSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PTZ00265 1353 GPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-218 |
4.39e-07 |
|
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: 49.86 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysaSSVAQQLAYVpqshtaaFPYSVRRM 100
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------ISFSSQFSWI-------MPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELG----RVPHTGLGSALRAEDHAAvdhAMARLGLQEMAERPVTqLSGGERQRVVLARALAQEAKALLLDEPMTGLDYG 176
Cdd:cd03291 118 IIFGvsydEYRYKSVVKACQLEEDIT---KFPEKDNTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2035452788 177 HQLRLM-SLLGEFAAEGRLILLTSHRpeELFAPASRVLVLDDG 218
Cdd:cd03291 194 TEKEIFeSCVCKLMANKTRILVTSKM--EHLKKADKILILHEG 234
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-200 |
5.58e-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: 5.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 129 RLGlqemaeRPVTQLSGGERQRVVLARALAQEAKA---LLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSH 200
Cdd:TIGR00630 822 RLG------QPATTLSGGEAQRIKLAKELSKRSTGrtlYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-174 |
6.78e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.00 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLK--PD---RGHVLLEGKPLGAYSASSVA--QQLAYVPQsHTAAFP 94
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTVDlrKEIGMVFQ-QPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 YSVRRMIELGrvphtglgsaLR---AEDHAAVDHAMARLGLQ-----EMAER---PVTQLSGGERQRVVLARALAQEAKA 163
Cdd:PRK14239 100 MSIYENVVYG----------LRlkgIKDKQVLDEAVEKSLKGasiwdEVKDRlhdSALGLSGGQQQRVCIARVLATSPKI 169
|
170
....*....|.
gi 2035452788 164 LLLDEPMTGLD 174
Cdd:PRK14239 170 ILLDEPTSALD 180
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-200 |
1.06e-06 |
|
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: 48.38 E-value: 1.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 138 RPVTQLSGGERQRVVLARALAQEA--KAL-LLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSH 200
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKRStgKTLyILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEH 230
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-231 |
1.25e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQshtaafpysvrrmI 101
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIEN-------------I 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 102 ELgrvphTGLGSALRAEDHAAVDHAM---ARLGlqEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQ 178
Cdd:PRK13545 107 EL-----KGLMMGLTKEKIKEIIPEIiefADIG--KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2035452788 179 LRLMSLLGEFAAEGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVT 231
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-223 |
1.58e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.64 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLR----RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAysassvAQQ 81
Cdd:COG4615 328 LELRGVTYRypgeDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA------DNR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 82 LAYvpQSHTAA-FP--YSVRRMIELGRVPhtglgsalraeDHAAVDHAMARLGLQEMaerpV---------TQLSGGERQ 149
Cdd:COG4615 402 EAY--RQLFSAvFSdfHLFDRLLGLDGEA-----------DPARARELLERLELDHK----VsvedgrfstTDLSQGQRK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 150 RVVLARALAQEAKALLLDE------PmtgldyghQLRLM---SLLGEFAAEGRLILLTSHrPEELFAPASRVLVLDDGHI 220
Cdd:COG4615 465 RLALLVALLEDRPILVFDEwaadqdP--------EFRRVfytELLPELKARGKTVIAISH-DDRYFDLADRVLKMDYGKL 535
|
...
gi 2035452788 221 VAD 223
Cdd:COG4615 536 VEL 538
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
133-232 |
1.76e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 133 QEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-ILLTSHRPEELFAPASR 211
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADR 238
|
90 100
....*....|....*....|.
gi 2035452788 212 VLVLDDGHIVADGLPQNVVTA 232
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQIFHA 259
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-234 |
2.75e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLK------PDR--------------------GH--VLLEGKPLGA 72
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvtADRmrfddidllrlsprerrklvGHnvSMIFQEPQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 73 YSAS-SVAQQLAYVPQSHT------AAFPYSVRRMIEL-GRVphtGLgsalraEDHAAVdhamarlglqeMAERPVtQLS 144
Cdd:PRK15093 102 LDPSeRVGRQLMQNIPGWTykgrwwQRFGWRKRRAIELlHRV---GI------KDHKDA-----------MRSFPY-ELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 145 GGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEF-AAEGRLILLTSHRPEELFAPASRVLVLDDGHIVAD 223
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250
....*....|.
gi 2035452788 224 GLPQNVVTAEH 234
Cdd:PRK15093 241 APSKELVTTPH 251
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-227 |
2.88e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 130 LGLQEMA-ERPVTQLSGGERQRVVLARALAQEAKAL--LLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRpEELF 206
Cdd:PRK00635 463 LGLPYLTpERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMI 541
|
90 100
....*....|....*....|....*..
gi 2035452788 207 APASRVLVLD------DGHIVADGLPQ 227
Cdd:PRK00635 542 SLADRIIDIGpgagifGGEVLFNGSPR 568
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
143-212 |
2.90e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.08 E-value: 2.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 143 LSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTsHRPEElfapASRV 212
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HNMQQ----AARV 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-231 |
3.62e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 20 TVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGllKPDRGHVLLEGKPlgAYSASSVAQ-------QLAYVPQSHTAa 92
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVI--TYDGITPEEikkhyrgDVVYNAETDVH- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 93 FPY-SVRRMIELG---RVPHT---GLGSALRAEDHAAVdhAMARLGLQEMAERPVTQ-----LSGGERQRVVLARALAQE 160
Cdd:TIGR00956 150 FPHlTVGETLDFAarcKTPQNrpdGVSREEYAKHIADV--YMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 161 AKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRL-----ILLTSHRPEELFapaSRVLVLDDGHIVADGLPQNVVT 231
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTtplvaIYQCSQDAYELF---DKVIVLYEGYQIYFGPADKAKQ 300
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
129-254 |
5.54e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.92 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 129 RLGLQEMAERPVTQLSGGERQRVVLA--RALAQEAKA-----LLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHR 201
Cdd:COG3593 149 SLRIEDGKELPLDRLGSGFQRLILLAllSALAELKRApanpiLLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHS 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452788 202 PE--ELFAPAS-RVLVLDDGHIVADGLPQNvvTAEHMSRLygvsLKQVDHEGSRFF 254
Cdd:COG3593 229 PHllSEVPLENiRRLRRDSGGTTSTKLIDL--DDEDLRKL----LRYLGVTRSELL 278
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
129-173 |
6.71e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 6.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2035452788 129 RLGlQemaerPVTQLSGGERQRVVLARALAQEA--KAL-LLDEPMTGL 173
Cdd:PRK00349 823 KLG-Q-----PATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGL 864
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-209 |
7.31e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGllkpDR-----GHVLLEGKPLGaySASSV---AQQLAYVPQS-Hta 91
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHpqgysNDLTLFGRRRG--SGETIwdiKKHIGYVSSSlH-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 92 aFPY----SVRRMIELGRVPHTGLGSALRAEDHAAVDHAMARLGL-QEMAERPVTQLSGGErQRVVL-ARALAQEAKALL 165
Cdd:PRK10938 347 -LDYrvstSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQ-QRLALiVRALVKHPTLLI 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2035452788 166 LDEPMTGLDYGHQLRLMSLLGEFAAEGRLILL-TSHRPEElfAPA 209
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAED--APA 467
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
136-200 |
8.72e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 8.72e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 136 AERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFaaEGRLiLLTSH 200
Cdd:PRK11147 434 AMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY--QGTV-LLVSH 495
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-200 |
1.31e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 125 HAMARLGLQEMA-ERPVTQLSGGERQRVVLARALAQEAKA---LLLDEPMTGLdYGHQLR-LMSLLGEFAAEGRLILLTS 199
Cdd:PRK00635 791 HALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELLAPSKKptlYVLDEPTTGL-HTHDIKaLIYVLQSLTHQGHTVVIIE 869
|
.
gi 2035452788 200 H 200
Cdd:PRK00635 870 H 870
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
141-201 |
2.20e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452788 141 TQLSGGERQRVVLARALAQEAKALLLDEPMTGLD----YGHQLRLMSLLGEfaaEGRLILLTSHR 201
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseYLVQKTINNLKGN---ENRITIIIAHR 639
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
134-222 |
2.74e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 134 EMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAaegRLILLTSHRPEELFAPASRVL 213
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNTVVTDIL 412
|
....*....
gi 2035452788 214 VLDDGHIVA 222
Cdd:PLN03073 413 HLHGQKLVT 421
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-216 |
4.72e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 13 LRRGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVllegkplgaysassvaqqlaYVPQSHT-- 90
Cdd:PRK13541 7 LQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI--------------------YYKNCNInn 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 91 AAFPYsvrrmieLGRVPHT-GLGSALRAEDH-----------AAVDHAMARLGLQEMAERPVTQLSGGERQRVVLARALA 158
Cdd:PRK13541 67 IAKPY-------CTYIGHNlGLKLEMTVFENlkfwseiynsaETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 159 QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEELfaPASRVLVLD 216
Cdd:PRK13541 140 CQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSI--KSAQILQLD 195
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-234 |
6.87e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 43.36 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKP------DRGHvlLEGKPLGAYSASS----VAQQLAYV---PQ 87
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtaDRFR--WNGIDLLKLSPRErrkiIGREIAMIfqePS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 88 ShtaafpySVRRMIELGR-----VPHTGLGSALRAEDHAAVDHAMA---RLGLQE----MAERPvTQLSGGERQRVVLAR 155
Cdd:COG4170 100 S-------CLDPSAKIGDqlieaIPSWTFKGKWWQRFKWRKKRAIEllhRVGIKDhkdiMNSYP-HELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 156 ALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAA-EGRLILLTSHRPEELFAPASRVLVLDDGHIVADGLPQNVVTAEH 234
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPH 251
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-230 |
7.73e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 6 LACEGVCLR-RGSRGTVLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAY 84
Cdd:PTZ00243 1309 LVFEGVQMRyREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 85 VPQShTAAFPYSVRRMIElgrvPHTglgSALRAEDHAAvdhamarLGLQEMAERPVTQLSG--------------GERQR 150
Cdd:PTZ00243 1389 IPQD-PVLFDGTVRQNVD----PFL---EASSAEVWAA-------LELVGLRERVASESEGidsrvleggsnysvGQRQL 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 151 VVLARALAQEAKA-LLLDEPMT----GLDYGHQLRLMSllgEFAAegRLILLTSHRPEELfAPASRVLVLDDGHIVADGL 225
Cdd:PTZ00243 1454 MCMARALLKKGSGfILMDEATAnidpALDRQIQATVMS---AFSA--YTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGS 1527
|
....*
gi 2035452788 226 PQNVV 230
Cdd:PTZ00243 1528 PRELV 1532
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-236 |
8.95e-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: 43.46 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 137 ERPVTQLSGGERQRVVLARALAQEAKALL--LDEPMTGLdygHQ---LRLMSLLGEFAAEGRLILLTSHrPEELFAPASR 211
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HQrdnRRLINTLKRLRDLGNTLIVVEH-DEDTIRAADY 558
|
90 100 110
....*....|....*....|....*....|....*..
gi 2035452788 212 VLVL------DDGHIVADGLPQNV------VTAEHMS 236
Cdd:TIGR00630 559 VIDIgpgageHGGEVVASGTPEEIlanpdsLTGQYLS 595
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-233 |
1.06e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.59 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 21 VLDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKPLGAYSASSVAQQLAYVPQShTAAFPYSVRRM 100
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQD-PILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 101 IELGR-VPHTGLGSALRAEDHAAVDHAMARlGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQL 179
Cdd:cd03288 115 LDPECkCTDDRLWEALEIAQLKNMVKSLPG-GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2035452788 180 RLMSLLGEFAAEgRLILLTSHRPEELFApASRVLVLDDGHIVADGLPQNVVTAE 233
Cdd:cd03288 194 ILQKVVMTAFAD-RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
137-203 |
1.28e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 1.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 137 ERPVTQLSGGERQRVVLARALA-----QEAK-----ALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPE 203
Cdd:cd03279 118 ARPVSTLSGGETFLASLSLALAlsevlQNRGgarleALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEE 194
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
137-203 |
1.83e-04 |
|
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: 41.47 E-value: 1.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035452788 137 ERPVTQLSGGERQRVVLARALAQEAKALL--LDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPE 203
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDED 200
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
137-205 |
2.82e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452788 137 ERPVTQLSGGERQ---RVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPEEL 205
Cdd:pfam13304 231 ELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-256 |
8.89e-04 |
|
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: 39.09 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 143 LSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRlilltshrpeelfapaSRVLVLDDGHIVA 222
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK----------------KTALVVEHDLAVL 135
|
90 100 110
....*....|....*....|....*....|....*.
gi 2035452788 223 DGLPQNVVTAEHMSRLYGVSLK-QVDHEG-SRFFTM 256
Cdd:cd03222 136 DYLSDRIHVFEGEPGVYGIASQpKGTREGiNRFLRG 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-201 |
1.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 138 RPVTQLSGGER-Q-----RVVLARALAQEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHR 201
Cdd:COG4717 554 RPVEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHE 623
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
136-203 |
2.09e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.18 E-value: 2.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452788 136 AERPVTQLSGGERQRVVLARALA------QEAKA----LLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPE 203
Cdd:TIGR00618 944 SVRPSATLSGGETFLASLSLALAladllsTSGGTvldsLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPE 1021
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-219 |
2.75e-03 |
|
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: 37.35 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 32 GELVGLLGLNGAGKSTllrillgllkpdrghvllegkplgaysassVAQQLAYvpqshtaAFPYSVRRMIELGrvphtgl 111
Cdd:smart00382 2 GEVILIVGPPGSGKTT------------------------------LARALAR-------ELGPPGGGVIYID------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 112 GSALRAEDHAavdhamarLGLQEMAERPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLDYGHQLRLM------SLL 185
Cdd:smart00382 38 GEDILEEVLD--------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 2035452788 186 GEFAAEGRLILLTSHR-----PEELFAPASRVLVLDDGH 219
Cdd:smart00382 110 LLKSEKNLTVILTTNDekdlgPALLRRRFDRRIVLLLIL 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-174 |
3.00e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 35 VGLLGLNGAGKSTLLRILLGLLKPDRGHVLLEGKplgaysassvaQQLAYVPQSHTAAFPYSVRRMIELGRVPHTGLGSA 114
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-----------VRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQK 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 115 LRAedHAAVDHAMARLGLQemaerPVTQLSGGERQRVVLARALAQEAKALLLDEPMTGLD 174
Cdd:PLN03073 607 LRA--HLGSFGVTGNLALQ-----PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
142-209 |
6.81e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.71 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 142 QLSGGERQ------RVVLARALAQ--EAKA----LLLDEPMTGLDYGHQLRLMSLLGEFAAEG-RLILLTSHrPEELFAP 208
Cdd:PRK02224 781 QLSGGERAlfnlslRCAIYRLLAEgiEGDAplppLILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSH-DDELVGA 859
|
.
gi 2035452788 209 A 209
Cdd:PRK02224 860 A 860
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
137-203 |
7.14e-03 |
|
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: 36.82 E-value: 7.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452788 137 ERPVTQLSGGERQ------RVVLARALAQEAKALLLDEPMTGLDYGH---QL-RLMSLLGEFaaEGRLILLTSHRPE 203
Cdd:cd03240 110 LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENieeSLaEIIEERKSQ--KNFQLIVITHDEE 184
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-174 |
7.90e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.18 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 24 NVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHVLLE-GKPLG-------AYSASSVaqqLAYVPQSHTAAFP- 94
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGklrqdqfAFEEFTV---LDTVIMGHTELWEv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 95 -------YSVRRMIElgrvpHTGLGSA-LRAEdHAAVD--HAMAR-----LGL---QEMAERPVTQLSGGERQRVVLARA 156
Cdd:PRK15064 96 kqerdriYALPEMSE-----EDGMKVAdLEVK-FAEMDgyTAEARagellLGVgipEEQHYGLMSEVAPGWKLRVLLAQA 169
|
170
....*....|....*...
gi 2035452788 157 LAQEAKALLLDEPMTGLD 174
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLD 187
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-63 |
8.20e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 36.72 E-value: 8.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2035452788 22 LDNVSVSLRAGELVGLLGLNGAGKSTLLRILLGLLKPDRGHV 63
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
132-211 |
9.56e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 36.13 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452788 132 LQEMAERpvtQLSGGERQRVVLARALA----QEAKALLLDEPMTGLDYGHQLRLMSLLGEFAAEGRLILLTSHRPeELFA 207
Cdd:cd03239 87 LQGKVEQ---ILSGGEKSLSALALIFAlqeiKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKK-EMFE 162
|
....
gi 2035452788 208 PASR 211
Cdd:cd03239 163 NADK 166
|
|
| |
