|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-233 |
2.60e-101 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 293.49 E-value: 2.60e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKstllsllsglQQPDSGKAIALGIDLSTFSRAAME 89
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKstllnilgglDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 90 RFRLEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAK 169
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 170 APKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQD 233
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-230 |
2.59e-94 |
|
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: 275.52 E-value: 2.59e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFR 92
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-237 |
1.47e-75 |
|
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: 228.47 E-value: 1.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 6 SHSSQPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSR 85
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 86 AAMERFRLEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVskRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIAR 165
Cdd:COG4181 82 DARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 166 AVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQDAQTS 237
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-235 |
8.72e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 210.68 E-value: 8.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERF 91
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RLeHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:COG2884 78 RR-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSHAD-RLLHMEDGAIQQDAQ 235
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPkRVLELEDGRLVRDEA 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-230 |
2.31e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 202.53 E-value: 2.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLsTFSRAAMERF 91
Cdd:COG1126 1 MIEIENLHKSF--GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RlEHTGFIFQGFNLFPSLTAIEQVQL-PMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKA 170
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 171 PKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDprlMSHA----DRLLHMEDGAI 230
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHE---MGFArevaDRVVFMDGGRI 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-230 |
9.08e-65 |
|
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: 200.89 E-value: 9.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 16 QDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRlEH 95
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR-RR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 TGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLF 175
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 176 ADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDprlM----SHADRLLHMEDGAI 230
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHE---MevvkRICDRVAVMEKGEV 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-230 |
1.81e-64 |
|
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: 199.68 E-value: 1.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLsTFSRAAMERFR 92
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lEHTGFIFQGFNLFPSLTAIEQVQL-PMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-238 |
4.59e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 189.50 E-value: 4.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMER 90
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 FRlEHTGFIFQGFNLFPSLTAIEQVQlpMGYLG--------VSKRTSEER--AMAALEDVGLSHRAHMYPAQLSGGEKQR 160
Cdd:COG3638 78 LR-RRIGMIFQQFNLVPRLSVLTNVL--AGRLGrtstwrslLGLFPPEDRerALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRL-MSHADRLLHMEDGAIQQDAQTSN 238
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLaRRYADRIIGLRDGRVVFDGPPAE 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-230 |
2.02e-59 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 190.67 E-value: 2.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 16 QDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLeH 95
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 TGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLF 175
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 176 ADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDprlMS----HADRLLHMEDGAI 230
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHE---MDvvrrICDRVAVLENGRI 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-230 |
1.69e-56 |
|
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: 179.62 E-value: 1.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAaMERF 91
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR-LRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RLEHTGFIFQ--GFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGL---SHRAHMYPAQLSGGEKQRVAIARA 166
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 167 VAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-228 |
2.02e-56 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 180.67 E-value: 2.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKstllsllsglQQPDSGKAIALGIDLSTFSRaa 87
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKstllrliaglEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 merfrleHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:COG1116 81 -------DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPR---LMshADRLLHMEDG 228
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-239 |
4.28e-56 |
|
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: 179.02 E-value: 4.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAA 87
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERFRLeHTGFIFQGFNLFPSLTAIEQVQLPMG-YLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARA 166
Cdd:COG1127 77 LYELRR-RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 167 VAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQ-----QDAQTSNH 239
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIaegtpEELLASDD 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-241 |
2.06e-55 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 187.24 E-value: 2.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMER 90
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 FRLEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKA 170
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 171 PKLLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQDAQTSNHKN 241
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVN 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-212 |
6.96e-55 |
|
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: 175.35 E-value: 6.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRaamerfr 92
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 leHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03293 74 --DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD 212
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-234 |
1.56e-54 |
|
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: 174.24 E-value: 1.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTfsRAAMERfr 92
Cdd:cd03259 1 LELKGLSKTY--GS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG--VPPERR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 leHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPR-LMSHADRLLHMEDGAIQQDA 234
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-232 |
3.12e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 177.60 E-value: 3.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFltGSltVPVLRHLSLTVNPGE-LTLIsGPSGCGKstllsllsglQQPDSGKaIAL-GIDLStfSRA 86
Cdd:COG3842 2 AMPALELENVSKRY--GD--VTALDDVSLSIEPGEfVALL-GPSGCGKttllrmiagfETPDSGR-ILLdGRDVT--GLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 87 AMERfrleHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARA 166
Cdd:COG3842 74 PEKR----NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 167 VAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPR-LMSHADRLLHMEDGAIQQ 232
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeALALADRIAVMNDGRIEQ 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
16-239 |
7.84e-54 |
|
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: 173.07 E-value: 7.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 16 QDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLeH 95
Cdd:cd03261 4 RGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 TGFIFQGFNLFPSLTAIEQVQLPM-GYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLL 174
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 175 FADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQ-----QDAQTSNH 239
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVaegtpEELRASDD 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-234 |
9.81e-53 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 170.34 E-value: 9.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAA 87
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERFRLEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQDA 234
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-230 |
1.37e-52 |
|
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: 170.06 E-value: 1.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFR 92
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lEHTGFIFQGFNLFPSLTAIEQVQLPM--------GYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIA 164
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 165 RAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRL-MSHADRLLHMEDGAI 230
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-233 |
1.48e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 169.89 E-value: 1.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 1 MVNFyshssqpvlqaQDISKSFltGslTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDL 80
Cdd:PRK09493 1 MIEF-----------KNVSKHF--G--PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 81 StfSRAAMER-FRLEhTGFIFQGFNLFPSLTAIEQVQL-PMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEK 158
Cdd:PRK09493 66 N--DPKVDERlIRQE-AGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 159 QRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDprlMSHA----DRLLHMEDGAIQQD 233
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHE---IGFAekvaSRLIFIDKGRIAED 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
12-228 |
5.25e-52 |
|
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: 167.81 E-value: 5.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERF 91
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RlEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIARtYGVTTLCVSHDPRLMSH-ADRLLHMEDG 228
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRvAHRVIILDDG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-230 |
8.72e-52 |
|
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: 175.48 E-value: 8.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 6 SHSSQPVLQAQDISKSF-LTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFS 84
Cdd:COG1123 254 AAAAEPLLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 85 RAAMERFRlEHTGFIFQgfN----LFPSLTAIEQVQLPMGYLGV-SKRTSEERAMAALEDVGLSHR-AHMYPAQLSGGEK 158
Cdd:COG1123 334 RRSLRELR-RRVQMVFQ--DpyssLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDlADRYPHELSGGQR 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 159 QRVAIARAVAKAPKLLFADEPTSALDAeSGQ-RVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDV-SVQaQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-233 |
3.94e-51 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 166.14 E-value: 3.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAA 87
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERFRLEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQD 233
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-230 |
1.48e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 165.36 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 14 QAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRl 93
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 94 EHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKL 173
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 174 LFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDprlM----SHADRLLHMEDGAI 230
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHE---MdvvkRICDRVAVIDAGRL 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-228 |
1.75e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 161.10 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 21 SFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAmerfRLEHTGFIF 100
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 101 QGFNL-FPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEP 179
Cdd:cd03225 82 QNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 942446941 180 TSALDAESGQRVINILHRIARTyGVTTLCVSHDP-RLMSHADRLLHMEDG 228
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLdLLLELADRVIVLEDG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
28-230 |
3.96e-49 |
|
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: 160.27 E-value: 3.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRlEHTGFIFQGFNLFP 107
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 108 SLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 188 GQRVINILHRIARTyGVTTLCVSHDPRLM-SHADRLLHMEDGAI 230
Cdd:cd03292 172 TWEIMNLLKKINKA-GTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-225 |
1.04e-48 |
|
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: 158.93 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 16 QDISKSFLTGSltvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLEH 95
Cdd:TIGR03608 2 KNISKKFGDKV----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 TGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLF 175
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 942446941 176 ADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSHADRLLHM 225
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-237 |
6.01e-48 |
|
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: 158.43 E-value: 6.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTfsRAAMERFR 92
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR--RRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 leHTGFIFQ----GFNlfPSLTAIEQVQLPMGYLGVSKRtsEERAMAALEDVGLSHR-AHMYPAQLSGGEKQRVAIARAV 167
Cdd:COG1124 80 --RVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPDR--EERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 168 AKAPKLLFADEPTSALDAeSGQ-RVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQDAQTS 237
Cdd:COG1124 154 ILEPELLLLDEPTSALDV-SVQaEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVA 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-236 |
6.51e-48 |
|
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: 165.08 E-value: 6.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSFLTGslTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPD---SGKAIALGIDLSTFSra 86
Cdd:COG1123 2 TPLLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 87 amERFRLEHTGFIFQGF--NLFPsLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIA 164
Cdd:COG1123 78 --EALRGRRIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 165 RAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQDAQT 236
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPP 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-237 |
6.76e-48 |
|
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: 158.23 E-value: 6.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERF 91
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RlEHTGFIFQGFNLFPSLTAIEQVQLP-MGY-------LGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAI 163
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGrLGYkptwrslLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 164 ARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRL-MSHADRLLHMEDGAIQQDAQTS 237
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLaKKYADRIVGLKAGEIVFDGAPS 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-225 |
3.57e-47 |
|
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: 158.68 E-value: 3.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSLTVPVLRHLSLTVNPGElTL-ISGPSGCGKSTLLSLLSGLQQP---DSGKAIALGIDLSTFSRAA 87
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGE-TLgLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERFRLEHTGFIFQG----FNlfPSLTAIEQVQLPMGY-LGVSKRTSEERAMAALEDVGLS---HRAHMYPAQLSGGEKQ 159
Cdd:COG0444 80 LRKIRGREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 160 RVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHM 225
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAVM 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-222 |
5.24e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 5.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSltVPVLRHLSLTVNPGELT-LIsGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERf 91
Cdd:COG1131 1 IEVRGLTKRY--GD--KTALDGVSLTVEPGEIFgLL-GPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 rlehTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:COG1131 75 ----IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHdprLMSHADRL 222
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTH---YLEEAERL 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-230 |
1.16e-45 |
|
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: 152.10 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfsRAAMERFR 92
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lEHTGFIFQgfN----LFpSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVA 168
Cdd:COG1122 75 -RKVGLVFQ--NpddqLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 169 KAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRL-MSHADRLLHMEDGAI 230
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLvAELADRVIVLDDGRI 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-232 |
5.48e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 151.07 E-value: 5.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKstllsllsglqQPDSGKaIAL-GIDLSTfSRAAMERf 91
Cdd:COG1118 3 IEVRNISKRF--GS--FTLLDDVSLEIASGELVALLGPSGSGKttllriiagleTPDSGR-IVLnGRDLFT-NLPPRER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 rleHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:COG1118 76 ---RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDP----RLmshADRLLHMEDGAIQQ 232
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQeealEL---ADRVVVMNQGRIEQ 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-233 |
7.65e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 151.25 E-value: 7.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGsltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSraA 87
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERfrleHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:PRK09452 84 ENR----HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPR---LMShaDRLLHMEDGAIQQD 233
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEealTMS--DRIVVMRDGRIEQD 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-230 |
6.10e-43 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.57 E-value: 6.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERF 91
Cdd:COG1120 1 MLEAENLSVGY--GG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RlehtGFIFQGFNLFPSLTAIEQVQL---P-MGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:COG1120 77 I----AYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRL-MSHADRLLHMEDGAI 230
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLLKDGRI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-230 |
5.47e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 5.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGsltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSraaMERFR 92
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lEHTGFIFQGFNLFPsltaiEQVQ--LPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPA-QLSGGEKQRVAIARAVAK 169
Cdd:COG4619 74 -RQVAYVPQEPALWG-----GTVRdnLPFPFQLRERKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 170 APKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPR-LMSHADRLLHMEDGAI 230
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-232 |
7.81e-42 |
|
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: 143.17 E-value: 7.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 15 AQDISKSFltgSLTVPVlRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLE 94
Cdd:cd03294 27 KEEILKKT---GQTVGV-NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 95 HTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLL 174
Cdd:cd03294 103 KISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 175 FADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDP----RLmshADRLLHMEDGAIQQ 232
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLdealRL---GDRIAIMKDGRLVQ 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-232 |
1.18e-41 |
|
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: 141.61 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 18 ISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALG----IDLSTFSRaamerfrl 93
Cdd:cd03300 6 VSKFY--GG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGE-ILLDgkdiTNLPPHKR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 94 eHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKL 173
Cdd:cd03300 73 -PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 174 LFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQ 232
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKIQQ 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-229 |
8.02e-41 |
|
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: 139.49 E-value: 8.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSF---LTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGkAIAL-----GIDLS 81
Cdd:COG4778 2 TTLLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG-SILVrhdggWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 82 TFSRAAMERFRLEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGL-SHRAHMYPAQLSGGEKQR 160
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRiARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGA 229
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-232 |
1.14e-40 |
|
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: 139.40 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLtvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfSRAAMERfr 92
Cdd:cd03296 3 IEVRNVSKRF--GDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQER-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 leHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSE----ERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVA 168
Cdd:cd03296 75 --NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 169 KAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQ 232
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqEEALEVADRVVVMNKGRIEQ 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-232 |
3.85e-40 |
|
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: 137.39 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfSRAAMERfr 92
Cdd:cd03301 1 VELENVTKRF--GN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 leHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03301 73 --DIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDP-RLMSHADRLLHMEDGAIQQ 232
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQvEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-230 |
1.36e-39 |
|
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: 136.41 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSraAMERFR 92
Cdd:cd03219 1 LEVRGLTKRF--GGLVA--LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP--PHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LehtGFI--FQGFNLFPSLTAIE------QVQLPMGYLGVSKRTSE----ERAMAALEDVGLSHRAHMYPAQLSGGEKQR 160
Cdd:cd03219 75 L---GIGrtFQIPRLFPELTVLEnvmvaaQARTGSGLLLARARREErearERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARtYGVTTLCVSHD-PRLMSHADRLLHMEDGAI 230
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-230 |
1.74e-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: 136.71 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGK---------STllsllsglqQPDSGKAIALGID 79
Cdd:COG0411 1 SDPLLEVRGLTKRF--GGLVA--VDDVSLEVERGEIVGLIGPNGAGKttlfnlitgFY---------RPTSGRILFDGRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 80 LStfSRAAMERFRLehtGFI--FQGFNLFPSLTAIEQVQLPM------GYLGVSKRTS---------EERAMAALEDVGL 142
Cdd:COG0411 68 IT--GLPPHRIARL---GIArtFQNPRLFPELTVLENVLVAAharlgrGLLAALLRLPrarreereaRERAEELLERVGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 143 SHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRL-MSHADR 221
Cdd:COG0411 143 ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLvMGLADR 222
|
....*....
gi 942446941 222 LLHMEDGAI 230
Cdd:COG0411 223 IVVLDFGRV 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-232 |
5.12e-39 |
|
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: 135.12 E-value: 5.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 16 QDISKSFLTGSltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleH 95
Cdd:cd03295 4 ENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 TGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGL--SHRAHMYPAQLSGGEKQRVAIARAVAKAPKL 173
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 174 LFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDP----RLmshADRLLHMEDGAIQQ 232
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIdeafRL---ADRIAIMKNGEIVQ 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
31-232 |
6.81e-39 |
|
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: 134.77 E-value: 6.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSrAAMERFrlehtGFIFQGFNLFPSLT 110
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRDI-----SYVPQNYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 AIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQR 190
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 942446941 191 VINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQ 232
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQ 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
31-236 |
1.01e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.88 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALG---IDLS---TFSRAAMERFRlEHTGFIFQGFN 104
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGT-IRVGditIDTArslSQQKGLIRQLR-QHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 105 LFPSLTAIEQV-QLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSAL 183
Cdd:PRK11264 96 LFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 184 DAESGQRVINILHRIARTyGVTTLCVSHDprlMSH----ADRLLHMEDGAI--QQDAQT 236
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQE-KRTMVIVTHE---MSFardvADRAIFMDQGRIveQGPAKA 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-241 |
1.40e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.99 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGK-AIA-LGIDLSTFSRAAMERFRLEHTGFIFQGFNLFPS 108
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlNIAgNHFDFSKTPSDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQ-VQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK11124 97 LTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 188 GQRVINILHRIARTyGVTTLCVSHDPRLMSH-ADRLLHMEDGAI--QQDA------QTSNHKN 241
Cdd:PRK11124 177 TAQIVSIIRELAET-GITQVIVTHEVEVARKtASRVVYMENGHIveQGDAscftqpQTEAFKN 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-228 |
2.11e-38 |
|
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: 131.54 E-value: 2.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTgsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFR 92
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 leHTGFIFQGFNLFPSLTAIEQVQLPmgylgvskrtseeramaaledvglshrahmypaqLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03229 77 --RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDG 228
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-232 |
6.97e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 135.20 E-value: 6.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKstllsllsglqQPDSGKaIAL-GIDLSTfsRAAMERf 91
Cdd:COG3839 4 LELENVSKSY--GG--VEALKDIDLDIEDGEFLVLLGPSGCGKstllrmiagleDPTSGE-ILIgGRDVTD--LPPKDR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 rleHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:COG3839 76 ---NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPR-LMSHADRLLHMEDGAIQQ 232
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVeAMTLADRIAVMNDGRIQQ 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-230 |
1.56e-37 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 131.29 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALG--IDLSTFSRAAMER 90
Cdd:COG4161 3 IQLKNINCFY--GS--HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 FRLEHTGFIFQGFNLFPSLTAIEQ-VQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAK 169
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 170 APKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKvASQVVYMEKGRI 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-230 |
4.04e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 4.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKstllsllsglQQPDSGKAIALGIDLstfsraa 87
Cdd:COG1121 2 MMMPAIELENLTVSY--GG--RPVLEDVSLTIPPGEFVAIVGPNGAGKstllkailglLPPTSGTVRLFGKPP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 meRFRLEHTGFIFQGFNL---FPsLTAIEQVQL----PMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQR 160
Cdd:COG1121 71 --RRARRRIGYVPQRAEVdwdFP-ITVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARtYGVTTLCVSHDP-RLMSHADRLLHMEDGAI 230
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLgAVREYFDRVLLLNRGLV 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-225 |
6.36e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.16 E-value: 6.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSF-LTGSL---TVPVLR---HLSLTVNPGElTL-ISGPSGCGKSTLLSLLSGLQQPDSGKAIALGID 79
Cdd:COG4608 3 MAEPLLEVRDLKKHFpVRGGLfgrTVGVVKavdGVSFDIRRGE-TLgLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 80 LSTFSRAAMERFRLeHTGFIFQgfN----LFPSLTAIEQVQLPMGYLGV-SKRTSEERAMAALEDVGLShRAHM--YPAQ 152
Cdd:COG4608 82 ITGLSGRELRPLRR-RMQMVFQ--DpyasLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLR-PEHAdrYPHE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAeSGQ-RVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHM 225
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDV-SIQaQVLNLLEDLQDELGLTYLFISHDLSVVRHiSDRVAVM 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-181 |
9.13e-37 |
|
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: 126.61 E-value: 9.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQGFNLFPSLTA 111
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 112 IEQVQLPMGYLGVSKRTSEERAMAALEDVGLSH----RAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTS 181
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-234 |
2.42e-36 |
|
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: 127.41 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 33 RHLSLTVN-----PGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIAL----------GIDLSTFSRaamerfrleHTG 97
Cdd:cd03297 9 RLPDFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGT-IVLngtvlfdsrkKINLPPQQR---------KIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 98 FIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALedVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFAD 177
Cdd:cd03297 79 LVFQQYALFPHLNVRENLAFGLKRKRNREDRISVDELLDL--LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 178 EPTSALDAESGQRVINILHRIARTYGVTTLCVSHDP-RLMSHADRLLHMEDGAIQQDA 234
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-228 |
2.70e-36 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 125.96 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 21 SFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIF 100
Cdd:cd03228 7 SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK----NIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 101 QGFNLFpSLTAIEQVqlpmgylgvskrtseeramaaledvglshrahmypaqLSGGEKQRVAIARAVAKAPKLLFADEPT 180
Cdd:cd03228 83 QDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 942446941 181 SALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDG 228
Cdd:cd03228 125 SALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-229 |
3.48e-36 |
|
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: 126.82 E-value: 3.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLstfsRAAMER 90
Cdd:COG4133 1 MMLEAENLSCRR--GE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 FRlEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVskRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKA 170
Cdd:COG4133 73 YR-RRLAYLGHADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 171 PKLLFADEPTSALDAESGQRVINILHRiARTYGVTTLCVSHDPrLMSHADRLLHMEDGA 229
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQP-LELAAARVLDLGDFK 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-228 |
1.19e-35 |
|
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: 123.89 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 14 QAQDISKSFLTGsltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrl 93
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 94 eHTGFIFQgfnlfpsltaieqvqlpmgylgvskrtseeramaaledvglshrahmypaqLSGGEKQRVAIARAVAKAPKL 173
Cdd:cd00267 74 -RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 174 LFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSHA-DRLLHMEDG 228
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
30-233 |
1.63e-35 |
|
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: 133.04 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIAL-GIDLSTFSRAAMERfrleHTGFIFQGFNLFpS 108
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR-ILIdGIDLRQIDPASLRR----QIGVVLQDVFLF-S 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLpmgylgVSKRTSEERAMAALEDVGLSH--RAHmyP-----------AQLSGGEKQRVAIARAVAKAPKLLF 175
Cdd:COG2274 563 GTIRENITL------GDPDATDEEIIEAARLAGLHDfiEAL--PmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 176 ADEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAIQQD 233
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-233 |
2.95e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.04 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMER 90
Cdd:PRK13548 1 AMLEARNLSVRL--GG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 FRlehtGFIFQGFNL-FPsLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVA- 168
Cdd:PRK13548 77 RR----AVLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 169 -----KAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQD 233
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVAD 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-232 |
4.98e-35 |
|
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: 131.03 E-value: 4.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAA 87
Cdd:COG4988 332 AGPPSIELEDVSFSYPGG---RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 -MERF-RLEHTGFIFQG---FNLfpsltaieqvqlpmgyLGVSKRTSEERAMAALEDVGLSHRAHMYP-----------A 151
Cdd:COG4988 409 wRRQIaWVPQNPYLFAGtirENL----------------RLGRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 152 QLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAIQ 231
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIV 550
|
.
gi 942446941 232 Q 232
Cdd:COG4988 551 E 551
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-232 |
9.83e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 127.12 E-value: 9.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 18 ISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSraAMERfrleHTG 97
Cdd:PRK10851 8 IKKSF--GR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH--ARDR----KVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 98 FIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTS----EERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKL 173
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTVLPRRERPNaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 174 LFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQ 232
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNIEQ 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-230 |
3.01e-34 |
|
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: 123.04 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMerf 91
Cdd:COG4555 1 MIEVENLSKKY--GK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 rlEHTGFIFQGFNLFPSLTAIEQVQlpmgYL----GVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:COG4555 74 --RQIGVLPDERGLYDRLTVRENIR----YFaelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEAlCDRVVILHKGKV 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-212 |
3.13e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 123.43 E-value: 3.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALGIDLSTFSRAamER 90
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGE-ITLDGVPVTGPGA--DR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 frlehtGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKA 170
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 942446941 171 PKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD 212
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-228 |
8.44e-34 |
|
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: 119.81 E-value: 8.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGslTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFr 92
Cdd:cd03230 1 IEVRNLSKRY--G--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lehtGFIFQGFNLFPSLTAIEQVqlpmgylgvskrtseeramaaledvglshrahmypaQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03230 76 ----GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSH-ADRLLHMEDG 228
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
30-230 |
1.02e-33 |
|
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: 119.85 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRlehtGFIFQgfnlfpsl 109
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI----AYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 taieqvqlpmgylgvskrtseeramaALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQ 189
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 942446941 190 RVINILHRIARTYGVTTLCVSHDPRL-MSHADRLLHMEDGAI 230
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDLNLaARYADRVILLKDGRI 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-230 |
1.24e-33 |
|
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: 126.72 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGElTL-ISGPSGCGKSTLLSLL-----SGLQQPdSGKAIALGIDLS 81
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGE-TLaLVGESGSGKSVTALSIlrllpDPAAHP-SGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 82 TFSRAAMERFRLEHTGFIFQ----GFNlfPSLTAIEQVQLPMG-YLGVSKRTSEERAMAALEDVGLSH---RAHMYPAQL 153
Cdd:COG4172 80 GLSERELRRIRGNRIAMIFQepmtSLN--PLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDperRLDAYPHQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 154 SGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEI 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-230 |
1.42e-33 |
|
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: 121.77 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDlsTFSRAAMERFRlEHTGFIFQG-FNLF 106
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIR-KKVGMVFQNpDNQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 PSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAE 186
Cdd:TIGR04520 91 VGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 187 SGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:TIGR04520 171 GRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-237 |
2.83e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.24 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 34 HLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRA----AMerfrlehtgfIFQGFNLFPSL 109
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpvSM----------LFQENNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVqlpmgYLGVS---KRTSEERA--MAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALD 184
Cdd:COG3840 87 TVAQNI-----GLGLRpglKLTAEQRAqvEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 942446941 185 AESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQDAQTS 237
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTA 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-232 |
3.68e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 125.65 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAA 87
Cdd:COG4987 329 PGGPSLELEDVSFRYPGAG--RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERfrleHTGFIFQGFNLFPS------LTAIEQVqlpmgylgvskrtSEERAMAALEDVGLSHRAHMYP----------- 150
Cdd:COG4987 407 LRR----RIAVVPQRPHLFDTtlrenlRLARPDA-------------TDEELWAALERVGLGDWLAALPdgldtwlgegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 151 AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRI 547
|
..
gi 942446941 231 QQ 232
Cdd:COG4987 548 VE 549
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
32-228 |
5.78e-33 |
|
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: 119.11 E-value: 5.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfsRAAMERFrlehtgFIFQGFNLFPSLTA 111
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT---EPGPDRM------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 112 IEQVQLPMGYLGVSKRTSEERAMAA--LEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQ 189
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAIVEehIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 942446941 190 RVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDG 228
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-230 |
6.04e-33 |
|
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: 124.80 E-value: 6.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLT--GSL--TVPVLR---HLSLTVNPGElTL-ISGPSGCGKSTLLSLLSGLQqPDSGKAIALGID 79
Cdd:COG4172 271 DAPPLLEARDLKVWFPIkrGLFrrTVGHVKavdGVSLTLRRGE-TLgLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 80 LSTFSRAAMERFRlEHTGFIFQ----GFNlfPSLTAIEQVQLPMG--YLGVSKRTSEERAMAALEDVGLSHRA-HMYPAQ 152
Cdd:COG4172 349 LDGLSRRALRPLR-RRMQVVFQdpfgSLS--PRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAArHRYPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD---PRLMSHadRLLHMEDGA 229
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlavVRALAH--RVMVMKDGK 503
|
.
gi 942446941 230 I 230
Cdd:COG4172 504 V 504
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-233 |
1.36e-32 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 119.01 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfsrAAMERFR 92
Cdd:PRK11247 13 LLLNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA----EAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LehtgfIFQGFNLFPSLTAIEQVQLPMgylgvsKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:PRK11247 85 L-----MFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQD 233
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKIGLD 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-228 |
2.45e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 117.28 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 16 QDISKSFLTGSltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRlEH 95
Cdd:PRK10908 5 EHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 TGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLF 175
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 942446941 176 ADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSHAD-RLLHMEDG 228
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-237 |
3.37e-32 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 117.28 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGK-----STLLSLLSGLQQPDSGKAIALGIDLSTFSRAA 87
Cdd:cd03260 1 IELRDLNVYY--GDKHA--LKDISLDIPKGEITALIGPSGCGKstllrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 ME-RFRLehtGFIFQGFNLFPsLTAIEQVQLPMGYLGVSKRTS-EERAMAALEDVGL----SHRAHmyPAQLSGGEKQRV 161
Cdd:cd03260 77 LElRRRV---GMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALwdevKDRLH--ALGLSGGQQQRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 162 AIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYgvTTLCVSHDP----RLmshADRLLHMEDGAIQQDAQTS 237
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMqqaaRV---ADRTAFLLNGRLVEFGPTE 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-235 |
3.39e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 117.12 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISksFLTGslTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRaam 88
Cdd:PRK10247 4 NSPLLQLQNVG--YLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 89 ERFRlEHTGFIFQGFNLFPSlTAIEQVQLPmgYLgVSKRTSEERAMAA-LEDVGLSHRAHMYP-AQLSGGEKQRVAIARA 166
Cdd:PRK10247 77 EIYR-QQVSYCAQTPTLFGD-TVYDNLIFP--WQ-IRNQQPDPAIFLDdLERFALPDTILTKNiAELSGGEKQRISLIRN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 167 VAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHME-DGAIQQDAQ 235
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQpHAGEMQEAR 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-233 |
9.06e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.99 E-value: 9.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPD------SGKAIALGID----LSTFSRAAMERFRLEHTgFIF 100
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSegsivvNGQTINLVRDkdgqLKVADKNQLRLLRTRLT-MVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 101 QGFNLFPSLTAIEQV-QLPMGYLGVSKRTSEERAMAALEDVGLSHRAHM-YPAQLSGGEKQRVAIARAVAKAPKLLFADE 178
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 179 PTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQD 233
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-231 |
1.27e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.37 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISksFLTGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFR 92
Cdd:COG4559 2 LEAENLS--VRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 ---LEHTGFIFqgfnlfpSLTAIEQVQlpMGYLGVSKRTSEER--AMAALEDVGLSHRAH-MYPaQLSGGEKQRVAIARA 166
Cdd:COG4559 78 avlPQHSSLAF-------PFTVEEVVA--LGRAPHGSSAAQDRqiVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 167 -------VAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQ 231
Cdd:COG4559 148 laqlwepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQyADRILLLHQGRLV 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
30-225 |
1.36e-31 |
|
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: 115.32 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDlstfsrAAMERFRLehtGFIFQGFNL---F 106
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP------LEKERKRI---GYVPQRRSIdrdF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 PsLTAIEQVQL----PMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSA 182
Cdd:cd03235 84 P-ISVRDVVLMglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 183 LDAESGQRVINILHRIARtYGVTTLCVSHDPR-LMSHADRLLHM 225
Cdd:cd03235 163 VDPKTQEDIYELLRELRR-EGMTILVVTHDLGlVLEYFDRVLLL 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-230 |
7.26e-31 |
|
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: 114.90 E-value: 7.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSLT-----VPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRA 86
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 87 AMERFRLEhTGFIFQ----GFNlfPSLTAIEQVQLPM-GYLGVSKRTSEERAMAALEDVGL-SHRAHMYPAQLSGGEKQR 160
Cdd:TIGR02769 82 QRRAFRRD-VQLVFQdspsAVN--PRMTVRQIIGEPLrHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLM-SHADRLLHMEDGAI 230
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQI 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-231 |
8.85e-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: 116.35 E-value: 8.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 36 SLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIAL----------GIDLSTfsraamERFRLehtGFIFQGFNL 105
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGR-IRLggevlqdsarGIFLPP------HRRRI---GYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 106 FPSLTAIEQVQLPMgylgvsKRTSEERAMAALEDV----GLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTS 181
Cdd:COG4148 89 FPHLSVRGNLLYGR------KRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 942446941 182 ALDAESGQRVINILHRIARTYGVTTLCVSHDP----RLmshADRLLHMEDGAIQ 231
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHSLdevaRL---ADHVVLLEQGRVV 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-237 |
2.06e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.63 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTGSLTVP-----VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSR 85
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 86 AAMERFRLEhTGFIFQ----GFNlfPSLTAIEQVQLPMGYL-GVSKRTSEERAMAALEDVGLSHR-AHMYPAQLSGGEKQ 159
Cdd:PRK10419 82 AQRKAFRRD-IQMVFQdsisAVN--PRKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 160 RVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQDAQTS 237
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVG 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-232 |
4.97e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 114.93 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 7 HSSQPVLQAQDISKSFlTGSLTVPvlrHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLS---TF 83
Cdd:PRK11607 14 KALTPLLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLShvpPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 84 SRAamerfrlehTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAI 163
Cdd:PRK11607 90 QRP---------INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 164 ARAVAKAPKLLFADEPTSALDAESGQR----VINILHRIartyGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQ 232
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV----GVTCVMVTHDqEEAMTMAGRIAIMNRGKFVQ 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-241 |
5.41e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 112.41 E-value: 5.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSFLTGSltvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDS---GKAIALGIDLSTFSRA 86
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 87 AME-RFRLEHTGFIFQGFNLFPSLTAIEQVQLpmGYLGVS----------KRTSEERAMAALEDVGLSHRAHMYPAQLSG 155
Cdd:PRK09984 78 ARDiRKSRANTGYIFQQFNLVNRLSVLENVLI--GALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 156 GEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQDA 234
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHVFYDG 235
|
....*..
gi 942446941 235 QTSNHKN 241
Cdd:PRK09984 236 SSQQFDN 242
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-228 |
2.12e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 112.90 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 35 LSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIAL----------GIDLSTFSRAamerfrlehTGFIFQGFN 104
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGE-IVLngrtlfdsrkGIFLPPEKRR---------IGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 105 LFPSLTAIEQvqLPMGY---LGVSKRTSEERAMAALedvGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTS 181
Cdd:TIGR02142 86 LFPHLSVRGN--LRYGMkraRPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 942446941 182 ALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDG 228
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDG 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-230 |
2.19e-29 |
|
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: 108.46 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISksFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRaamERFR 92
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP---NELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lEHTGFIFQGFNLFPSlTAIEQVqlpmgylgvskrtseeramaaledvglshrahmypaqLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03246 76 -DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 173 LLFADEPTSALDAEsGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:cd03246 117 ILVLDEPNSHLDVE-GERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-230 |
2.30e-29 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 111.00 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRlEHTGFIFQgfnlFPslta 111
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQ----FP---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 112 iEQvQL------------PMGyLGVSKRTSEERAMAALEDVGLS----HRAhmyPAQLSGGEKQRVAIARAVAKAPKLLF 175
Cdd:TIGR04521 92 -EH-QLfeetvykdiafgPKN-LGLSEEEAEERVKEALELVGLDeeylERS---PFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 176 ADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDprlMSH----ADRLLHMEDGAI 230
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHS---MEDvaeyADRVIVMHKGKI 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
30-212 |
2.55e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 110.56 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaiaLGIDLSTFSRAAMERfrlehtGFIFQGFNLFPSL 109
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS---ITLDGKPVEGPGAER------GVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQ 189
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|...
gi 942446941 190 RVINILHRIARTYGVTTLCVSHD 212
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHD 188
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-232 |
3.47e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.20 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLEHTGFIFQGFNLFPSLTA 111
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 112 IEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRV 191
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 942446941 192 INILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQ 232
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQ 245
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
30-230 |
2.04e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.57 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKstllsllsglqQPDSGKaIAL-GIDLSTFSRAAmerFRlEHTGFIFQGFNLFpS 108
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKstlvnlllrfyDPTSGR-ILIdGVDIRDLTLES---LR-RQIGVVPQDTFLF-S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLpmGYLGVSkrtsEERAMAALEDVGLSHRAHMYP-----------AQLSGGEKQRVAIARAVAKAPKLLFAD 177
Cdd:COG1132 428 GTIRENIRY--GRPDAT----DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 178 EPTSALDAESGQRVINILHRIARtyGVTTLCVSHdpRLMS--HADRLLHMEDGAI 230
Cdd:COG1132 502 EATSALDTETEALIQEALERLMK--GRTTIVIAH--RLSTirNADRILVLDDGRI 552
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
30-227 |
2.05e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.80 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPD---SGKAIALGIDLSTfsRAAMERfrleHTGFIFQGFNLF 106
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA--LPAEQR----RIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 PSLTAIEQVQ--LPMGylgVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALD 184
Cdd:COG4136 89 PHLSVGENLAfaLPPT---IGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 942446941 185 AESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMED 227
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
29-232 |
3.04e-28 |
|
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: 107.24 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 29 VPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRaameRFRLEHTGFIFQGFNLFpS 108
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNL----RWLRSQIGLVSQEPVLF-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLpmgylGVSKRTSEERAMAA-----------LEDvGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFAD 177
Cdd:cd03249 91 GTIAENIRY-----GKPDATDEEVEEAAkkanihdfimsLPD-GYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 178 EPTSALDAESGQRVINILHRIARtyGVTTLCVSHdpRL--MSHADRLLHMEDGAIQQ 232
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMK--GRTTIVIAH--RLstIRNADLIAVLQNGQVVE 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-230 |
3.19e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGK---------------A 73
Cdd:COG1129 1 AEPLLEMRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEilldgepvrfrsprdA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 74 IALGIdlstfsraamerfrlehtGFIFQGFNLFPSLTAIEQV---QLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYP 150
Cdd:COG1129 77 QAAGI------------------AIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 151 AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHdpRL---MSHADRLLHMED 227
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISH--RLdevFEIADRVTVLRD 215
|
...
gi 942446941 228 GAI 230
Cdd:COG1129 216 GRL 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-228 |
3.46e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.82 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLsllsglqqpdsgKAIAlgiDLSTFSRAAMERFRLEHTGFIFQgfnlfpsl 109
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLL------------RAIA---GLWPYGSGRIARPAGARVLFLPQ-------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 taieQVQLPMG-------YLGVSKRTSEERAMAALEDVGLSHRAHMY------PAQLSGGEKQRVAIARAVAKAPKLLFA 176
Cdd:COG4178 434 ----RPYLPLGtlreallYPATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 942446941 177 DEPTSALDAESGQRVINILHRiaRTYGVTTLCVSHDPRLMSHADRLLHMEDG 228
Cdd:COG4178 510 DEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-233 |
4.83e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 105.74 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSltvpVLRHLSLTVNPGELTLIsGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLstfsRAAMERFR 92
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lEHTGFIFQGFNLFPSLTAIEQVQLpMGYL-GVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDY-IAWLkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIA--RTYGVTTLCVShDprLMSHADRLLHMEDGAIQQD 233
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGedRIVILSTHIVE-D--VESLCNQVAVLNKGKLVFE 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-230 |
5.67e-28 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.42 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 14 QAQDISKSFLTGSLtvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfsraamERFRL 93
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 94 EHTGFIFQ--GFNLFpSLTAIEQVqlpmgYLGvSKRTSE--ERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAK 169
Cdd:cd03226 71 KSIGYVMQdvDYQLF-TDSVREEL-----LLG-LKELDAgnEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 170 APKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-234 |
6.13e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.65 E-value: 6.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfSRAAMERfr 92
Cdd:PRK11432 7 VVLKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 leHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:PRK11432 79 --DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDprlMSHA----DRLLHMEDGAIQQDA 234
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD---QSEAfavsDTVIVMNKGKIMQIG 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-222 |
1.59e-27 |
|
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: 104.76 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFr 92
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lehtGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03266 81 ----GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSHdprLMSHADRL 222
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTH---IMQEVERL 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-225 |
2.54e-27 |
|
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: 109.30 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGkAIAL-GIDLSTFSRAamerFRLEHTGFIFQGFNLFPS 108
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG-SIAVnGVPLADADAD----SWRDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 lTAIEQVQLPMGYL------GVSKRTSEERAMAALEDvGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSA 182
Cdd:TIGR02857 411 -TIAENIRLARPDAsdaeirEALERAGLDEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 942446941 183 LDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHM 225
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
30-233 |
7.31e-27 |
|
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: 103.63 E-value: 7.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIAL------GIDLST-------FSRAAMERFRLEHT 96
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfgerrgGEDVWElrkriglVSPALQLRFPRDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 97 GF--IFQGFNlfpsltaieqvqlpmGYLGVSKRTSEE---RAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:COG1119 97 VLdvVLSGFF---------------DSIGLYREPTDEqreRARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD----PRLMSHAdrlLHMEDGAIQQD 233
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHveeiPPGITHV---LLLKDGRVVAA 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-222 |
9.51e-27 |
|
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: 102.83 E-value: 9.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFr 92
Cdd:cd03265 1 IEVENLVKKY--GDFEA--VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lehtGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03265 76 ----GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDprlMSHADRL 222
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHY---MEEAEQL 198
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
30-223 |
1.92e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSG-------KAIALGIDLSTFSRAamerfrlehtgfifqg 102
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGtvrraggARVAYVPQRSEVPDS---------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 103 fnlFPsLTAIEQVQL----PMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADE 178
Cdd:NF040873 70 ---LP-LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 942446941 179 PTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSHADRLL 223
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-230 |
2.58e-26 |
|
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: 101.58 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMerf 91
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 rLEHTGFIFQGFNLFPSLTAIEQ----VQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:cd03234 80 -QKCVAYVRQDDILLPGLTVRETltytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPR--LMSHADRLLHMEDGAI 230
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRsdLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-230 |
2.64e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.17 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQG-FNLFPS 108
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR----QVGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESG 188
Cdd:PRK13635 97 ATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 942446941 189 QRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:PRK13635 177 REVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-230 |
2.72e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 101.14 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGsltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAamerfr 92
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LEHTGFIFQGFNLFPSLTAIEQvqlpMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSHdprLMSH----ADRLLHMEDGAI 230
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSH---LLSEiqkvADRIGIINKGKL 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-231 |
3.36e-26 |
|
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: 101.43 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAmerfr 92
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LEHTGFIFQGFNLFPSLTAIEQVQLpMGYL-GVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRF-YARLkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 172 KLLFADEPTSALDAESgQRVI-NILHRIARtyGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQ 231
Cdd:cd03263 153 SVLLLDEPTSGLDPAS-RRAIwDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
31-232 |
3.81e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQ--PDSGKAI------------------------------ALGI 78
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvgepcpvcggtlePEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 79 DLSTFSRAAMERFRlEHTGFIFQ-GFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGE 157
Cdd:TIGR03269 95 DFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 158 KQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQ 232
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIWLENGEIKE 249
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-230 |
3.91e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 3.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSLtvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStFSRAAMERF 91
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RlEHTGFIFQGFN--LFPSlTAIEQVQL-PMGyLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVA 168
Cdd:PRK13639 77 R-KTVGIVFQNPDdqLFAP-TVEEDVAFgPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 169 KAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMS-HADRLLHMEDGAI 230
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPvYADKVYVMSDGKI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-230 |
4.31e-26 |
|
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: 100.65 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 34 HLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAmerfrlEHTGFIFQGFNLFPSLTAIE 113
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 114 QVQLpmgylGVS---KRTSEER-AM-AALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESG 188
Cdd:cd03298 90 NVGL-----GLSpglKLTAEDRqAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 942446941 189 QRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-231 |
7.44e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGiDLSTFSRAAMERfrlEHTGFIFQG-FNLFPS 108
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWDIR---HKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESG 188
Cdd:PRK13650 97 ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 942446941 189 QRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQ 231
Cdd:PRK13650 177 LELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVE 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
30-230 |
1.15e-24 |
|
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: 97.69 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSraaMERFRlEHTGFIFQGFNLF--- 106
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLR-RAIGVVPQDTVLFndt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 ---------PSLTAIEQV-------------QLPMGY---LGvskrtseERamaaledvGLshrahmypaQLSGGEKQRV 161
Cdd:cd03253 91 igynirygrPDATDEEVIeaakaaqihdkimRFPDGYdtiVG-------ER--------GL---------KLSGGEKQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 162 AIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-225 |
1.33e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 99.27 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQD------ISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLS 81
Cdd:PRK11308 1 SQQPLLQAIDlkkhypVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 82 TFSRAAMERFRlEHTGFIFQgfNLFPSLTAIEQV--QL--PMGY---LGVSKRTseERAMAALEDVGL-SHRAHMYPAQL 153
Cdd:PRK11308 81 KADPEAQKLLR-QKIQIVFQ--NPYGSLNPRKKVgqILeePLLIntsLSAAERR--EKALAMMAKVGLrPEHYDRYPHMF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 154 SGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHM 225
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVM 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
30-230 |
1.36e-24 |
|
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: 97.30 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQGFNLFpSL 109
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR----QIGLVSQDVFLF-ND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLpmGYLGVSKRTSEERAMAA--------LEDvGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTS 181
Cdd:cd03251 91 TVAENIAY--GRPGATREEVEEAARAAnahefimeLPE-GYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 942446941 182 ALDAESGQRVINILHRIARtyGVTTLCVSHdpRL--MSHADRLLHMEDGAI 230
Cdd:cd03251 168 ALDTESERLVQAALERLMK--NRTTFVIAH--RLstIENADRIVVLEDGKI 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
30-220 |
2.90e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.53 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRlEHTGFIFQGFNLFPSL 109
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPmgyLGVSKRTSEE----RAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDA 185
Cdd:PRK11831 100 NVFDNVAYP---LREHTQLPAPllhsTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 942446941 186 ESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHAD 220
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDvPEVLSIAD 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
29-233 |
7.45e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 94.96 E-value: 7.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 29 VPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQGFNLFpS 108
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR----NIGYVPQDVTLF-Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLPMGYlgvskrTSEERAMAALEDVGLSHRAHMYP-----------AQLSGGEKQRVAIARAVAKAPKLLFAD 177
Cdd:cd03245 92 GTLRDNITLGAPL------ADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 178 EPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAIQQD 233
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-230 |
9.30e-24 |
|
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: 99.02 E-value: 9.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 21 SFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIF 100
Cdd:TIGR02203 337 TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRR----QVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 101 QGFNLFPSlTAIEQVQLPMGYLGVSKRTSEERAMAALEDV------GLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLL 174
Cdd:TIGR02203 413 QDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 175 FADEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-233 |
3.07e-23 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.09 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQGFNLFpSLT 110
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR----QVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 AIEQVQLpmGYLGVSKRTSEERA-MAALEDV------GLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSAL 183
Cdd:cd03252 92 IRDNIAL--ADPGMSMERVIEAAkLAGAHDFiselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 942446941 184 DAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAIQQD 233
Cdd:cd03252 170 DYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
29-230 |
4.91e-23 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 97.08 E-value: 4.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 29 VPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAmerFRlEHTGFIFQGFNLFpS 108
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE---LR-ARMALVPQDPVLF-A 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLpmGYLGVSKRTSEERAMAALED---VGLSHRAHMYPAQ----LSGGEKQRVAIARAVAKAPKLLFADEPTS 181
Cdd:TIGR02204 428 ASVMENIRY--GRPDATDEEVEAAARAAHAHefiSALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATS 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 942446941 182 ALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:TIGR02204 506 ALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLKADRIVVMDQGRI 552
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-238 |
6.54e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.90 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERf 91
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 rlEHTGFIFQGFNL-FPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKA 170
Cdd:PRK13644 77 --KLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 171 PKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSHADRLLHMEDGAIQQDAQTSN 238
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPEN 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-239 |
1.12e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 92.29 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMerfrLEHTGFIFQGFNLFPSl 109
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPmgylgvSKRTSEERAMAALEDVGL----SHRAHMYPAQ-------LSGGEKQRVAIARAVAKAPKLLFADE 178
Cdd:cd03254 92 TIMENIRLG------RPNATDEEVIEAAKEAGAhdfiMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 179 PTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAIqqdAQTSNH 239
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKI---IEEGTH 221
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
11-228 |
3.21e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.82 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSF-----LTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSR 85
Cdd:COG4167 3 ALLEVRNLSKTFkyrtgLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 86 aameRFRLEHTGFIFQGFN--LFPSLTAIEQVQLPMGY---LGVSKRtsEERAMAALEDVGLS--HrAHMYPAQLSGGEK 158
Cdd:COG4167 83 ----KYRCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLntdLTAEER--EERIFATLRLVGLLpeH-ANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 159 QRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDG 228
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-212 |
3.23e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.87 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPD---SGKAIALGIDLSTFS 84
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 85 RAAMERFRLEHTGFIFQG--FNLFPSLTAIEQV-QLPMGYLGVSKRTSEERAMAALEDVGLSH---RAHMYPAQLSGGEK 158
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 942446941 159 QRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD 212
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-195 |
3.53e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 91.07 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGsltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSraaM-ERF 91
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP---MhKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RLeHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:cd03218 74 RL-GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180
....*....|....*....|....*..
gi 942446941 172 KLLFADEPTSALDAESG---QRVINIL 195
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVqdiQKIIKIL 179
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
32-230 |
3.96e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.03 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLsTFSRAAMERFRlEHTGFIFQ--GFNLFPSl 109
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIR-KKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHR--AHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 188 GQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-230 |
4.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.69 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRlehTGFIFQgfNLFPSL 109
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNK---AGMVFQ--NPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAI---EQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAE 186
Cdd:PRK13633 99 VATiveEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 187 SGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-230 |
4.62e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.79 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 29 VPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRlEHTGFIFQG-FNLFP 107
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR-EKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 108 SLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 942446941 188 GQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-232 |
4.69e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 94.04 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIAL-GIDLSTFSRAAMERfrleHTGFIFQGFNLF 106
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS-VRLdGADLSQWDREELGR----HIGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 P-----------SLTAiEQV--------------QLPMGY---LGVSkrtseeramaaledvglshrahmyPAQLSGGEK 158
Cdd:COG4618 419 DgtiaeniarfgDADP-EKVvaaaklagvhemilRLPDGYdtrIGEG------------------------GARLSGGQR 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 159 QRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILhRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQ 232
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-230 |
1.49e-21 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 87.48 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFR 92
Cdd:cd03216 1 LELRGITKRF--GG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LehtGFIFQgfnlfpsltaieqvqlpmgylgvskrtseeramaaledvglshrahmypaqLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03216 77 I---AMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHdpRL---MSHADRLLHMEDGAI 230
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISH--RLdevFEIADRVTVLRDGRV 160
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-230 |
1.71e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.72 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQGFNLFpSL 109
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR----NIAVVFQDAGLF-NR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLpmgylGVSKRTSEE-----RAMAALE-----DVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEP 179
Cdd:PRK13657 424 SIEDNIRV-----GRPDATDEEmraaaERAQAHDfierkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 942446941 180 TSALDAESGQRVINILHRIARtyGVTTLCVSHdpRL--MSHADRLLHMEDGAI 230
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMK--GRTTFIIAH--RLstVRNADRILVFDNGRV 547
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-230 |
2.30e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.20 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 7 HSSQPVLQAQDISKSFLTGSLtvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIAL-GIDLSTFSR 85
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE-ILLnGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 86 AAMErfrlEHTGFIFQGFNLFpSLTAIEQVQLpmgylgVSKRTSEERAMAALEDVGLSHRAHMYPA----------QLSG 155
Cdd:PRK11160 410 AALR----QAISVVSQRVHLF-SATLRDNLLL------AAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 156 GEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-233 |
2.51e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSLT-VPVLRHLSLTVNPGE-LTLIsGPSGCGKSTLLSLLSGLQQPDSGKAIALGID---LSTFSRAA 87
Cdd:COG1101 2 LELKNLSKTFNPGTVNeKRALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MerfrlehTGFIFQ----GfnLFPSLTaIEQvQLPMGY---------LGVSKRTSEE-RAMAALEDVGLSHRAHMYPAQL 153
Cdd:COG1101 81 Y-------IGRVFQdpmmG--TAPSMT-IEE-NLALAYrrgkrrglrRGLTKKRRELfRELLATLGLGLENRLDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 154 SGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDprlMSHA----DRLLHMEDGA 229
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN---MEQAldygNRLIMMHEGR 226
|
....
gi 942446941 230 IQQD 233
Cdd:COG1101 227 IILD 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-228 |
3.15e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 87.61 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 24 TGSLTVPVLRHLSLTVNPGELTLISGPSGCGKST--LLSLLSGLQQPDSGKAIALGIDLStfsraaMERFRlEHTGFIFQ 101
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINGRPLD------KRSFR-KIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 102 GFNLFPSLTAIEQvqlpmgylgvskrtseeramaaledvgLSHRAHMypAQLSGGEKQRVAIARAVAKAPKLLFADEPTS 181
Cdd:cd03213 90 DDILHPTLTVRET---------------------------LMFAAKL--RGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 942446941 182 ALDAESGQRVINILHRIARTyGVTTLCVSHDPR--LMSHADRLLHMEDG 228
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADT-GRTIICSIHQPSseIFELFDKLLLLSQG 188
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-236 |
4.49e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 89.37 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSLTV-PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAA---- 87
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 -MERFRLEHT---------------GFIFQ--GFNLFPSltAIEQVQL--PMGYlGVSKRTSEERAMAALEDVGLS---- 143
Cdd:PRK13651 83 vLEKLVIQKTrfkkikkikeirrrvGVVFQfaEYQLFEQ--TIEKDIIfgPVSM-GVSKEEAKKRAAKYIELVGLDesyl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 144 HRAhmyPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRL 222
Cdd:PRK13651 160 QRS---PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRT 235
|
250
....*....|....
gi 942446941 223 LHMEDGAIQQDAQT 236
Cdd:PRK13651 236 IFFKDGKIIKDGDT 249
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-230 |
7.65e-21 |
|
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: 87.14 E-value: 7.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSlTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSraamERF 91
Cdd:cd03248 11 IVKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE----HKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RLEHTGFIFQGFNLFP-SLtaieQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYP-------AQLSGGEKQRVAI 163
Cdd:cd03248 86 LHSKVSLVGQEPVLFArSL----QDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 164 ARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYgvTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-222 |
9.09e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.12 E-value: 9.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFrlehtGFIFQGFNLFPSL 109
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI-----GVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESG- 188
Cdd:PRK13536 130 TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARh 209
|
170 180 190
....*....|....*....|....*....|....*..
gi 942446941 189 ---QRVINILHRiartyGVTTLCVSHdprLMSHADRL 222
Cdd:PRK13536 210 liwERLRSLLAR-----GKTILLTTH---FMEEAERL 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
5-228 |
1.07e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.49 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 5 YSHSSQPVLQA------QDISKSFLTGSLTVP-----VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKA 73
Cdd:TIGR00955 3 YSWRNSDVFGRvaqdgsWKQLVSRLRGCFCRErprkhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 74 IALGIDLSTFSRAAMERFrlehTGFIFQGFNLFPSLTAIEQVQ----LPMGYlGVSKRTSEERAMAALEDVGLSHRAHM- 148
Cdd:TIGR00955 83 GSVLLNGMPIDAKEMRAI----SAYVQQDDLFIPTLTVREHLMfqahLRMPR-RVTKKEKRERVDEVLQALGLRKCANTr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 149 --YPAQ---LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIArTYGVTTLCVSHDP--RLMSHADR 221
Cdd:TIGR00955 158 igVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPssELFELFDK 236
|
....*..
gi 942446941 222 LLHMEDG 228
Cdd:TIGR00955 237 IILMAEG 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-213 |
1.30e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.55 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 14 QAQDISKSFLTGSLTV--PVLRHLSLTVNPGELTLISGPSGCGKstllsllsglqqpdsgkaialgidlSTFSRAAMERF 91
Cdd:COG2401 26 RVAIVLEAFGVELRVVerYVLRDLNLEIEPGEIVLIVGASGSGK-------------------------STLLRLLAGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 R-LEHTGFIFQGFNLFPS-LTAIEQVqlpmgylgvSKRTSEERAMAALEDVGLSHrAHMY---PAQLSGGEKQRVAIARA 166
Cdd:COG2401 81 KgTPVAGCVDVPDNQFGReASLIDAI---------GRKGDFKDAVELLNAVGLSD-AVLWlrrFKELSTGQKFRFRLALL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 942446941 167 VAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDP 213
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-231 |
1.69e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 6 SHSSQPVLQAQDISKSFltGSLtvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALG--IDLSTF 83
Cdd:COG0488 309 ERLGKKVLELEGLSKSY--GDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGetVKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 84 S--RAAMErfrlehtgfifqgfnlfPSLTAIEQVQlpmgylGVSKRTSEERAMAALEDVGLS-HRAHMYPAQLSGGEKQR 160
Cdd:COG0488 384 DqhQEELD-----------------PDKTVLDELR------DGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAESgqrvINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQ 231
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDRYFLDRvATRILEFEDGGVR 508
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
8-228 |
2.32e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.58 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFlTGSLTVpvlRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAA 87
Cdd:PRK11300 1 MSQPLLSVSGLMMRF-GGLLAV---NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERFRLEHTgfiFQGFNLFPSLTAIEQV------QLPMGYL-GVSK----RTSE----ERAMAALEDVGLSHRAHMYPAQ 152
Cdd:PRK11300 77 IARMGVVRT---FQHVRLFREMTVIENLlvaqhqQLKTGLFsGLLKtpafRRAEsealDRAATWLERVGLLEHANRQAGN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRL-MSHADRLLHMEDG 228
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLvMGISDRIYVVNQG 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-224 |
2.70e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.14 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSF-LTGSLTVPVLR------HLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLS 81
Cdd:PRK10261 310 GEPILQVRNLVTRFpLRSGLLNRVTRevhaveKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 82 TFSRAAMERFRlEHTGFIFQG--FNLFPSLTAIEQVQLPMGYLGV-SKRTSEERAMAALEDVGL-SHRAHMYPAQLSGGE 157
Cdd:PRK10261 390 TLSPGKLQALR-RDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 158 KQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDprlMSHADRLLH 224
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHD---MAVVERISH 532
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-224 |
3.06e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.17 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAM 88
Cdd:PRK13537 4 SVAPIDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 89 ERfrlehTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVA 168
Cdd:PRK13537 80 QR-----VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 169 KAPKLLFADEPTSALDAESG----QRVINILHRiartyGVTTLCVSHdprLMSHADRLLH 224
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARhlmwERLRSLLAR-----GKTILLTTH---FMEEAERLCD 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-222 |
3.20e-20 |
|
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: 85.41 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIalgIDLSTFSRAAMERFr 92
Cdd:cd03269 1 LEVENVTKRF--GRVTA--LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL---FDGKPLDIAARNRI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 lehtGFIFQGFNLFPSLTAIEQvqlpMGYL----GVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVA 168
Cdd:cd03269 73 ----GYLPEERGLYPKMKVIDQ----LVYLaqlkGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 942446941 169 KAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDprlMSHADRL 222
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQ---MELVEEL 194
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-222 |
3.27e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.09 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAM--- 88
Cdd:COG4152 1 MLELKGLTKRF--GDKTA--VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 89 --ERfrlehtGfifqgfnLFPSLTAIEQvqlpMGYL----GVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVA 162
Cdd:COG4152 77 peER------G-------LYPKMKVGEQ----LVYLarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 163 IARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDprlMSHADRL 222
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQ---MELVEEL 195
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-232 |
3.97e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIalgIDLSTFSRAAMERFRlEHTGFIFQG-FNLFPSLT 110
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF---YNNQAITDDNFEKLR-KHIGIVFQNpDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 AIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQR 190
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 942446941 191 VINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQ 232
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-225 |
3.97e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.07 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 22 FLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLEhTGFIFQ 101
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 102 G--FNLFPSLTAIEQVQLPMG--YLGVSKRTSEERAMAALEDVGL-SHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFA 176
Cdd:PRK15079 106 DplASLNPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 942446941 177 DEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHM 225
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-236 |
4.71e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.91 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 23 LTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPD----SGKAIALGIdlstfsRAAMERFRLEHTGF 98
Cdd:PRK10418 10 IALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK------PVAPCALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 99 IFQ----GFNlfPSLT----AIEQVqlpmgyLGVSKRTSEERAMAALEDVGLSHRA---HMYPAQLSGGEKQRVAIARAV 167
Cdd:PRK10418 84 IMQnprsAFN--PLHTmhthARETC------LALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 168 -AKAPkLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD----PRLmshADRLLHMEDGAI--QQDAQT 236
Cdd:PRK10418 156 lCEAP-FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDmgvvARL---ADDVAVMSHGRIveQGDVET 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-232 |
5.35e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.21 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALG----IDLSTFSRA-A 87
Cdd:PRK11650 4 LKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIGgrvvNELEPADRDiA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MerfrlehtgfIFQGFNLFPSLTAIEQvqlpMGY----LGVSKRTSEER---AMAALEDVGLSHRAhmyPAQLSGGEKQR 160
Cdd:PRK11650 80 M----------VFQNYALYPHMSVREN----MAYglkiRGMPKAEIEERvaeAARILELEPLLDRK---PRELSGGQRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAEsgQRV-----INILHriaRTYGVTTLCVSHDP-RLMSHADRLLHMEDGAIQQ 232
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAK--LRVqmrleIQRLH---RRLKTTSLYVTHDQvEAMTLADRVVVMNGGVAEQ 215
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-229 |
5.65e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 83.36 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLsllsglqqpdsgKAIAlgiDLSTFSRAAMERFRLEHTGFIFQGfNLFPSL 109
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLF------------RALA---GLWPWGSGRIGMPEGEDLLFLPQR-PYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPmgylgvskrtseeramaaLEDVglshrahmypaqLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQ 189
Cdd:cd03223 79 TLREQLIYP------------------WDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 942446941 190 RviniLHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGA 229
Cdd:cd03223 129 R----LYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-213 |
6.59e-20 |
|
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: 87.80 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTGSltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMER 90
Cdd:TIGR02868 333 PTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 FrlehTGFIFQGFNLFPSlTAIEQVQLPMGylgvskRTSEERAMAALEDVGLSHRAHMYP-----------AQLSGGEKQ 159
Cdd:TIGR02868 410 R----VSVCAQDAHLFDT-TVRENLRLARP------DATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 942446941 160 RVAIARAVAKAPKLLFADEPTSALDAESGQRVINILhrIARTYGVTTLCVSHDP 213
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-232 |
6.77e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSlTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERf 91
Cdd:TIGR00958 478 LIEFQDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 rleHTGFIFQGFNLFPSltaieQVQLPMGYlGVSKRTSEE---RAMAALEDVGLSHRAHMYP-------AQLSGGEKQRV 161
Cdd:TIGR00958 556 ---QVALVGQEPVLFSG-----SVRENIAY-GLTDTPDEEimaAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRI 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 162 AIARAVAKAPKLLFADEPTSALDAESGQRVINILHRiartYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQ 232
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQESRSR----ASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-230 |
7.08e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.85 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVN---PGE-LTLISGPSGCGKSTLLSLLSGLQQPDSGKaIAL----------GIDLSTFSRaamerfrleHTG 97
Cdd:PRK11144 10 LGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGR-IVLngrvlfdaekGICLPPEKR---------RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 98 FIFQGFNLFPSLTaieqVQLPMGYlGVSKrtseerAMAALED-----VGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:PRK11144 80 YVFQDARLFPHYK----VRGNLRY-GMAK------SMVAQFDkivalLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD----PRLmshADRLLHMEDGAI 230
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSldeiLRL---ADRVVVLEQGKV 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
29-230 |
7.87e-20 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 84.41 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 29 VPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfSRAAMERFRLeHTGFIFQGFNLFPS 108
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPHERARA-GIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLpmgylGVSKRTSEERAmAALEDV-----GLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSAL 183
Cdd:cd03224 90 LTVEENLLL-----GAYARRRAKRK-ARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 942446941 184 DAESGQRVINILHRIARTyGVTTLCVSHDPRL-MSHADRLLHMEDGAI 230
Cdd:cd03224 164 APKIVEEIFEAIRELRDE-GVTILLVEQNARFaLEIADRAYVLERGRV 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-232 |
8.01e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.01 E-value: 8.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 17 DISKSFltGslTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaiaLGIDLSTFSRAA-MERfrleH 95
Cdd:PRK11000 8 NVTKAY--G--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD---LFIGEKRMNDVPpAER----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 TGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLF 175
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 176 ADEPTSALDAesGQRV-----INILHriaRTYGVTTLCVSHDP-RLMSHADRLLHMEDGAIQQ 232
Cdd:PRK11000 157 LDEPLSNLDA--ALRVqmrieISRLH---KRLGRTMIYVTHDQvEAMTLADKIVVLDAGRVAQ 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-230 |
9.54e-20 |
|
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: 83.13 E-value: 9.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaialgIDLSTFSRAAMERFR 92
Cdd:cd03247 1 LSINNVSFSYPEQE--QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE-----ITLDGVPVSDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LEHTGFIFQGFNLFpsltaieqvqlpmgylgvskrtseerAMAALEDVGlshrahmypAQLSGGEKQRVAIARAVAKAPK 172
Cdd:cd03247 74 SSLISVLNQRPYLF--------------------------DTTLRNNLG---------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-230 |
1.09e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.98 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 7 HSSQPVLQAQDISKSFLTGSltvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALG-----IDLS 81
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 82 TFSRAamERFRLEHT--GFIFQ----GfnLFPSLTAIEQVQLPMGYLGVsKRTSEERAMAA--LEDVGL-SHRAHMYPAQ 152
Cdd:PRK11701 77 ALSEA--ERRRLLRTewGFVHQhprdG--LRMQVSAGGNIGERLMAVGA-RHYGDIRATAGdwLERVEIdAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD---PRLMSHadRLLHMEDGA 229
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlavARLLAH--RLLVMKQGR 229
|
.
gi 942446941 230 I 230
Cdd:PRK11701 230 V 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-212 |
1.30e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQqPDSGKAIALGIDLSTFSRAAMERFRlEHTGFIFQGFN--LFPS 108
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNssLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQ--LPMGYLGVSKRTSEERAMAALEDVGLSHRA-HMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDA 185
Cdd:PRK15134 379 LNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
|
170 180
....*....|....*....|....*..
gi 942446941 186 ESGQRVINILHRIARTYGVTTLCVSHD 212
Cdd:PRK15134 459 TVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
12-230 |
1.70e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 83.86 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfSRAAMERF 91
Cdd:TIGR04406 1 TLVAENLIKSY--KKRKV--VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIT--HLPMHERA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RLeHTGFIFQGFNLFPSLTAIEQVqlpMGYLGVSKRTS----EERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:TIGR04406 75 RL-GIGYLPQEASIFRKLTVEENI---MAVLEIRKDLDraerEERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 168 AKAPKLLFADEPTSALDAESgqrVINI--LHRIARTYGVTTLCVSHDPR-LMSHADRLLHMEDGAI 230
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDPIA---VGDIkkIIKHLKERGIGVLITDHNVReTLDICDRAYIISDGKV 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-228 |
2.59e-19 |
|
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: 80.96 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGsltvPVLRHLSLTVNPGE-LTLIsGPSGCGKstllsllsglqqpdsgkaialgidlSTFSRAAMERF 91
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDrIGLV-GRNGAGK-------------------------STLLKLIAGEL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RlEHTGFIFQGFNLfpsltaieqvqlPMGYLgvskrtseeramaaledvglshrahmypAQLSGGEKQRVAIARAVAKAP 171
Cdd:cd03221 51 E-PDEGIVTWGSTV------------KIGYF----------------------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 172 KLLFADEPTSALDAESGQRVINILhriaRTYGVTTLCVSHDPRLMSH-ADRLLHMEDG 228
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-213 |
2.86e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.74 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPD-----SGKAIALGIDLSTFSRAAMERFRleHTGFIFQGFNL 105
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEVRR--EVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 106 FPSLTAIEQVQLPMGYLGVSKRTSE--ERAMAALEDVGL----SHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEP 179
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190
....*....|....*....|....*....|....
gi 942446941 180 TSALDAESGQRVINILHRIARTYgvTTLCVSHDP 213
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSP 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-236 |
3.34e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.09 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 34 HLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRA----AMerfrlehtgfIFQGFNLFPSL 109
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpvSM----------LFQENNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TaIEQvqlPMGyLGVS---KRTSEERAM--AALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALD 184
Cdd:PRK10771 87 T-VAQ---NIG-LGLNpglKLNAAQREKlhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 942446941 185 AESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQDAQT 236
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSlEDAARIAPRSLVVADGRIAWDGPT 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
30-225 |
6.26e-19 |
|
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: 81.64 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTfsraaMERFRLEHTGFIFQGFNLFPSL 109
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-----QRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYLGVSKRTSEEramaALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAEsGQ 189
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GV 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 942446941 190 RVINILHRIARTYGVTTLCVSHDPRLMSHAdRLLHM 225
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQDLGLVEA-RELRL 198
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
153-230 |
6.93e-19 |
|
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: 84.87 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARtyGVTTLCVSHdpRL--MSHADRLLHMEDGAI 230
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH--RLstIVDADEILVLEAGRI 570
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-230 |
9.19e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.54 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTgslTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERF 91
Cdd:PRK13652 3 LIETRDLCYSYSG---SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 rlehTGFIFQGFNLFPSLTAIEQ-VQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKA 170
Cdd:PRK13652 80 ----VGLVFQNPDDQIFSPTVEQdIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942446941 171 PKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLM-SHADRLLHMEDGAI 230
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRI 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
32-237 |
1.08e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGkaiALGIDLSTFSRAAMERFRlEHTGFIFQG-FNLFPSLT 110
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG---KVKIDGELLTAENVWNLR-RKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 AIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQR 190
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 942446941 191 VINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQDAQTS 237
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPS 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-238 |
1.41e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.08 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSFLtgSLTVPVLR---HLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKA-IALG---IDLSt 82
Cdd:TIGR03269 277 EPIIKVRNVSKRYI--SVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGdewVDMT- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 83 fSRAAMERFRL-EHTGFIFQGFNLFPSLTAIEQVQLPMGyLGVSKRTSEERAMAALEDVGLSHRA-----HMYPAQLSGG 156
Cdd:TIGR03269 354 -KPGPDGRGRAkRYIGILHQEYDLYPHRTVLDNLTEAIG-LELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 157 EKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQDAQ 235
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGD 511
|
...
gi 942446941 236 TSN 238
Cdd:TIGR03269 512 PEE 514
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-232 |
2.35e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALG----------I 78
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 79 DLSTFSRAAMERFRLEHTGFIFQG--FNLFPSLTAIEQVQLPMG-YLGVSKRTSEERAMAALEDVGLSHRAHM---YPAQ 152
Cdd:PRK10261 89 ELSEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHM------ 225
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMyqgeav 248
|
....*..
gi 942446941 226 EDGAIQQ 232
Cdd:PRK10261 249 ETGSVEQ 255
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
28-222 |
2.62e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.26 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKSTLLsllsglqqpdsgKAI--AL--------------GIDLSTFSraAMERF 91
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIA------------KAIcgITkdnwhvtadrfrwnGIDLLKLS--PRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RL--EHTGFIFQ--GFNLFPSLTAIEQVQ--LPMGYLGVS----KRTSEERAMAALEDVGL-SHRAHM--YPAQLSGGEK 158
Cdd:COG4170 85 KIigREIAMIFQepSSCLDPSAKIGDQLIeaIPSWTFKGKwwqrFKWRKKRAIELLHRVGIkDHKDIMnsYPHELTEGEC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 159 QRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRL 222
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQwADTI 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-228 |
3.98e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGL-QQPD----SGKAIALGIDLST 82
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlPSPPvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 83 FSRAAMERFRLEHTGFIFQG--FNLFPsLTAIEQvQLP---MGYLGVSKRTSEERAMAALEDVGLSH---RAHMYPAQLS 154
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEpmVSLNP-LHTLEK-QLYevlSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 155 GGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDG 228
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-230 |
4.03e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQP-DS-----GKAIALGIDLSTFSRAAMERfrleHTGFIFQGFN 104
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIKLRK----EVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 105 LFPSLTAIEQVQLPMGYLGVSKRTSEERAMA-ALEDVGLSHRAH---MYPA-QLSGGEKQRVAIARAVAKAPKLLFADEP 179
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLWKEVYdrlNSPAsQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 942446941 180 TSALDAESGQRVINILHRIARTygVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGEL 230
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
35-230 |
4.66e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 81.33 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 35 LSLTVNPGELTLISGPSGCGKSTLLSLLS-GLQQPDSGKAIAL---GIDLSTFSRAAMERFRLEHTGFIFQG--FNLFPS 108
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMgLIDYPGRVMAEKLefnGQDLQRISEKERRNLVGAEVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLPMG-YLGVSKRTSEERAMAALEDVGL---SHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALD 184
Cdd:PRK11022 106 YTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 942446941 185 AESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQV 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
13-211 |
9.25e-18 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.98 E-value: 9.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSltvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIalgidlstFSRAAMERFR 92
Cdd:TIGR03740 1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEII--------FDGHPWTRKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEEramaALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPK 172
Cdd:TIGR03740 69 LHKIGSLIESPPLYENLTARENLKVHTTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 942446941 173 LLFADEPTSALDAESGQRVINILhRIARTYGVTTLCVSH 211
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELI-RSFPEQGITVILSSH 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-184 |
1.05e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.92 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIAL-GIDLSTFSraaM- 88
Cdd:COG1137 2 MTLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGR-IFLdGEDITHLP---Mh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 89 ERFRL-------EHTgfIFQGfnlfpsLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRV 161
Cdd:COG1137 74 KRARLgigylpqEAS--IFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180
....*....|....*....|...
gi 942446941 162 AIARAVAKAPKLLFADEPTSALD 184
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVD 168
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-213 |
1.18e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.19 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQ--PD---SGKAIALGIDLstFS 84
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDI--FK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 85 RAAME-RFRLEhtgFIFQGFNLFPSLTAIEQVQL--PMGYLGVSKRTSEERAMAALEDVGL----SHRAHMYPAQLSGGE 157
Cdd:PRK14247 75 MDVIElRRRVQ---MVFQIPNPIPNLSIFENVALglKLNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 158 KQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTygVTTLCVSHDP 213
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFP 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-212 |
1.29e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 26 SLTVP---VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQG 102
Cdd:PRK10575 18 SFRVPgrtLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 103 FNLFPSLTAIEQVQLPM----GYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADE 178
Cdd:PRK10575 94 LPAAEGMTVRELVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190
....*....|....*....|....*....|....
gi 942446941 179 PTSALDAESGQRVINILHRIARTYGVTTLCVSHD 212
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-221 |
1.47e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFltGSLTVpvLRHLSLTVNPGEL------------TL---ISGpsgcgkstllsllsgLQQPDSGK 72
Cdd:COG3845 1 MMPPALELRGITKRF--GGVVA--NDDVSLTVRPGEIhallgengagksTLmkiLYG---------------LYQPDSGE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 73 ---------------AIALGIdlstfsraamerfrlehtGFIFQGFNLFPSLTAIEQVQL---PMGYLGVSKRTSEERAM 134
Cdd:COG3845 62 ilidgkpvrirsprdAIALGI------------------GMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 135 AALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHdpR 214
Cdd:COG3845 124 ELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITH--K 200
|
250
....*....|
gi 942446941 215 L---MSHADR 221
Cdd:COG3845 201 LrevMAIADR 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-233 |
1.80e-17 |
|
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: 80.94 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGSltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERF- 91
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFi 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 -RLEHTGFIFQGfnlfpslTAIEQVqlpmgYLGVSKRTSEERAMAALEDV-----------GLSHRAHMYPAQLSGGEKQ 159
Cdd:TIGR01193 551 nYLPQEPYIFSG-------SILENL-----LLGAKENVSQDEIWAACEIAeikddienmplGYQTELSEEGSSISGGQKQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 160 RVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTygvTTLCVSHDPRLMSHADRLLHMEDGAIQQD 233
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-214 |
2.16e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTF---SRAAMERFRLEHTGFIFQGFNLFP 107
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 108 SLTAIEQVQLPMgylgvSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK10895 98 NLMAVLQIRDDL-----SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180
....*....|....*....|....*..
gi 942446941 188 GQRVINILHRIaRTYGVTTLCVSHDPR 214
Cdd:PRK10895 173 VIDIKRIIEHL-RDSGLGVLITDHNVR 198
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-232 |
2.48e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALGIDLSTFSRAAMERFRL-EHTGFIFQgfnlFPSLT 110
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT-VTIGERVITAGKKNKKLKPLrKKVGIVFQ----FPEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 AIEQVQL------PMGYlGVSKRTSEERAMAALEDVGLSHRA-HMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSAL 183
Cdd:PRK13634 98 LFEETVEkdicfgPMNF-GVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 942446941 184 DAESGQRVINILHRIARTYGVTTLCVSHdprLM----SHADRLLHMEDGAIQQ 232
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTH---SMedaaRYADQIVVMHKGTVFL 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
31-222 |
2.48e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.54 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKstllsllsglqqpdsgkaialgidlSTFSRAaMER-------FRLE--------- 94
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGK-------------------------STLLRC-LNRmndlipgARVEgeilldged 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 95 -------------HTGFIFQGFNLFPslTAI-EQVQLPMGYLGV-SKRTSEERAMAALEDVGL----SHRAHMYPAQLSG 155
Cdd:COG1117 80 iydpdvdvvelrrRVGMVFQKPNPFP--KSIyDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 156 GEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYgvTTLCVSHDprlMSHADRL 222
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHN---MQQAARV 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-230 |
2.55e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFLTGSltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStFSRAAMERF 91
Cdd:PRK13636 5 ILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RlEHTGFIFQG--FNLFpSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAK 169
Cdd:PRK13636 81 R-ESVGMVFQDpdNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 170 APKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMS-HADRLLHMEDGAI 230
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-222 |
2.62e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFLTGSltvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQ--PD---SGKAIALGIDLSTf 83
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 84 SRAAMERFRLEhTGFIFQGFNLFPsLTAIEQVQLPMGYLGVSKRTSEERAM------AALEDvGLSHRAHMYPAQLSGGE 157
Cdd:PRK14239 77 PRTDTVDLRKE-IGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVekslkgASIWD-EVKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 158 KQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYgvTTLCVSHDprlMSHADRL 222
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRS---MQQASRI 213
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-222 |
4.07e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.08 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQpDSGKAIA-----LGIDLSTFSR 85
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTAdrmrfDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 86 AAMERFRLEHTGFIFQGFN--LFPSLTAIEQ-VQLPMGY---------LGVSKRtseeRAMAALEDVGL-SHRAHM--YP 150
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQscLDPSERVGRQlMQNIPGWtykgrwwqrFGWRKR----RAIELLHRVGIkDHKDAMrsFP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 151 AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRL 222
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKI 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
32-228 |
6.39e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.47 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfsrAAMERFRLEHTGFIFQGFN--LFpSL 109
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN----AENEKWVRSKVGLVFQDPDdqVF-SS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAeSGQ 189
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP-RGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 942446941 190 RVI-NILHRIARTyGVTTLCVSHDPRL-MSHADRLLHMEDG 228
Cdd:PRK13647 175 ETLmEILDRLHNQ-GKTVIVATHDVDLaAEWADQVIVLKEG 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
28-233 |
6.46e-17 |
|
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: 76.99 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFrlehtGFIF-QGFNLF 106
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRI-----GVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 PSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAE 186
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 942446941 187 SGQRVINILHRIARTYGVTTLCVSHDPR-LMSHADRLLHMEDGAIQQD 233
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLLYD 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-231 |
7.07e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFLTGSLtvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaiaLGIDLSTFSRAAM 88
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGE---IKIDGITISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 89 ERFRlEHTGFIFQG-FNLFPSLTAIEQVQLPMGylgvSKRTSEERAMAALEDvgLSHRAHMY------PAQLSGGEKQRV 161
Cdd:PRK13632 79 KEIR-KKIGIIFQNpDNQFIGATVEDDIAFGLE----NKKVPPKKMKDIIDD--LAKKVGMEdyldkePQNLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 162 AIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQ 231
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-212 |
1.81e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.23 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTGSltvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDS-----GKAIALGIDLSTfSR 85
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 86 AAMERFRlEHTGFIFQGFNLFPsLTAIEQVQLPMGYLGVSKRTS-EERAMAALEDVGL----SHRAHMYPAQLSGGEKQR 160
Cdd:PRK14258 81 VNLNRLR-RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEiDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD 212
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-230 |
2.15e-16 |
|
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: 74.39 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSfltgsltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMer 90
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 frlehtgfifqgfnlfpsltaieqVQLPMGYLgvskrtSEERAMAAL-------EDVGLshrahmyPAQLSGGEKQRVAI 163
Cdd:cd03215 73 ------------------------IRAGIAYV------PEDRKREGLvldlsvaENIAL-------SSLLSGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 164 ARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDGAI 230
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
29-230 |
2.20e-16 |
|
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: 75.40 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 29 VPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfSRAAMERFRLehtGFIF--QGFNLF 106
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPHRIARL---GIGYvpEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 PSLTAIEQVQLpmgylGVSKRTSEERAMAALEDVG-----LSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTs 181
Cdd:COG0410 91 PSLTVEENLLL-----GAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 182 aldaeSG------QRVINILHRIARTyGVTTLCVSHDPRL-MSHADRLLHMEDGAI 230
Cdd:COG0410 165 -----LGlaplivEEIFEIIRRLNRE-GVTILLVEQNARFaLEIADRAYVLERGRI 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
30-230 |
2.24e-16 |
|
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: 75.22 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRaamERFRlEHTGFI------FQG- 102
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGL---HDLR-SRISIIpqdpvlFSGt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 103 --FNLFPsltaieqvqlpmgyLGVSkrtSEERAMAALEDV-----------GLSHRAHMYPAQLSGGEKQRVAIARAVAK 169
Cdd:cd03244 94 irSNLDP--------------FGEY---SDEELWQALERVglkefveslpgGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 170 APKLLFADEPTSALDAESGQrvinILHRIARTY--GVTTLCVSHdpRL--MSHADRLLHMEDGAI 230
Cdd:cd03244 157 KSKILVLDEATASVDPETDA----LIQKTIREAfkDCTVLTIAH--RLdtIIDSDRILVLDKGRV 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-200 |
2.43e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALGIDLSTFSRAAMERFRLEHTGFifqgfnLFPSL 109
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT-IKLDGGDIDDPDVAEACHYLGHRNA------MKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYLGvskrTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIAR-AVAKAPkLLFADEPTSALDAESG 188
Cdd:PRK13539 89 TVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARlLVSNRP-IWILDEPTAALDAAAV 163
|
170
....*....|...
gi 942446941 189 QRVIN-ILHRIAR 200
Cdd:PRK13539 164 ALFAElIRAHLAQ 176
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
129-232 |
5.88e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 129 SEERAMAALEDVGLSHRAHMYP-----------AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHR 197
Cdd:PRK11174 451 SDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
|
90 100 110
....*....|....*....|....*....|....*..
gi 942446941 198 IARtyGVTTLCVSHdpRL--MSHADRLLHMEDGAIQQ 232
Cdd:PRK11174 531 ASR--RQTTLMVTH--QLedLAQWDQIWVMQDGQIVQ 563
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
31-230 |
7.94e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 73.71 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGID---LSTFSRAAMerfrleHTGFIFQGFNLFP 107
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHERARA------GIAYVPQGREIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 108 SLTAIEQVQLPMGYLGVSKRTSEERAMA---ALEDVgLSHRAhmypAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALD 184
Cdd:TIGR03410 89 RLTVEENLLTGLAALPRRSRKIPDEIYElfpVLKEM-LGRRG----GDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 942446941 185 ---AESGQRVINilhRIARTYGVTTLCV-SHDPRLMSHADRLLHMEDGAI 230
Cdd:TIGR03410 164 psiIKDIGRVIR---RLRAEGGMAILLVeQYLDFARELADRYYVMERGRV 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
35-230 |
1.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 35 LSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLEHTGFIFQgfnlFPSLTAIEQ 114
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 115 VQL------PMGYlGVSKRTSEERAMAALEDVGLSHRA-HMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK13643 101 TVLkdvafgPQNF-GIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 188 GQRVINILHRIARTyGVTTLCVSH-DPRLMSHADRLLHMEDGAI 230
Cdd:PRK13643 180 RIEMMQLFESIHQS-GQTVVLVTHlMDDVADYADYVYLLEKGHI 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-230 |
2.67e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.11 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMER 90
Cdd:PRK09536 2 PMIDVSDLSVEF--GD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 frleHTGFIFQGFNL---FPSLTAIEQVQLP----MGYLGVSKRTSEERAMAALEDVGLSHRAhmyPAQLSGGEKQRVAI 163
Cdd:PRK09536 78 ----RVASVPQDTSLsfeFDVRQVVEMGRTPhrsrFDTWTETDRAAVERAMERTGVAQFADRP---VTSLSGGERQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 164 ARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMS-HADRLLHMEDGAI 230
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAArYCDELVLLADGRV 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-187 |
2.81e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 33 RHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLstfsRAAMERFRLE------HTGfifqgfnLF 106
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQDllylghQPG-------IK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 PSLTAIEQVQLpmgYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAE 186
Cdd:PRK13538 87 TELTALENLRF---YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
.
gi 942446941 187 S 187
Cdd:PRK13538 164 G 164
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
31-230 |
3.38e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLS---GLQQPDSGKAIALGIDLSTFSRAAMERFRLEHTGFIF--QGFNL 105
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdlTGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLpqAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 106 FPsLTAIEQVQL---PMGYL-GVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAK---------APK 172
Cdd:PRK13547 96 FA-FSAREIVLLgryPHARRaGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMS-HADRLLHMEDGAI 230
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAI 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
31-230 |
5.71e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.94 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQGFNLFPSLT 110
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 AIEQV---QLPMGYLGVSKRTSEERAMA-ALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAE 186
Cdd:PRK10253 98 VQELVargRYPHQPLFTRWRKEDEEAVTkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 942446941 187 SGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAI 230
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKI 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
30-232 |
5.89e-15 |
|
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: 70.90 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSraaMERFRlehtgfifqgfnlfPSL 109
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR--------------SSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQ-VQLPMGY----LGVSKRTSEERAMAALE--DVGLShrahmypaqLSGGEKQRVAIARAVAKAPKLLFADEPTSA 182
Cdd:cd03369 85 TIIPQdPTLFSGTirsnLDPFDEYSDEEIYGALRvsEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 942446941 183 LDAESG---QRVINilhriARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQ 232
Cdd:cd03369 156 IDYATDaliQKTIR-----EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
153-228 |
6.60e-15 |
|
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: 70.96 E-value: 6.60e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVIN--ILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDG 228
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-228 |
7.48e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.17 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALG--IDLSTFSRAaMERFRLEhTGFIFQgfnlFPSL 109
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKN-LKKLRKK-VSLVFQ----FPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 -----TAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHR-AHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSAL 183
Cdd:PRK13641 97 qlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 942446941 184 DAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDG 228
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHG 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-230 |
1.97e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.93 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 16 QDISKSFLTGS-LTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLE 94
Cdd:PRK13649 6 QNVSYTYQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 95 HTGFIFQgfnlFPSLTAIEQVQL------PMGYlGVSKRTSEERAMAALEDVGLSHRA-HMYPAQLSGGEKQRVAIARAV 167
Cdd:PRK13649 86 KVGLVFQ----FPESQLFEETVLkdvafgPQNF-GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHdprLM----SHADRLLHMEDGAI 230
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTH---LMddvaNYADFVYVLEKGKL 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-230 |
4.27e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFlTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSG---------------KAIA 75
Cdd:PRK15439 10 PLLCARSISKQY-SG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtleiggnpcarltpaKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 76 LGIDLstfsraamerfrlehtgfIFQGFNLFPSLTAIEQVqlpmgYLGVSKRTSEERAMAAL-EDVGLSHRAHMYPAQLS 154
Cdd:PRK15439 86 LGIYL------------------VPQEPLLFPNLSVKENI-----LFGLPKRQASMQKMKQLlAALGCQLDLDSSAGSLE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 155 GGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILhRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAI 230
Cdd:PRK15439 143 VADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-231 |
5.42e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 15 AQDISKSFltGslTVPVLRHLSLTVNPGE-LTLIsGPSGCGKSTLLSLLSGLQQPDSGkaialgidlsTFSRAAMERFrl 93
Cdd:COG0488 1 LENLSKSF--G--GRPLLDDVSLSINPGDrIGLV-GRNGAGKSTLLKILAGELEPDSG----------EVSIPKGLRI-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 94 ehtGFIFQGFNLFPSLTAIEQV--------QLPMGYLGVSKRTSEE------------------------RAMAALEDVG 141
Cdd:COG0488 64 ---GYLPQEPPLDDDLTVLDTVldgdaelrALEAELEELEAKLAEPdedlerlaelqeefealggweaeaRAEEILSGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 142 LSHRAHMYP-AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESgqrvINILHRIARTYGVTTLCVSHDPRLMSH-A 219
Cdd:COG0488 141 FPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGTVLVVSHDRYFLDRvA 216
|
250
....*....|..
gi 942446941 220 DRLLHMEDGAIQ 231
Cdd:COG0488 217 TRILELDRGKLT 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-198 |
5.58e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSFlTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLsTFS--RAA 87
Cdd:PRK10762 2 QALLQLKGIDKAF-PG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNgpKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MErfrlEHTGFIFQGFNLFPSLTAIEQVQL------PMGYLGVSKRTSEerAMAALEDVGLSHRAHMYPAQLSGGEKQRV 161
Cdd:PRK10762 77 QE----AGIGIIHQELNLIPQLTIAENIFLgrefvnRFGRIDWKKMYAE--ADKLLARLNLRFSSDKLVGELSIGEQQMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 942446941 162 AIARAVAKAPKLLFADEPTSAL-DAESGQ--RVIN-----------ILHRI 198
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALtDTETESlfRVIRelksqgrgivyISHRL 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-237 |
7.04e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSF--LTGSL---TVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTfsra 86
Cdd:PRK15112 4 LLEVRNLSKTFryRTGWFrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 87 AMERFRLEHTGFIFQ--GFNLFPSLTAIEQVQLPMGY-LGVSKRTSEERAMAALEDVGL-SHRAHMYPAQLSGGEKQRVA 162
Cdd:PRK15112 80 GDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 163 IARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAIQQDAQTS 237
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTA 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-216 |
8.25e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStFSRAAMERFRlEHTGFIFQGFNLFPSL 109
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALR-QQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQ-VQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMyPAQ-LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK13638 93 TDIDSdIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180
....*....|....*....|....*....
gi 942446941 188 GQRVINILHRIARTyGVTTLCVSHDPRLM 216
Cdd:PRK13638 172 RTQMIAIIRRIVAQ-GNHVIISSHDIDLI 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-211 |
1.19e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFlTGsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALGIDLSTFS--RA 86
Cdd:PRK11288 1 SSPYLSFDGIGKTF-PG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS-ILIDGQEMRFAstTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 87 AMerfrleHTG--FIFQGFNLFPSLTAIEQV---QLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRV 161
Cdd:PRK11288 76 AL------AAGvaIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 942446941 162 AIARAVAKAPKLLFADEPTSALDAesgqRVINILHRIA---RTYGVTTLCVSH 211
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSA----REIEQLFRVIrelRAEGRVILYVSH 198
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-230 |
1.44e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.50 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRL-EHTGFIFQ--GFNLFPS 108
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLrKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 lTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHR-AHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 188 GQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAI 230
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
31-223 |
1.60e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaialgidlstfsraaMERFRLEHTGFIFQGFNLFPS-- 108
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV---------------IKRNGKLRIGYVPQKLYLDTTlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQVQLPMGylgvskrTSEERAMAALEDVGLSHrAHMYPAQ-LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK09544 84 LTVNRFLRLRPG-------TKKEDILPALKRVQAGH-LIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 942446941 188 GQRVINILHRIARTYGVTTLCVSHDPRL-MSHADRLL 223
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHLvMAKTDEVL 192
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-228 |
4.52e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrleHTGFIFQgFNLFPSL 109
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR----RLALLPQ-HHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQV-------QLPM-GYLGVSKRTSEERAMaalEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTS 181
Cdd:PRK11231 91 ITVRELvaygrspWLSLwGRLSAEDNARVNQAM---EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 942446941 182 ALDAeSGQRVINILHRIARTYGVTTLCVSHDPRLMS-HADRLLHMEDG 228
Cdd:PRK11231 168 YLDI-NHQVELMRLMRELNTQGKTVVTVLHDLNQASrYCDHLVVLANG 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-229 |
8.58e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTgsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLStfsraamer 90
Cdd:PRK09700 4 PYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 fRLEHT-------GFIFQGFNLFPSLTAIEQV---QLP----MGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGG 156
Cdd:PRK09700 71 -KLDHKlaaqlgiGIIYQELSVIDELTVLENLyigRHLtkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 157 EKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSHD-PRLMSHADRLLHMEDGA 229
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKlAEIRRICDRYTVMKDGS 222
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-228 |
1.11e-12 |
|
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: 64.57 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLsglqqpdSGKAIALGI--DLSTFSRAA 87
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-------AGRKTAGVItgEILINGRPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERFRLEhTGFIFQGFNLFPSLTAIEQVQLPmgylgvskrtseeramAALEDVGLSHRahmypaqlsggekQRVAIARAV 167
Cdd:cd03232 74 DKNFQRS-TGYVEQQDVHSPNLTVREALRFS----------------ALLRGLSVEQR-------------KRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDP--RLMSHADRLLHMEDG 228
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPsaSIFEKFDRLLLLKRG 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-225 |
1.77e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.19 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 6 SHSSQPVLQAQDIS---KSFLTgsltvpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQ-----PDSGKAIALG 77
Cdd:PRK14243 4 LNGTETVLRTENLNvyyGSFLA-------VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 78 IDLSTFSRAAME-RFRLehtGFIFQGFNLFPSlTAIEQVQLPMGYLGVSKRTSE--ERAM--AALEDvGLSHRAHMYPAQ 152
Cdd:PRK14243 77 KNLYAPDVDPVEvRRRI---GMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDElvERSLrqAALWD-EVKDKLKQSGLS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYgvTTLCVSHDprlMSHADRLLHM 225
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHN---MQQAARVSDM 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-229 |
2.27e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 7 HSSQPVLQAQDISKSfltgSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaialgIDLSTFSRA 86
Cdd:PRK13543 6 HTAPPLLAAHALAFS----RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQ-----IQIDGKTAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 87 AMERFRleHTGFIFQGFNLFPSLTAIEQVQLPMGYLGvskRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARA 166
Cdd:PRK13543 77 RGDRSR--FMAYLGHLPGLKADLSTLENLHFLCGLHG---RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 167 VAKAPKLLFADEPTSALDAESgqrvINILHRIARTY---GVTTLCVSHDPR-LMSHADRLLHMEDGA 229
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEG----ITLVNRMISAHlrgGGAALVTTHGAYaAPPVRTRMLTLEAAA 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
122-230 |
7.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 122 LGVSKRTSEERAMAALEDVGLSHR-AHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAEsGQRVINILHRIAR 200
Cdd:PRK13631 145 LGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAK 223
|
90 100 110
....*....|....*....|....*....|....
gi 942446941 201 TYGVTTLCVSHDprlMSH----ADRLLHMEDGAI 230
Cdd:PRK13631 224 ANNKTVFVITHT---MEHvlevADEVIVMDKGKI 254
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
29-230 |
7.36e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 29 VPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfrlEHTGFIFQGFNLFPS 108
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMR---EAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 LTAIEQvqLPMGYLGVSKRTSEERAMAALEDVG-LSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:PRK11614 95 MTVEEN--LAMGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 188 GQRVINILHRIaRTYGVTTLCVSHDP-RLMSHADRLLHMEDGAI 230
Cdd:PRK11614 173 IQQIFDTIEQL-REQGMTIFLVEQNAnQALKLADRGYVLENGHV 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-206 |
8.22e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTfsraAMERFRlEHTGFIFQGFNLFPSL 109
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVR-QSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQ 189
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170
....*....|....*....
gi 942446941 190 RVINIL--HRIARTYGVTT 206
Cdd:TIGR01257 1099 SIWDLLlkYRSGRTIIMST 1117
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
31-230 |
9.48e-12 |
|
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: 62.16 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKstllsllsglqqpdsgkaialgidlSTFSRAAM--ERFRLEHTGFIFQGFNLfps 108
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGK-------------------------STLAKTIMghPKYEVTEGEILFKGEDI--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 109 ltaieqVQLPMgylgvskrtsEERAMAALedvGLSHRahmYPAQ----------------LSGGEKQRVAIARAVAKAPK 172
Cdd:cd03217 67 ------TDLPP----------EERARLGI---FLAFQ---YPPEipgvknadflryvnegFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 173 LLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSHDPRLMSH--ADRLLHMEDGAI 230
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYikPDRVHVLYDGRI 183
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
131-212 |
1.04e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 131 ERAMAAL------EDVGlshrahmypaQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESgqrvINILHRIARTYGV 204
Cdd:PRK11819 146 EIAMDALrcppwdAKVT----------KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQFLHDYPG 211
|
....*...
gi 942446941 205 TTLCVSHD 212
Cdd:PRK11819 212 TVVAVTHD 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
16-230 |
1.09e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.79 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 16 QDISKSFltGslTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERfRLEh 95
Cdd:COG4604 5 KNVSKRY--G--GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK-RLA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 tgfIFQGFNLFPS-LTAIEQVQL---PmgYlgvSK-R-TSEERAM--AALEDVGLSHRAHMYPAQLSGGEKQRVAIARAV 167
Cdd:COG4604 79 ---ILRQENHINSrLTVRELVAFgrfP--Y---SKgRlTAEDREIidEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 168 AKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRV 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-236 |
1.26e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 8 SSQPVLQAQDISKSFLTGSltvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDL---STFS 84
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKT----VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 85 RAAMERFRlEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGL----SHRAHMYPAQLSGGEKQR 160
Cdd:PRK14271 93 YRDVLEFR-RRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTygVTTLCVSHD-PRLMSHADRLLHMEDGAIQQDAQT 236
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNlAQAARISDRAALFFDGRLVEEGPT 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-230 |
1.66e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLEHTGFIFQgfnlFPSLTA 111
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 112 IE-QVQLPMGY----LGVSKRTSEERAMAALEDVGLShRAHMY--PAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALD 184
Cdd:PRK13646 99 FEdTVEREIIFgpknFKMNLDEVKNYAHRLLMDLGFS-RDVMSqsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 942446941 185 AESGQRVINILHRIARTYGVTTLCVSHD-PRLMSHADRLLHMEDGAI 230
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-228 |
1.88e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLsllsglqqpdsgKAIALGIDLSTFSRAAMERFR------LEHTGFIFQGFN 104
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLL------------NALAGRIQGNNFTGTILANNRkptkqiLKRTGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 105 LFPSLTAIEQV------QLPMGylgVSKRTSEERAMAALEDVGLSH-----RAHMYPAQLSGGEKQRVAIARAVAKAPKL 173
Cdd:PLN03211 151 LYPHLTVRETLvfcsllRLPKS---LTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 174 LFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDP--RLMSHADRLLHMEDG 228
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPssRVYQMFDSVLVLSEG 283
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
30-230 |
2.17e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.62 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKS--TLLSLLSGLQQPDSGKAIALGIDLSTFSraAMERFRLehtGfIFQGFnlfp 107
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKStlAKVLMGHPKYEVTSGSILLDGEDILELS--PDERARA---G-IFLAF---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 108 sltaieqvQLPMGYLGVS-----------KRTSEERAMA-------ALEDVGLS----HRAhmYPAQLSGGEKQRVAIAR 165
Cdd:COG0396 84 --------QYPVEIPGVSvsnflrtalnaRRGEELSAREflkllkeKMKELGLDedflDRY--VNEGFSGGEKKRNEILQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 166 AVAKAPKLLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSHDPRLMSH--ADRLLHMEDGAI 230
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHYQRILDYikPDFVHVLVDGRI 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-187 |
3.01e-11 |
|
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: 60.58 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGkaialgiDLSTFSRAAMERFRLEHTGFIFQGF--NLFPS 108
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG-------RVLLNGGPLDFQRDSIARGLLYLGHapGIKTT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 109 LTAIEQVQLpmgylgVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:cd03231 88 LSVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
119-212 |
3.62e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 119 MGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILhRI 198
Cdd:PRK15056 109 MGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL-RE 187
|
90
....*....|....
gi 942446941 199 ARTYGVTTLCVSHD 212
Cdd:PRK15056 188 LRDEGKTMLVSTHN 201
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-229 |
3.69e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 60.81 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 18 ISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFRLEHTG 97
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 98 FIFQGFNLFpSLTAIEQVQLPMGYlgvskrtSEERAMAALEDVGLSHRAHMYP-----------AQLSGGEKQRVAIARA 166
Cdd:cd03290 83 YAAQKPWLL-NATVEENITFGSPF-------NKQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 167 VAKAPKLLFADEPTSALDAESGQRVIN--ILhRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGA 229
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHLSDHLMQegIL-KFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-228 |
3.73e-11 |
|
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: 60.35 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 17 DISKSFLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLsllsglqqpdsgKAIALGIDLS-------TFSRAAME 89
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLL------------KALANRTEGNvsvegdiHYNGIPYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 90 RFRLEHTG---FIFQGFNLFPSLTAIEQVqlpmgylgvskrtseeramaaleDVGLSHRAHMYPAQLSGGEKQRVAIARA 166
Cdd:cd03233 76 EFAEKYPGeiiYVSEEDVHFPTLTVRETL-----------------------DFALRCKGNEFVRGISGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942446941 167 VAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTL--CVSHDPRLMSHADRLLHMEDG 228
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFvsLYQASDEIYDLFDKVLVLYEG 196
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
32-229 |
4.90e-11 |
|
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: 59.64 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQqpdsgKAIALGIDLSTFSraamerfrleHTGFIFQGfnlfpSLTA 111
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYAS-----GKARLISFLPKFS----------RNKLIFID-----QLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 112 IeqVQLPMGYLgvskrtSEERAMAALedvglshrahmypaqlSGGEKQRVAIARAVAKAPK--LLFADEPTSALDAESGQ 189
Cdd:cd03238 71 L--IDVGLGYL------TLGQKLSTL----------------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 942446941 190 RVINILHRIaRTYGVTTLCVSHDPRLMSHADRLLHMEDGA 229
Cdd:cd03238 127 QLLEVIKGL-IDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
137-229 |
5.65e-11 |
|
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: 60.35 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 137 LEDVGLSH----RAHMypaQLSGGEKQRVAIARAV-AKAPKLLFA-DEPTSALDAESGQRVINILHRIaRTYGVTTLCVS 210
Cdd:cd03270 121 LVDVGLGYltlsRSAP---TLSGGEAQRIRLATQIgSGLTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVE 196
|
90
....*....|....*....
gi 942446941 211 HDPRLMSHADRLLHMEDGA 229
Cdd:cd03270 197 HDEDTIRAADHVIDIGPGA 215
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
35-228 |
8.91e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.30 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 35 LSLTVNPGELTLISGPSGCGKSTLlsllsglQQPDSGKAIALGIDLSTFSRAAMerFRLEHTGFIFQGfnlfpslTAIEQ 114
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSL-------FRILGELWPVYGGRLTKPAKGKL--FYVPQRPYMTLG-------TLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 115 VQLPMGYLGVSKR-TSEERAMAALEDVGLSH---RAHMYPA------QLSGGEKQRVAIARAVAKAPKLLFADEPTSALD 184
Cdd:TIGR00954 535 IIYPDSSEDMKRRgLSDKDLEQILDNVQLTHileREGGWSAvqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 942446941 185 AESGQRviniLHRIARTYGVTTLCVSHDPRLMSHADRLLHMeDG 228
Cdd:TIGR00954 615 VDVEGY----MYRLCREFGITLFSVSHRKSLWKYHEYLLYM-DG 653
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
149-228 |
9.93e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 149 YPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES---------------GQRVINILHRIARTYGVTTLCVSHDP 213
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSekliektivdikdkaDKTIITIAHRIASIKRSDKIVVFNNP 1434
|
90 100
....*....|....*....|..
gi 942446941 214 R-----LMSHA--DRLLHMEDG 228
Cdd:PTZ00265 1435 DrtgsfVQAHGthEELLSVQDG 1456
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
153-223 |
1.08e-10 |
|
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: 60.95 E-value: 1.08e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAEsgQRVI--NILHRIARTYGVTTLCVSHDprLMSH---ADRLL 223
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAvaKAIRRFAENRGKTAMVVDHD--IYLIdyiSDRLM 527
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-230 |
1.55e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 7 HSSQPVLQAQDISksfLTGSLTVPVLRHLSLTVNPGELTLISGPSGCGkstllsllsglQQ-----------PDSGKAIA 75
Cdd:COG3845 252 EPGEVVLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNG-----------QSelaealaglrpPASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 76 LGIDLSTFSRAAMERFRLehtGFI---FQGFNLFPSLTAIE------QVQLPMGYLG-VSKRTSEERAMAALE--DV--- 140
Cdd:COG3845 318 DGEDITGLSPRERRRLGV---AYIpedRLGRGLVPDMSVAEnlilgrYRRPPFSRGGfLDRKAIRAFAEELIEefDVrtp 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 141 GLSHRAhmypAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILhRIARTYGVTTLCVSHDPR-LMSHA 219
Cdd:COG3845 395 GPDTPA----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL-LELRDAGAAVLLISEDLDeILALS 469
|
250
....*....|.
gi 942446941 220 DRLLHMEDGAI 230
Cdd:COG3845 470 DRIAVMYEGRI 480
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
153-223 |
2.15e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.15e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAEsgQRVI--NILHRIARTYGVTTLCVSHDprLMSH---ADRLL 223
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAvaKAIRRIAEEREATALVVDHD--IYMIdyiSDRLM 525
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
30-230 |
2.42e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.03 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMErfrlEHTGFIFQGFNLFPSL 109
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR----NQVALVSQNVHLFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEqvqlpMGYLGVSKRTSE--ERA--MA-ALE-----DVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEP 179
Cdd:PRK11176 433 IANN-----IAYARTEQYSREqiEEAarMAyAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 942446941 180 TSALDAESG---QRVINILHRiartyGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:PRK11176 508 TSALDTESEraiQAALDELQK-----NRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-230 |
2.61e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSfltgsltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGK---------------AIA 75
Cdd:COG1129 255 VVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEirldgkpvrirsprdAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 76 LGIDLSTFSRAAmerfrlehtgfifQGfnLFPSLTAIEQVQLP-MGYLG----VSKRTSEERAMAALEDVGL-SHRAHMY 149
Cdd:COG1129 327 AGIAYVPEDRKG-------------EG--LVLDLSIRENITLAsLDRLSrgglLDRRRERALAEEYIKRLRIkTPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 150 PAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDG 228
Cdd:COG1129 392 VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSElPELLGLSDRILVMREG 470
|
..
gi 942446941 229 AI 230
Cdd:COG1129 471 RI 472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
153-231 |
3.63e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVIN--ILHRIArtyGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALA---GKTRVLATHQVHVVPRADYVVALGDGRV 859
|
.
gi 942446941 231 Q 231
Cdd:PTZ00243 860 E 860
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-230 |
5.49e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDisksfLTGSltvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAme 89
Cdd:PRK15439 266 APVLTVED-----LTGE----GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 90 rfRLEhTGFIF-------QGFNLFPSLTAiEQVQLPMGYLGVSKRTSEERAM-----AALeDVGLSHRAHmyPAQ-LSGG 156
Cdd:PRK15439 335 --RLA-RGLVYlpedrqsSGLYLDAPLAW-NVCALTHNRRGFWIKPARENAVleryrRAL-NIKFNHAEQ--AARtLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 157 EKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHD----PRLmshADRLLHMEDGAI 230
Cdd:PRK15439 408 NQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDleeiEQM---ADRVLVMHQGEI 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-212 |
7.26e-10 |
|
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: 58.41 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFLTGSltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKA-IALGIDLstfsraa 87
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEArPQPGIKV------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 merfrlehtGFIFQGFNLFPSLTAIEQVQLPMG--------YLGVSKRTSEERA--------MAALEDVGLSHRAHMYPA 151
Cdd:TIGR03719 71 ---------GYLPQEPQLDPTKTVRENVEEGVAeikdaldrFNEISAKYAEPDAdfdklaaeQAELQEIIDAADAWDLDS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 152 Q-------------------LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESgqrvINILHRIARTYGVTTLCVSHD 212
Cdd:TIGR03719 142 QleiamdalrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
152-225 |
1.55e-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: 55.06 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 152 QLSGGEKQRVAIARAVAKAPK----LLFADEPTSALDAESGQRVINIlhrIARTY--GVTTLCVSHDPRLMSHADRLLHM 225
Cdd:cd03227 77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEA---ILEHLvkGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-211 |
1.66e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 9 SQPVLQAQDISKSFLTgsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQqPD---SGKAIALGIDLstfsR 85
Cdd:PRK13549 2 MEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEEL----Q 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 86 AAMERfRLEHTG--FIFQGFNLFPSLTAIEQVQL-----PMGYLGVSKRTSeeRAMAALEDVGLSHRAHMYPAQLSGGEK 158
Cdd:PRK13549 73 ASNIR-DTERAGiaIIHQELALVKELSVLENIFLgneitPGGIMDYDAMYL--RAQKLLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 942446941 159 QRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSH 211
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISH 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-212 |
1.84e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.63 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSF--------LTGSL---------TVPVLRHLSLTVNPGELTLISGPSGCGKstllsllsglqQPDSGKAI 74
Cdd:COG4586 1 IIEVENLSKTYrvyekepgLKGALkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKsttikmltgilVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 75 ALGIDlsTFSRAamERFrLEHTGFIF-QGFNLFPSLTAIEQVQLpmgyL----GVSKRTSEERaMAALEDV-GLSH---- 144
Cdd:COG4586 81 VLGYV--PFKRR--KEF-ARRIGVVFgQRSQLWWDLPAIDSFRL----LkaiyRIPDAEYKKR-LDELVELlDLGElldt 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 145 --RahmypaQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHD 212
Cdd:COG4586 151 pvR------QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-228 |
2.27e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKstLLSLLSGLQQPDSGkAIALGIDL-------STFSRAamerfrlehTGFIFQGF 103
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGK--TTLLNVLAERVTTG-VITGGDRLvngrpldSSFQRS---------IGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 104 NLFPSLTAIEQVQLPmGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSG--GE------KQRVAIARAVAKAPKLL- 174
Cdd:TIGR00956 846 LHLPTSTVRESLRFS-AYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGvpGEglnveqRKRLTIGVELVAKPKLLl 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 175 FADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPR--LMSHADRLLHMEDG 228
Cdd:TIGR00956 925 FLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-238 |
3.79e-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: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMeRFRLEhtgFIFQGFNLFPSlt 110
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKIT---IIPQDPVLFSG-- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 aieqvQLPMGYLGVSKRTSEERAMA-----------ALEDvGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEP 179
Cdd:TIGR00957 1375 -----SLRMNLDPFSQYSDEEVWWAlelahlktfvsALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 180 TSALDAESGqrviNILHRIARTY--GVTTLCVSHdpRLMSHAD--RLLHMEDGAIQQDAQTSN 238
Cdd:TIGR00957 1449 TAAVDLETD----NLIQSTIRTQfeDCTVLTIAH--RLNTIMDytRVIVLDKGEVAEFGAPSN 1505
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-241 |
3.80e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 151 AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESG---QRVIN------------ILHRIARTYGVTTLCVSHDPRL 215
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINnlkgnenritiiIAHRLSTIRYANTIFVLSNRER 657
|
90 100
....*....|....*....|....*.
gi 942446941 216 MSHADRLLHMEDGAIQQDAQTSNHKN 241
Cdd:PTZ00265 658 GSTVDVDIIGEDPTKDNKENNNKNNK 683
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-211 |
5.76e-09 |
|
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: 55.60 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFltGSltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDS--GKAIALGIDLSTFSRAAME 89
Cdd:TIGR02633 1 LLEMKGIVKTF--GG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 90 RfrlEHTGFIFQGFNLFPSLTAIE------QVQLPMGYLGVSKRTseERAMAALEDVGLSHRAHMYP-AQLSGGEKQRVA 162
Cdd:TIGR02633 77 R---AGIVIIHQELTLVPELSVAEniflgnEITLPGGRMAYNAMY--LRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 942446941 163 IARAVAKAPKLLFADEPTSALDAESGQRVINILhRIARTYGVTTLCVSH 211
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDII-RDLKAHGVACVYISH 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
41-228 |
6.75e-09 |
|
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: 53.15 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 41 PGELTLISGPSGCGKstllsllsglqqpdsgkaialgidlSTFSRAAMERFRLEHTGFIFqgfnlfpsltaieqvqlpmg 120
Cdd:smart00382 1 PGEVILIVGPPGSGK-------------------------TTLARALARELGPPGGGVIY-------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 121 ylgvskrTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVI-----NIL 195
Cdd:smart00382 36 -------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLL 108
|
170 180 190
....*....|....*....|....*....|....*....
gi 942446941 196 HRIARTYGVTTLCVSHDPR------LMSHADRLLHMEDG 228
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLI 147
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-229 |
8.78e-09 |
|
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: 55.40 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 137 LEDVGLSH----RAhmyPAQLSGGEKQRVAIARAV-AKAPKLLFA-DEPTSALDAESGQRVINILHRIaRTYGVTTLCVS 210
Cdd:TIGR00630 472 LIDVGLDYlslsRA---AGTLSGGEAQRIRLATQIgSGLTGVLYVlDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVE 547
|
90
....*....|....*....
gi 942446941 211 HDPRLMSHADRLLHMEDGA 229
Cdd:TIGR00630 548 HDEDTIRAADYVIDIGPGA 566
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-240 |
9.04e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.10 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFsRAAMERFRL---EHTGFIFQ--- 101
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL-QLDSWRSRLavvSQTPFLFSdtv 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 102 GFNLF---PSLTA--IEQV-----------QLPMGYLgvskrtseeramaalEDVGlsHRAHMypaqLSGGEKQRVAIAR 165
Cdd:PRK10789 406 ANNIAlgrPDATQqeIEHVarlasvhddilRLPQGYD---------------TEVG--ERGVM----LSGGQKQRISIAR 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 166 AVAKAPKLLFADEPTSALDaesGQRVINILHRIARTYGVTTLCVS-HDPRLMSHADRLLHMEDGAIqqdAQTSNHK 240
Cdd:PRK10789 465 ALLLNAEILILDDALSAVD---GRTEHQILHNLRQWGEGRTVIISaHRLSALTEASEILVMQHGHI---AQRGNHD 534
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-231 |
9.15e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFlTGSlTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGID-LSTFSRAAmer 90
Cdd:TIGR01257 1937 ILRLNELTKVY-SGT-SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVH--- 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 91 frlEHTGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKA 170
Cdd:TIGR01257 2012 ---QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 171 PKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDGAIQ 231
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSmEECEALCTRLAIMVKGAFQ 2149
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
153-233 |
9.21e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVIN-ILHRIARtyGVTTLCVSHDPRLMSHADRLLHMEDGAIQ 231
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIK 818
|
..
gi 942446941 232 QD 233
Cdd:PLN03130 819 EE 820
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
35-228 |
1.04e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.08 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 35 LSLTVNPGELTLISGPSGCGKSTLLSLLSGLqQPDSGKAIALGIDLSTFSRAAMERFR------LEHTGFI--FQGFNLF 106
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqqQSPPFAMpvFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 -PSLTAIEQVQLPMGYLgvskrtseeramaaLEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAK-------APKLLFADE 178
Cdd:COG4138 94 qPAGASSEAVEQLLAQL--------------AEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 942446941 179 PTSALDAesGQRVI--NILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDG 228
Cdd:COG4138 160 PMNSLDV--AQQAAldRLLRELCQQ-GITVVMSSHDlNHTLRHADRVWLLKQG 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-212 |
1.45e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 32 LRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaIALGIDLSTfsrAAMERFRLEhtgfifqgfnLFPSLTA 111
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-IHCGTKLEV---AYFDQHRAE----------LDPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 112 IEQvqlpmgyLGVSKRTSE----ER-AMAALEDVGLSHRAHMYPAQ-LSGGEKQRVAIARAVAKAPKLLFADEPTSALDA 185
Cdd:PRK11147 401 MDN-------LAEGKQEVMvngrPRhVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
170 180
....*....|....*....|....*..
gi 942446941 186 ESgqrvINILHRIARTYGVTTLCVSHD 212
Cdd:PRK11147 474 ET----LELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
153-223 |
1.47e-08 |
|
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: 53.57 E-value: 1.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLL 223
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYlADRLI 187
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-200 |
1.61e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKS----TLLSLLSGLQQPDSGKAIALGIDLSTFsraaMERFRLEhTGFIFQGF 103
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCStllkTIASNTDGFHIGVEGVITYDGITPEEI----KKHYRGD-VVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 104 NLFPSLTAIE------QVQLPMG-YLGVSKRTSEER----AMAALedvGLSH-----------RAhmypaqLSGGEKQRV 161
Cdd:TIGR00956 148 VHFPHLTVGEtldfaaRCKTPQNrPDGVSREEYAKHiadvYMATY---GLSHtrntkvgndfvRG------VSGGERKRV 218
|
170 180 190
....*....|....*....|....*....|....*....
gi 942446941 162 AIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIAR 200
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSAN 257
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-186 |
1.62e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGkAIALGidlSTFSRAAMERF 91
Cdd:TIGR03719 322 VIEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG-TIEIG---ETVKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RLehtgfifqgfNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAAL---------EDVGlshrahmypaQLSGGEKQRVA 162
Cdd:TIGR03719 394 RD----------ALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRfnfkgsdqqKKVG----------QLSGGERNRVH 453
|
170 180
....*....|....*....|....
gi 942446941 163 IARAVAKAPKLLFADEPTSALDAE 186
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-233 |
1.67e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.55 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSF------------------LTGSLTVPVLRHLSLTVNPGE-LTLIsGPSGCGKSTLLSLLSGLQQPDSGK 72
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGEsVGII-GRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 73 AIALGidlstfSRAAMerfrLEHTGfifqGFNlfPSLTAIEQVQLPMGYLGVSKRTSEERamaaLEDV----GLSHRAHM 148
Cdd:COG1134 83 VEVNG------RVSAL----LELGA----GFH--PELTGRENIYLNGRLLGLSRKEIDEK----FDEIvefaELGDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 149 ----YpaqlSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLM-SHADRLL 223
Cdd:COG1134 143 pvktY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVrRLCDRAI 217
|
250
....*....|
gi 942446941 224 HMEDGAIQQD 233
Cdd:COG1134 218 WLEKGRLVMD 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-232 |
2.65e-08 |
|
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: 54.18 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKStllsllsglqqpdsgkaialgidlSTFSRAAMERFRLEHTGFIFQGFNLFPSL 109
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKS------------------------SLLSALLAEMDKVEGHVHMKGSVAYVPQQ 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYLgVSKRTSEERAMAALEDVGLSHRAHMYPA-----------QLSGGEKQRVAIARAVAKAPKLLFADE 178
Cdd:TIGR00957 708 AWIQNDSLRENIL-FGKALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 179 PTSALDAESGQRVI-NILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQ 232
Cdd:TIGR00957 787 PLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
28-233 |
2.95e-08 |
|
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: 52.53 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALG-----IDLSTfsraamerfrlehtgfifqG 102
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvsslLGLGG-------------------G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 103 FNlfPSLTAIEQVQLPMGYLGVSKRTSEER-----AMAALEDVGLSHRAHmypaqLSGGEKQRVAIARAVAKAPKLLFAD 177
Cdd:cd03220 95 FN--PELTGRENIYLNGRLLGLSRKEIDEKideiiEFSELGDFIDLPVKT-----YSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 942446941 178 EPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLM-SHADRLLHMEDGAIQQD 233
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIkRLCDRALVLEKGKIRFD 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
152-212 |
3.09e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 3.09e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 152 QLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAesGQR--VINILHRIARtyGVTTLCVSHD 212
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI--RQRlnVARLIRELAE--GKYVLVVEHD 270
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-232 |
4.48e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 33 RHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSR--------AAMERFRLEhTGFiFQGFN 104
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmAYITESRRD-NGF-FPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 105 LFPSLTAIEQVQLPmGYLG----VSKRTSEERAMAALEDVGLS-HRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEP 179
Cdd:PRK09700 358 IAQNMAISRSLKDG-GYKGamglFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 942446941 180 TSALDAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDGAIQQ 232
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCDRIAVFCEGRLTQ 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
153-230 |
5.13e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 5.13e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDGAI 230
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDlPEVLGVADRIVVMREGRI 474
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
130-212 |
6.05e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 130 EERAMAALEDVGLShrAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESgqrvINILHRIARTYGVTTLCV 209
Cdd:PRK11147 136 ENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFI 209
|
...
gi 942446941 210 SHD 212
Cdd:PRK11147 210 SHD 212
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
35-232 |
6.23e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 35 LSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIalgIDLSTFSRAAMERFRlEHTGFIFQGFNLFpsltaiEQ 114
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL---LDGKPVTAEQPEDYR-KLFSAVFTDFHLF------DQ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 115 VQLPMGylgvsKRTSEERAMAALEDVGLSHRAH-----MYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQ 189
Cdd:PRK10522 412 LLGPEG-----KPANPALVEKWLERLKMAHKLEledgrISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 942446941 190 RVINILHRIARTYGVTTLCVSHDPRLMSHADRLLHMEDGAIQQ 232
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-228 |
8.05e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 35 LSLTVNPGELTLISGPSGCGKSTLLSLLSGLQqPDSGKAIALGIDLSTFSRAAMERFRlehtGFIFQGFNLFPSLTAIEQ 114
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 115 VQLpmgYLGVSKRTSEERAmaALEDV----GLSHRAHMYPAQLSGGEKQRVAIA-------RAVAKAPKLLFADEPTSAL 183
Cdd:PRK03695 90 LTL---HQPDKTRTEAVAS--ALNEVaealGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 942446941 184 DAesGQRVI--NILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDG 228
Cdd:PRK03695 165 DV--AQQAAldRLLSELCQQ-GIAVVMSSHDlNHTLRHADRVWLLKQG 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
153-230 |
9.88e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 9.88e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSHD-PRLMSHADRLLHMEDGAI 230
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
35-233 |
1.12e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 51.72 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 35 LSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGkaiALGIDLSTFSRAAMERFRlEHTGFIFQGFNLFPSLtaieq 114
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESG---EILLDGQPVTADNREAYR-QLFSAVFSDFHLFDRL----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 115 vqlpmgyLGVSKRTSEERAMAALEDVGLSHRAHMY-----PAQLSGGEKQRVAIARAVA-KAPKLLFaDEptSALDaesg 188
Cdd:COG4615 422 -------LGLDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLeDRPILVF-DE--WAAD---- 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 942446941 189 Q-----RVI--NILHRIARTyGVTTLCVSHDPRLMSHADRLLHMEDGAIQQD 233
Cdd:COG4615 488 QdpefrRVFytELLPELKAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVEL 538
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
152-212 |
1.16e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 1.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 152 QLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAesGQR--VINILHRIARTyGVTTLCVSHD 212
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRlnVARLIRELAEE-GKYVLVVEHD 271
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-238 |
1.74e-07 |
|
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: 50.68 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMeRFRLE---HTGFIFQG---F 103
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL-RSRLSiilQDPILFSGsirF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 104 NLFPsltaieqvqlpmgylgvSKRTSEERAMAALEDVGLSHRAHMYPAQL-----------SGGEKQRVAIARAVAKAPK 172
Cdd:cd03288 114 NLDP-----------------ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 173 LLFADEPTSALDAESGqrviNILHRIARTYGV--TTLCVSHDPRLMSHADRLLHMEDGAIQQDAQTSN 238
Cdd:cd03288 177 ILIMDEATASIDMATE----NILQKVVMTAFAdrTVVTIAHRVSTILDADLVLVLSRGILVECDTPEN 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-233 |
1.87e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 10 QPVLQAQDISKSFLT--GSLTVPVLRHLSLTVNPGELTLISGPSGCGKStllsllsglqqpdsgkaialgidlSTFSRAA 87
Cdd:PLN03232 609 QPGAPAISIKNGYFSwdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKT------------------------SLISAML 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 88 MERFRLEHTGFIFQGFNLF-PSLTAIEQVQLPMGYLGVSKRTSEeRAMAALEDVGLSHRAHMYPAQ-----------LSG 155
Cdd:PLN03232 665 GELSHAETSSVVIRGSVAYvPQVSWIFNATVRENILFGSDFESE-RYWRAIDVTALQHDLDLLPGRdlteigergvnISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 156 GEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVIN--ILHRIArtyGVTTLCVSHDPRLMSHADRLLHMEDGAIQQD 233
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
153-226 |
2.55e-07 |
|
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: 49.11 E-value: 2.55e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 153 LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHME 226
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
131-211 |
2.72e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 131 ERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVS 210
Cdd:NF040905 118 RRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIIS 196
|
.
gi 942446941 211 H 211
Cdd:NF040905 197 H 197
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
108-224 |
3.19e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 108 SLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAES 187
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
90 100 110
....*....|....*....|....*....|....*..
gi 942446941 188 GQRVINILHRIARTyGVTTLCVShdpRLMSHADRLLH 224
Cdd:NF000106 180 RNEVWDEVRSMVRD-GATVLLTT---QYMEEAEQLAH 212
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
132-225 |
3.64e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.54 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 132 RAMAALEDVGLSHRAHMYPA-QLSGGEKQRVAIARAVAKA---PKLLFADEPTSALDAESGQRVINILHRIARTyGVTTL 207
Cdd:cd03271 148 RKLQTLCDVGLGYIKLGQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVV 226
|
90
....*....|....*...
gi 942446941 208 CVSHDPRLMSHADRLLHM 225
Cdd:cd03271 227 VIEHNLDVIKCADWIIDL 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
152-212 |
4.89e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.29 E-value: 4.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 152 QLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAesGQR--VINILHRIARTyGVTTLCVSHD 212
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDI--KQRlnAARLIRELAED-DNYVLVVEHD 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
151-233 |
5.62e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 151 AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDGA 229
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSElPEVLGLSDRVLVMHEGK 482
|
....
gi 942446941 230 IQQD 233
Cdd:PRK13549 483 LKGD 486
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
98-229 |
9.27e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 98 FIFQGfNLFPSLTAIEQVqlpmgYLGVSKRtseeraMAALEDVGLSH----RAhmyPAQLSGGEKQRVAIARAV-AKAPK 172
Cdd:PRK00635 433 FIFLS-QLPSKSLSIEEV-----LQGLKSR------LSILIDLGLPYltpeRA---LATLSGGEQERTALAKHLgAELIG 497
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 942446941 173 LLFA-DEPTSALDAESGQRVINILHRIaRTYGVTTLCVSHDPRLMSHADRLLHMEDGA 229
Cdd:PRK00635 498 ITYIlDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISLADRIIDIGPGA 554
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-230 |
1.52e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.56 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 5 YSHSSQPV----LQAQDISKSFLTGSltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDL 80
Cdd:PRK10790 329 YGNDDRPLqsgrIDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 81 STFSRAAMERfrleHTGFIFQ-----GFNLFPSLTaieqvqlpmgyLGvsKRTSEERAMAALEDVGLSHRAHMYPA---- 151
Cdd:PRK10790 406 SSLSHSVLRQ----GVAMVQQdpvvlADTFLANVT-----------LG--RDISEEQVWQALETVQLAELARSLPDglyt 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 152 -------QLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILhRIARTYgvTTLCV-SHDPRLMSHADRLL 223
Cdd:PRK10790 469 plgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREH--TTLVViAHRLSTIVEADTIL 545
|
....*..
gi 942446941 224 HMEDGAI 230
Cdd:PRK10790 546 VLHRGQA 552
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
151-233 |
2.29e-06 |
|
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: 47.90 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 151 AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHD-PRLMSHADRLLHMEDGA 229
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSElAEVLGLSDRVLVIGEGK 480
|
....
gi 942446941 230 IQQD 233
Cdd:TIGR02633 481 LKGD 484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-230 |
4.57e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMERFR--LEHTGFIFQG---FN 104
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLsiIPQSPVLFSGtvrFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 105 LFPS--------LTAIEQVQLPmgylGVSKRTSeeramaaledVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFA 176
Cdd:PLN03232 1330 IDPFsehndadlWEALERAHIK----DVIDRNP----------FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 177 DEPTSALDAesgqRVINILHRIART--YGVTTLCVSHDPRLMSHADRLLHMEDGAI 230
Cdd:PLN03232 1396 DEATASVDV----RTDSLIQRTIREefKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-184 |
5.53e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 6 SHSSQPVLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGI-----DL 80
Cdd:NF033858 260 DDDDEPAIEARGLTMRF--GDFTA--VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagDI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 81 STfsraameRFRLehtGFIFQGFNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQR 160
Cdd:NF033858 336 AT-------RRRV---GYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQR 405
|
170 180
....*....|....*....|....
gi 942446941 161 VAIARAVAKAPKLLFADEPTSALD 184
Cdd:NF033858 406 LSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-228 |
5.99e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQqpdSGKAIALGIDLSTFSRAAMERFRLehTGFIFQGFNLFPSLT 110
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK---TGGYIEGDIRISGFPKKQETFARI--SGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 AIEQVqLPMGYLGVSKRTSEERAMAALEDV-------GLSHRAHMYPA--QLSGGEKQRVAIARAVAKAPKLLFADEPTS 181
Cdd:PLN03140 970 VRESL-IYSAFLRLPKEVSKEEKMMFVDEVmelveldNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 942446941 182 ALDAESGQRVINILHRIARTyGVTTLCVSHDPR--LMSHADRLLHMEDG 228
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDT-GRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-230 |
6.43e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 11 PVLQAQDISKSFLTGSLtvpVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAI-ALGIDLSTFSRAAME 89
Cdd:PLN03073 507 PIISFSDASFGYPGGPL---LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrSAKVRMAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 90 RFRLEHTGFIFQgFNLFPsltaieqvqlpmgylGVskrtSEERAMAALEDVGLSHRAHMYPA-QLSGGEKQRVAIARAVA 168
Cdd:PLN03073 584 GLDLSSNPLLYM-MRCFP---------------GV----PEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITF 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 169 KAPKLLFADEPTSALDAESGQRVINILhrIARTYGVttLCVSHDPRLMSHA-DRLLHMEDGAI 230
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGV--LMVSHDEHLISGSvDELWVVSEGKV 702
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-225 |
7.05e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 131 ERAMAALEDVGLSHRAHMYPA-QLSGGEKQRVAIARAVAK---APKLLFADEPTSALDAESGQRVINILHRIARTyGVTT 206
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTV 885
|
90
....*....|....*....
gi 942446941 207 LCVSHDPRLMSHADRLLHM 225
Cdd:TIGR00630 886 VVIEHNLDVIKTADYIIDL 904
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
143-237 |
8.75e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 143 SHRAHMypAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVTTLCVSHDPRLMSHADRL 222
Cdd:PRK10982 384 GHRTQI--GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRI 461
|
90
....*....|....*...
gi 942446941 223 LHMEDG---AIQQDAQTS 237
Cdd:PRK10982 462 LVMSNGlvaGIVDTKTTT 479
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-234 |
9.90e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGcgkstllsllsglqqpdSGKAIALGI-----------DLSTFSRaamERFRLE---- 94
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNG-----------------AGKSTLLSLitgdhpqgysnDLTLFGR---RRGSGEtiwd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 95 ---HTGFIFQGFNL-FPSLTAIEQVQLPmGY---LGVSKRTSEER---AMAALEDVGLSHRAHMYPAQ-LSGGEKQRVAI 163
Cdd:PRK10938 334 ikkHIGYVSSSLHLdYRVSTSVRNVILS-GFfdsIGIYQAVSDRQqklAQQWLDILGIDKRTADAPFHsLSWGQQRLALI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 164 ARAVAKAPKLLFADEPTSALDAESGQ---RVINILHRIARTygvTTLCVSHD----PRLMSHadRLLHMEDGAI---QQD 233
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLISEGET---QLLFVSHHaedaPACITH--RLEFVPDGDIyryVQT 487
|
.
gi 942446941 234 A 234
Cdd:PRK10938 488 K 488
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-197 |
1.30e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 132 RAMAALEDVGLShrahmY-----PA-QLSGGEKQRVAIARAVAKA--PKLLFA-DEPTSALDAESGQRVINILHR 197
Cdd:COG0178 805 RKLQTLQDVGLG-----YiklgqPAtTLSGGEAQRVKLASELSKRstGKTLYIlDEPTTGLHFHDIRKLLEVLHR 874
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
31-232 |
1.49e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.85 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSgkaiALGIDLSTFSRAAMERFR-----LEHTGFIFQGfnl 105
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG----DIQIDGVSWNSVPLQKWRkafgvIPQKVFIFSG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 106 fpsltAIEQVQLPMGylgvskRTSEERAMAALEDVGLSHRAHMYPAQL-----------SGGEKQRVAIARAVAKAPKLL 174
Cdd:cd03289 92 -----TFRKNLDPYG------KWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 175 FADEPTSALDAESGQRVINIL-HRIArtyGVTTLCVSHDPRLMSHADRLLHMEDGAIQQ 232
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLkQAFA---DCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-230 |
1.60e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 13 LQAQDISKSFLTGsltvPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaialgIDLStfSRAAMERFR 92
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-----VKWS--ENANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 93 LEHTGFIFQGFNLFPSLTAIEQV----QLPMGYLGvskrtseeRAMAALEDVGLSHRAhmypaqLSGGEKQRVAIARAVA 168
Cdd:PRK15064 389 QDHAYDFENDLTLFDWMSQWRQEgddeQAVRGTLG--------RLLFSQDDIKKSVKV------LSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942446941 169 KAPKLLFADEPTSALDAESgqrvINILHRIARTYGVTTLCVSHDPRLMSH-ADRLLHMEDGAI 230
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDREFVSSlATRIIEITPDGV 513
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
44-226 |
3.12e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 44 LTLISGPSGCGKStllsllsglqqpdsgkAIALGIDLSTFSRAAMERFRLEHTgfifqgfnlfPSLTAIEQV--QLPMGY 121
Cdd:cd03240 24 LTLIVGQNGAGKT----------------TIIEALKYALTGELPPNSKGGAHD----------PKLIREGEVraQVKLAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 122 LGVSKRTSE-ERAMAALEDVGLSHRAHM------YPAQLSGGEKQ------RVAIARAV-AKAPkLLFADEPTSALDAEs 187
Cdd:cd03240 78 ENANGKKYTiTRSLAILENVIFCHQGESnwplldMRGRCSGGEKVlasliiRLALAETFgSNCG-ILALDEPTTNLDEE- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 942446941 188 gqRVINILHRIARTYGVTT----LCVSHDPRLMSHADRLLHME 226
Cdd:cd03240 156 --NIEESLAEIIEERKSQKnfqlIVITHDEELVDAADHIYRVE 196
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
153-223 |
3.37e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.22 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 153 LSGGEKQRVAIAravakapkLLFA------------DEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHAD 220
Cdd:cd03278 114 LSGGEKALTALA--------LLFAifrvrpspfcvlDEVDAALDDANVERFARLLKEFSK--ETQFIVITHRKGTMEAAD 183
|
...
gi 942446941 221 RLL 223
Cdd:cd03278 184 RLY 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
31-184 |
3.42e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.52 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSgkaiALGIDLSTFSRAAMERFR-----LEHTGFIFQG--- 102
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG----EIQIDGVSWNSVTLQTWRkafgvIPQKVFIFSGtfr 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 103 FNLFPsltaieqvqlpmgylgvSKRTSEERAMAALEDVGLSHRAHMYPAQ-----------LSGGEKQRVAIARAVAKAP 171
Cdd:TIGR01271 1310 KNLDP-----------------YEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKA 1372
|
170
....*....|...
gi 942446941 172 KLLFADEPTSALD 184
Cdd:TIGR01271 1373 KILLLDEPSAHLD 1385
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
132-198 |
3.79e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 3.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 132 RAMAALEDVGLShrahmY-----PA-QLSGGEKQRVAIARAVAKAP--KLLFA-DEPTSALDAESGQRVINILHRI 198
Cdd:PRK00349 809 RKLQTLVDVGLG-----YiklgqPAtTLSGGEAQRVKLAKELSKRStgKTLYIlDEPTTGLHFEDIRKLLEVLHRL 879
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-184 |
4.84e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 4.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 128 TSEERAMAALedVGLSHRAHMY---PAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALD 184
Cdd:PLN03073 319 TAEARAASIL--AGLSFTPEMQvkaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-184 |
7.56e-05 |
|
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: 42.92 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 17 DISKSFLTGSLTV-PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaialgidlstfsraamerfrLEH 95
Cdd:cd03291 37 DNNLFFSNLCLVGaPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK--------------------IKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 96 TG---FIFQGFNLFPSlTAIEQVQLPMGYlgvskrtSEERAMAALEDVGLSHRAHMYPAQ-----------LSGGEKQRV 161
Cdd:cd03291 97 SGrisFSSQFSWIMPG-TIKENIIFGVSY-------DEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARI 168
|
170 180
....*....|....*....|...
gi 942446941 162 AIARAVAKAPKLLFADEPTSALD 184
Cdd:cd03291 169 SLARAVYKDADLYLLDSPFGYLD 191
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
152-238 |
8.04e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 152 QLSGGEKQRVAIAravakapkLLFA------------DEPTSALDAESGQRVINILHRiaRTYGVTTLCVSHDPRLMSHA 219
Cdd:pfam02463 1077 LLSGGEKTLVALA--------LIFAiqkykpapfyllDEIDAALDDQNVSRVANLLKE--LSKNAQFIVISLREEMLEKA 1146
|
90
....*....|....*....
gi 942446941 220 DRLLhmedGAIQQDAQTSN 238
Cdd:pfam02463 1147 DKLV----GVTMVENGVST 1161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-184 |
8.16e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAAMeRFRL---EHTGFIFQG---F 103
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL-RKVLgiiPQAPVLFSGtvrF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 104 NLFPsLTAIEQVQLpmgylgvskRTSEERAMaaLEDV------GLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFAD 177
Cdd:PLN03130 1332 NLDP-FNEHNDADL---------WESLERAH--LKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
....*..
gi 942446941 178 EPTSALD 184
Cdd:PLN03130 1400 EATAAVD 1406
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
153-226 |
9.71e-05 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 42.57 E-value: 9.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 153 LSGGEKQRV-----AIARAVAKAPKLLFaDEPTSALDAESGQRVINILHRIARTYGVttLCVSHDPRLMSHADRLLHME 226
Cdd:cd03241 171 ASGGELSRLmlalkAILARKDAVPTLIF-DEIDTGISGEVAQAVGKKLKELSRSHQV--LCITHLPQVAAMADNHFLVE 246
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-222 |
1.08e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 31 VLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTFSRAamerfrleHTGFIFQGFNLFPSLT 110
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--------YCTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 111 AIEQVQLPMGYLgvskrTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQR 190
Cdd:PRK13541 87 VFENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180 190
....*....|....*....|....*....|..
gi 942446941 191 VINILHRIARTYGVtTLCVSHDPRLMSHADRL 222
Cdd:PRK13541 162 LNNLIVMKANSGGI-VLLSSHLESSIKSAQIL 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
128-226 |
1.43e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 128 TSEERAMAALEDVGLSHRAHMYPAQ-LSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESgqrVInILHRIARTYGVTT 206
Cdd:PRK10636 124 TIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VI-WLEKWLKSYQGTL 199
|
90 100
....*....|....*....|.
gi 942446941 207 LCVSHDPRLMSH-ADRLLHME 226
Cdd:PRK10636 200 ILISHDRDFLDPiVDKIIHIE 220
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-238 |
1.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 150 PAQLSGGEKQ------RVAIARAVAKA-------PKLLFaDEPTSALDAESGQRVINILHRIaRTYGV-TTLCVSHDPRL 215
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDSGHVSQLVDLVESM-RRLGVeQIVVVSHDDEL 856
|
90 100
....*....|....*....|...
gi 942446941 216 MSHADRLLHMEdgaiqQDAqTSN 238
Cdd:PRK02224 857 VGAADDLVRVE-----KDP-TTN 873
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-211 |
2.02e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 17 DISKSFLTgsltVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALG--IDLSTfSRAAMErfrlE 94
Cdd:PRK10982 3 NISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKS-SKEALE----N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 95 HTGFIFQGFNLFPSLTAIEQVQL---PMGYLGVSKRTSEERAMAALEDVGLSHRAHMYPAQLSGGEKQRVAIARAVAKAP 171
Cdd:PRK10982 74 GISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 942446941 172 KLLFADEPTSALDAESGQRVINILHRIaRTYGVTTLCVSH 211
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISH 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
151-231 |
2.33e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 151 AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGVttlcVSHDPRLM-SHADRLLHMEDGA 229
Cdd:PRK10636 429 RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVV----VSHDRHLLrSTTDDLYLVHDGK 504
|
..
gi 942446941 230 IQ 231
Cdd:PRK10636 505 VE 506
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-218 |
3.13e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKstllsllsglqqpdsgkaialgidlSTFSR--AAMERFRLEHTGFIFQGFNLF- 106
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGK-------------------------STLSAtlAGREDYEVTGGTVEFKGKDLLe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 107 --PSLTAIEQV----QLPMGYLGVSKR---------TSEERAMAAL-----EDVgLSHRAHM--YPAQL---------SG 155
Cdd:PRK09580 70 lsPEDRAGEGIfmafQYPVEIPGVSNQfflqtalnaVRSYRGQEPLdrfdfQDL-MEEKIALlkMPEDLltrsvnvgfSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 156 GEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRV---INILHRIARTYgvttLCVSHDPRLMSH 218
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVadgVNSLRDGKRSF----IIVTHYQRILDY 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
153-226 |
3.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 153 LSGGEKQ------RVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGvTTLCVSHDPRLMSHADRLLHME 226
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIP-QVIIVSHDEELKDAADYVIRVS 867
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-184 |
4.24e-04 |
|
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: 41.43 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 27 LTVPVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKaialgidlstfsraamerfrLEHTG---FIFQGF 103
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK--------------------IKHSGrisFSPQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 104 NLFPSlTAIEQVQLPMGYlGVSKRTSEERAMAALEDVGLSHRAHMYP-----AQLSGGEKQRVAIARAVAKAPKLLFADE 178
Cdd:TIGR01271 497 WIMPG-TIKDNIIFGLSY-DEYRYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDS 574
|
....*.
gi 942446941 179 PTSALD 184
Cdd:TIGR01271 575 PFTHLD 580
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
150-199 |
8.14e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 8.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 942446941 150 PAQLSGGEKQRVAIARAVAkapklLFADepTSALDAESGQRVINILHRIA 199
Cdd:COG0419 156 IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-220 |
8.14e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.16 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 30 PVLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGKAIALGIDLSTfSRAAMERfrleHTGFIFQGFNLFPSL 109
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQK----QLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 110 TAIEQVQLPMGYlgvskrtsEERAMAALEDVGLSHRAHM--YP-AQLSGGEKQRVAIARAVAKAPKLLFADEPTSALDAE 186
Cdd:PRK13540 90 TLRENCLYDIHF--------SPGAVGITELCRLFSLEHLidYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 942446941 187 SgqrVINILHRIA--RTYGVTTLCVSHDPRLMSHAD 220
Cdd:PRK13540 162 S---LLTIITKIQehRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
28-230 |
8.51e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 28 TVPVLRHLSLTVNPGELTLISGPSGCGKstllsllsglqqpdsgkaialgidlSTFSR--AAMERFRLEHTGFIFQGFNL 105
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGK-------------------------STLSKviAGHPAYKILEGDILFKGESI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 106 FpSLTAIEQVQL--------PMGYLGVS-----------KRTSE-----------ERAMAALEDVGLS-HRAHMYPAQ-L 153
Cdd:CHL00131 74 L-DLEPEERAHLgiflafqyPIEIPGVSnadflrlaynsKRKFQglpeldpleflEIINEKLKLVGMDpSFLSRNVNEgF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942446941 154 SGGEKQRVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTyGVTTLCVSHDPRLMSH--ADRLLHMEDGAI 230
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYikPDYVHVMQNGKI 230
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
153-220 |
8.63e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 8.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942446941 153 LSGGEKQ------RVAIARAVAKAPKLLFADEPTSALDAESGQRVINILHRIARTYGV--TTLCVSHDPRLMSHAD 220
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDipQVIMISHHRELLSVAD 877
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
151-197 |
1.85e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.44 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 151 AQLSGGEKQR---VAIARAVA----------KAPKLLFADEPTSALDAESGQRVINILHR 197
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
151-235 |
2.09e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 151 AQLSGGEKQRVAIARAVAKAPK---LLFADEPTSALDAESGQRVINILhRIARTYGVTTLCVSHDPRLMSHADRLLHMED 227
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQL-RTLVSLGHSVIYIDHDPALLKQADYLIEMGP 1776
|
....*...
gi 942446941 228 GAIQQDAQ 235
Cdd:PRK00635 1777 GSGKTGGK 1784
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
152-221 |
2.38e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.01 E-value: 2.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942446941 152 QLSGGEKQRVAIA-----RAVAKAPKLLFaDEPTSALDAESGQRVINILHRIARtyGVTTLCVSHDPRLMSHADR 221
Cdd:cd03272 158 QLSGGQKSLVALAlifaiQKCDPAPFYLF-DEIDAALDAQYRTAVANMIKELSD--GAQFITTTFRPELLEVADK 229
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
137-225 |
3.59e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 137 LEDVGLShrahmY-----PAQ-LSGGEKQRVAIARA-------VakapklLFA-DEPTSAL---DAEsgqRVINILHRIa 199
Cdd:COG0178 469 LVDVGLD-----YltldrSAGtLSGGEAQRIRLATQigsglvgV------LYVlDEPSIGLhqrDND---RLIETLKRL- 533
|
90 100
....*....|....*....|....*.
gi 942446941 200 RTYGVTTLCVSHDPRLMSHADRLLHM 225
Cdd:COG0178 534 RDLGNTVIVVEHDEDTIRAADYIIDI 559
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-225 |
4.24e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 136 ALEDVGLSHRAHMYP-AQLSGGEKQRVAIAR---AVAKAPKLLFADEPTSALDAESGQRVINILHRIarTY-GVTTLCVS 210
Cdd:PRK00635 792 ALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSL--THqGHTVVIIE 869
|
90
....*....|....*
gi 942446941 211 HDPRLMSHADRLLHM 225
Cdd:PRK00635 870 HNMHVVKVADYVLEL 884
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-186 |
5.50e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.41 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 12 VLQAQDISKSFltGSLTVpvLRHLSLTVNPGELTLISGPSGCGKSTLLSLLSGLQQPDSGkAIALGidlSTFSRAAMERF 91
Cdd:PRK11819 324 VIEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG-TIKIG---ETVKLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942446941 92 RLehtgfifqgfNLFPSLTAIEQVQLPMGYLGVSKRTSEERAMAAL---------EDVGlshrahmypaQLSGGEKQRVA 162
Cdd:PRK11819 396 RD----------ALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGRfnfkggdqqKKVG----------VLSGGERNRLH 455
|
170 180
....*....|....*....|....
gi 942446941 163 IARAVAKAPKLLFADEPTSALDAE 186
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| |
