|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
4.76e-97 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 283.09 E-value: 4.76e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEK----ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAL 76
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 77 ADLRRKQMGFVFQQPTLLKNLNVLDNIVLPAQ-KGNEKQADNlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRA 155
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLlAGVSRKERR--ERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-218 |
2.23e-87 |
|
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: 258.19 E-value: 2.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQEK----ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLR 80
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 RKQMGFVFQQPTLLKNLNVLDNIVLPAQKGNEKQADNlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKER-RERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-223 |
7.93e-66 |
|
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: 203.82 E-value: 7.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEK----ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADL 79
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRKQMGFVFQQPTLLKNLNVLDNIVLPAQKGNEKQAdnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGD 159
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA---RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVTHDAKVAAQTQRVLFMSDGQIVSEMQ 223
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-220 |
4.40e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 194.12 E-value: 4.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEK-ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRK 82
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 83 qMGFVFQQPTLLKNLNVLDNIVLP--AQKGNEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:COG2884 81 -IGVVFQDFRLLPDRTVYENVALPlrVTGKSRKEIR---RRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAK-VAAQTQRVLFMSDGQIVS 220
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElVDRMPKRVLELEDGRLVR 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-219 |
1.30e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 186.03 E-value: 1.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 3 KMIVGTNIEKSF-GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRR 81
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 82 kQMGFVFQQPTLLKNLNVLDNI-------------VLPAQKGNEKQadnlmkKGQTLMEKMGIAGLEQRDITQVSGGQLQ 148
Cdd:COG3638 81 -RIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsLLGLFPPEDRE------RALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 149 RAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQG--TAIClVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVV-NLHQVDLARRyADRIIGLRDGRVV 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-219 |
5.37e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 181.73 E-value: 5.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELaTLSENALADLRRKq 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLP---AQKGNEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLApikVKKMSKAEAE---ERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD----AKVAaqtQRVLFMSDGQIV 219
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEmgfaREVA---DRVVFMDGGRIV 215
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-213 |
1.38e-56 |
|
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: 179.35 E-value: 1.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFV 87
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVLP--AQKGNEKQADNLMKKgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGlkYKKLSKKEKREKKKE---ALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2519204862 166 DEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFM 213
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-217 |
1.45e-55 |
|
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: 175.84 E-value: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlRRKQMGFVF 88
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--LRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPaqkgnekqadnlmkkgqtlmekmgiagleqrditqVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03229 83 QDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQ-GTAICLVTHD-AKVAAQTQRVLFMSDGQ 217
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQlGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
2.82e-55 |
|
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: 177.54 E-value: 2.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQ 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDnIVL----PAQKGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGD 159
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRE-LVAlgryPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVTHDAKVAAQT-QRVLFMSDGQIVSE 221
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQ 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-218 |
1.85e-54 |
|
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: 174.25 E-value: 1.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELaTLSENALADLRRKqMGFV 87
Cdd:cd03262 4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQK-VGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVLP---AQKGNEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:cd03262 82 FQQFNLFPHLTVLENITLApikVKGMSKAEAE---ERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD---AKVAAqtQRVLFMSDGQI 218
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEmgfAREVA--DRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-219 |
6.43e-54 |
|
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: 173.91 E-value: 6.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEK-ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRkQMGFV 87
Cdd:cd03256 5 NLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR-QIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVLP--AQKGNEKQADNLMKKGQT-----LMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:cd03256 84 FQQFNLIERLSVLENVLSGrlGRRSTWRSLFGLFPKEEKqralaALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-219 |
6.64e-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: 172.70 E-value: 6.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnaladlRRKQMGFV 87
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVLP--AQKGNEKQADNLMKKgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGlkLRGVPKAEIRARVRE---LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 166 DEPTGALNSKSAQEIMTLLSEI-NQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDqEEALALADRIAVMNEGRIV 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-220 |
9.58e-54 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 183.39 E-value: 9.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSF----GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQ 83
Cdd:PRK10535 8 KDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLPA-QKGNEKQADnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAvYAGLERKQR--LLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQIVS 220
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-218 |
4.70e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 4.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVF 88
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW----RRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNlNVLDNIVLPAQKGNEKQADNLMKKgqtLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDE 167
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDRERALE---LLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 168 PTGALNSKSAQEIMTLLSE-INQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQI 218
Cdd:COG4619 157 PTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-218 |
6.34e-53 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 170.67 E-value: 6.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFG----QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADL 79
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRKQMGFVFQQPTLLKNLNVLDNIVLPAQKGNEKQADNLMKKGQTLmEKMGIAGLEQRDITQVSGGQLQRAGICRALMGD 159
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVL-NLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-219 |
2.02e-52 |
|
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: 169.61 E-value: 2.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSF----GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnALADLRRKQM 84
Cdd:cd03257 6 NLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR-RLRKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 85 GFVFQQPtlLKNLN----VLDNI--VLPAQKGNEKQADNLMKKGQtLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALM 157
Cdd:cd03257 85 QMVFQDP--MSSLNprmtIGEQIaePLRIHGKLSKKEARKEAVLL-LLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-222 |
2.52e-52 |
|
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: 169.19 E-value: 2.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQE----KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATlsenaladlRRKQM 84
Cdd:cd03293 5 NVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 85 GFVFQQPTLLKNLNVLDNIVLP--AQKGNEKQAdnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGleLQGVPKAEA---RERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEI-NQQGTAICLVTHD-AKVAAQTQRVLFMS--DGQIVSEM 222
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDiDEAVFLADRVVVLSarPGRIVAEV 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-221 |
7.56e-52 |
|
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: 168.14 E-value: 7.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQ----EKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADL 79
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRkQMGFVFQQPTLLKNLNVLDNIVLPAQKGNEKQADnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGD 159
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAE-IEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-219 |
7.93e-52 |
|
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: 168.23 E-value: 7.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLR 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 RKqMGFVFQQPTLLKNLNVLDNIVLP---AQKGNEKQADNL--MKkgqtlMEKMGIAGLEQRDITQVSGGQLQRAGICRA 155
Cdd:COG1127 82 RR-IGMLFQGGALFDSLTVFENVAFPlreHTDLSEAEIRELvlEK-----LELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIaDRVAVLADGKII 221
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-217 |
8.48e-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: 167.43 E-value: 8.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSF-GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRK 82
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 83 qMGFVFQQPTLLKNLNVLDNIVLP----AQKGNEKQadnlmKKGQTLMEKMGiagLEQRDIT---QVSGGQLQRAGICRA 155
Cdd:TIGR02673 81 -IGVVFQDFRLLPDRTVYENVALPlevrGKKEREIQ-----RRVGAALRQVG---LEHKADAfpeQLSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQ 217
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVaHRVIILDDGR 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-222 |
1.38e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 168.34 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEK----ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaladlrrKQM 84
Cdd:COG1116 12 GVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---------PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 85 GFVFQQPTLLKNLNVLDNIVLP--AQKGNEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGleLRGVPKAERR---ERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEI-NQQGTAICLVTHD-------AkvaaqtQRVLFMSD--GQIVSEM 222
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDvdeavflA------DRVVVLSArpGRIVEEI 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-219 |
5.54e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 166.86 E-value: 5.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATlsenalaDL--RRKQMGF 86
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-------NLppRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 VFQQPTLLKNLNVLDNIV--LPAQKGNEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:COG1118 80 VFQHYALFPHMTVAENIAfgLRVRPPSKAEIR---ARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEI--NQQGTAIcLVTHD----AKVAaqtQRVLFMSDGQIV 219
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLhdELGGTTV-FVTHDqeeaLELA---DRVVVMNQGRIE 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-222 |
6.30e-50 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 163.45 E-value: 6.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQQPTLLK 95
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 NLNVLDNIVLPAQKGNEKQADnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSK 175
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKPAE-INSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2519204862 176 SAQEIMTLLSEIN-QQGTAICLVTHDAKVAAQTQRVLFMSDGQIVSEM 222
Cdd:PRK11629 180 NADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-242 |
1.17e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.54 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAladlrRKQMGFV 87
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-----RRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVLPAQ-KGNEKqaDNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARlYGLPR--KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQIVSEMQffPED--DLNLEEKMVQVTEK 242
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGT--PDElkARLLEDVFLELTGE 233
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-219 |
2.38e-49 |
|
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: 162.08 E-value: 2.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFG-QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRK 82
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 83 qMGFVFQQPTLLKNLNVLDNIVLP--AQKGNEKQADNLMKKGQT-----LMEKMGIAGLEQRDITQVSGGQLQRAGICRA 155
Cdd:TIGR02315 81 -IGMIFQHYNLIERLTVLENVLHGrlGYKPTWRSLLGRFSEEDKeralsALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVT-HDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINlHQVDLAKKyADRIVGLKAGEIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-219 |
5.60e-49 |
|
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: 168.16 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQE-----KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKq 83
Cdd:COG1123 265 NLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRR- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPT--LLKNLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:COG1123 344 VQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:COG1123 424 KLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-221 |
8.37e-49 |
|
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: 160.36 E-value: 8.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKqMGFVF 88
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR-MGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAqkgNEKQADNLMKKGQTLMEKMGIAGLEQRD---ITQVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:cd03261 84 QSGALFDSLTVFENVAFPL---REHTRLSEEEIREIVLEKLEAVGLRGAEdlyPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 166 DEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQT-QRVLFMSDGQIVSE 221
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAE 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-219 |
8.56e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 163.71 E-value: 8.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSF----GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADL 79
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRKqMGFVFQQPTLLKNLNVLDNIVLP---AQKGNEKQAdnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRAL 156
Cdd:COG1135 81 RRK-IGMIFQHFNLLSSRTVAENVALPleiAGVPKAEIR----KRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 157 MGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRIcDRVAVLENGRIV 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-221 |
1.06e-47 |
|
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: 155.67 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQMGFVF 88
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA----RKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QqptllknlnvldnivlpaqkgnekqadnlmkkgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03214 80 Q-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-222 |
1.20e-47 |
|
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: 158.04 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQ----EKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELatlSENALADL 79
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRkQMGFVFQQPTLLKN--LNVLDNIVLPAQ----KGNEKQADNLMkkgqtlmEKMGI-AGLEQRDITQVSGGQLQRAGI 152
Cdd:COG1124 78 RR-RVQMVFQDPYASLHprHTVDRILAEPLRihglPDREERIAELL-------EQVGLpPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 153 CRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSEM 222
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-217 |
2.40e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 156.09 E-value: 2.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRKqMGFVFQQP-TL 93
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRK-VGLVFQNPdDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNLNVLDNIVLPAQkgNEKQADNLMKKGQT-LMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:cd03225 88 FFGPTVEEEVAFGLE--NLGLPEEEIEERVEeALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2519204862 173 NSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQ 217
Cdd:cd03225 166 DPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-219 |
3.48e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 159.88 E-value: 3.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlR 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 RkQMGFVFQQPTLLKNLNVLDNIV--LPAQKGNEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMG 158
Cdd:COG3842 77 R-NVGMVFQDYALFPHLTVAENVAfgLRMRGVPKAEIR---ARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 159 DPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDakvaaQTQ------RVLFMSDGQIV 219
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHD-----QEEalaladRIAVMNDGRIE 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-221 |
6.32e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 155.57 E-value: 6.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELatlSENALADLRRKqMGFVFQQP-TL 93
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRK-VGLVFQNPdDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNLNVLDNIVL-PAQKG-NEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGA 171
Cdd:COG1122 88 LFAPTVEEDVAFgPENLGlPREEIR---ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 172 LNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSE 221
Cdd:COG1122 165 LDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-221 |
1.58e-46 |
|
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: 154.52 E-value: 1.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrRKQMGFVF 88
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA---RLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQ---------KGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGD 159
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQartgsglllARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAE 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-218 |
3.45e-46 |
|
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: 154.03 E-value: 3.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLsenalaDLRRKQM 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 85 GFVFQQPTLLKNLNVLDNIV--LPAQKGNEKQADNLMK-KGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQ 161
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAfgLRVKPRSERPPEAEIRaKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQI 218
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-219 |
7.75e-46 |
|
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: 159.68 E-value: 7.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSF--GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID---EGSVQFDGKELATLSEna 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 76 laDLRRKQMGFVFQQP-TLLKNLNVLDNI--VLPAQKGNEKQADNLMKKgqtLMEKMGIAGLEQRDITQVSGGQLQRAGI 152
Cdd:COG1123 79 --ALRGRRIGMVFQDPmTQLNPVTVGDQIaeALENLGLSRAEARARVLE---LLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 153 CRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEiADRVVVMDDGRIV 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-218 |
1.03e-45 |
|
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: 151.79 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKqMGFVFQQPTLLKNLNV 99
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNIVLPAQKGNEKQADnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQE 179
Cdd:cd03292 96 YENVAFALEVTGVPPRE-IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2519204862 180 IMTLLSEINQQGTAICLVTHDAKVAAQTQ-RVLFMSDGQI 218
Cdd:cd03292 175 IMNLLKKINKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-219 |
1.70e-45 |
|
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: 151.56 E-value: 1.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEI-----DEGSVQFDGKELATLSENALAdlRRK 82
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLE--LRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 83 QMGFVFQQPTLLkNLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGLEQR--DITQVSGGQLQRAGICRALMGDP 160
Cdd:cd03260 82 RVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEYTIV-IVTHNMQQAARvADRTAFLLNGRLV 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
6.87e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.62 E-value: 6.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELAtlsenaladLR 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR---------RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 RKQMGFVFQQPTLLKN--LNVLDnIVL-----------PAQKGNEKQADNlmkkgqtLMEKMGIAGLEQRDITQVSGGQL 147
Cdd:COG1121 74 RRRIGYVPQRAEVDWDfpITVRD-VVLmgrygrrglfrRPSRADREAVDE-------ALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 148 QRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQI 218
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-219 |
8.17e-45 |
|
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: 152.51 E-value: 8.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQE----KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDE---IDEGSVQFDGKELATLSENALADLRR 81
Cdd:COG0444 6 NLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKIRG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 82 KQMGFVFQQPtlLKNLN----VLDNIVLPA---QKGNEKQADnlmKKGQTLMEKMGIAGLEQRdIT----QVSGGQLQRA 150
Cdd:COG0444 86 REIQMIFQDP--MTSLNpvmtVGDQIAEPLrihGGLSKAEAR---ERAIELLERVGLPDPERR-LDryphELSGGMRQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 151 GICRALMGDPQIIFGDEPTGALN-SKSAQeIMTLLSEINQQ-GTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDvTIQAQ-ILNLLKDLQRElGLAILFITHDLGVVAEIaDRVAVMYAGRIV 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-218 |
3.45e-44 |
|
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: 146.77 E-value: 3.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAladlrRKQM 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV-----KRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 85 GFVFQQPTLLKNLNVLDNIVLpaqkgnekqadnlmkkgqtlmekmgiagleqrditqvSGGQLQRAGICRALMGDPQIIF 164
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLKL-------------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQI 218
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-218 |
4.84e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 151.77 E-value: 4.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnaladlRRKQMGFVF 88
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNI-----VLPAQKgnEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQII 163
Cdd:PRK10851 81 QHYALFRHMTVFDNIafgltVLPRRE--RPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEINQQ--GTAIcLVTHDAKVAAQ-TQRVLFMSDGQI 218
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEElkFTSV-FVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-219 |
1.23e-43 |
|
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: 147.00 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlrRKQMGFVF 88
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQKGNEKQADnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAE-IKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVA-AQTQRVLFMSDGQIV 219
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEAlTMSDRIAVMNKGKIQ 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
10-221 |
1.38e-43 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 146.85 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 10 IEKSFGQEK----ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMG 85
Cdd:PRK10584 12 LKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 86 FVFQQPTLLKNLNVLDNIVLPAQKGNEKQADNlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGESSRQS-RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 166 DEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-219 |
2.26e-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: 145.09 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 10 IEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQ 89
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 90 QPTLLKNLNVLDNIVLPAQKGNEKQADNLmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAERE-ERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 170 GALNSKSAQEIMTLLSEIN-QQGTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:cd03294 189 SALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLgDRIAIMKDGRLV 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-200 |
7.88e-42 |
|
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: 141.90 E-value: 7.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 13 SFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELAtlsenaladLRRKQMGFVFQQPT 92
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE---------KERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 LLKN--LNVLDNIVLPAQK-----GNEKQADnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:cd03235 79 IDRDfpISVRDVVLMGLYGhkglfRRLSKAD--KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2519204862 166 DEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD 200
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHD 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-221 |
1.51e-41 |
|
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: 142.49 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrkQMGFV- 87
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA-----RLGIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 -FQQPTLLKNLNVLDNIVLPAQ--------------KGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGI 152
Cdd:COG0411 84 tFQNPRLFPELTVLENVLVAAHarlgrgllaallrlPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 153 CRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVTHDAK-VAAQTQRVLFMSDGQIVSE 221
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDlVMGLADRIVVLDFGRVIAE 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-219 |
6.92e-41 |
|
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: 148.44 E-value: 6.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRkQMGFVFQQPTLL 94
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRR-QIGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 kNLNVLDNIVLpaqkGNEKQADnlmkkgQTLMEKMGIAGLEQrDI--------TQV-------SGGQLQRAGICRALMGD 159
Cdd:COG2274 562 -SGTIRENITL----GDPDATD------EEIIEAARLAGLHD-FIealpmgydTVVgeggsnlSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLKGRTVI-IIAHRLSTIRLADRIIVLDKGRIV 688
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-217 |
7.41e-41 |
|
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: 137.76 E-value: 7.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFV 87
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----RRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQptllknlnvldnivlpaqkgnekqadnlmkkgqtlmekmgiagleqrditqvSGGQLQRAGICRALMGDPQIIFGDE 167
Cdd:cd00267 79 PQL----------------------------------------------------SGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 168 PTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQ 217
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-221 |
4.12e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 138.75 E-value: 4.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRrkq 83
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 mGFVFQQPTLLKNLNVLDnIV----LPAQkGNEKQADNLMkkgQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALM-- 157
Cdd:PRK13548 79 -AVLPQHSSLSFPFTVEE-VVamgrAPHG-LSRAEDDALV---AAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 158 ----GDPQIIFGDEPTGALNSKSAQEIMTLLSEI-NQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVAD 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-219 |
8.93e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 140.21 E-value: 8.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnaladlRRKQMGFVF 88
Cdd:COG3839 8 NVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP------KDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLP--AQKGNEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:COG3839 82 QSYALYPHMTVYENIAFPlkLRKVPKAEID---RRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAkVAAQT--QRVLFMSDGQIV 219
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQ-VEAMTlaDRIAVMNDGRIQ 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-217 |
1.39e-39 |
|
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: 134.82 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLL 94
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 kNLNVLDNIvlpaqkgnekqadnlmkkgqtlmekmgiagleqrditqVSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:cd03228 89 -SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2519204862 175 KSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQ 217
Cdd:cd03228 130 ETEALILEALRALAKGKTVI-VIAHRLSTIRDADRIIVLDDGR 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-219 |
2.53e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 139.17 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKI----LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADL 79
Cdd:PRK11153 1 MIELKNISKVFPQGGRtihaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRkQMGFVFQQPTLLKNLNVLDNIVLPAQKGNEKQADnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGD 159
Cdd:PRK11153 81 RR-QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAE-IKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRIcDRVAVIDAGRLV 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-219 |
2.72e-39 |
|
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: 135.46 E-value: 2.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlrRKQMGFVF 88
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------DRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQKGNEKQaDNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPK-DEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVA-AQTQRVLFMSDGQIV 219
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAmTMADRIAVMNDGQIQ 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-210 |
6.95e-39 |
|
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: 134.14 E-value: 6.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAladlrRKQ 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-----RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLPAQ-KGNEKQADNLmkkgQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAAlYGLRADREAI----DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRV 210
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-219 |
1.16e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 134.76 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKEL---ATLSENALADLRRKqMG 85
Cdd:COG4161 7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQK-VG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 86 FVFQQPTLLKNLNVLDNIV---LPAQKGNEKQAdnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:COG4161 86 MVFQQYNLWPHLTVMENLIeapCKVLGLSKEQA---REKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVaSQVVYMEKGRII 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-218 |
1.39e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 134.45 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGkeLATLSENALADLRRKQ 83
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVL-PAQ-KGNEKQADNlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQ 161
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFgPLRvRGASKEEAE--KQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQI 218
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRI 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-219 |
7.18e-38 |
|
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: 132.42 E-value: 7.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSF-GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnalADLRRKqMGFV 87
Cdd:cd03295 5 NVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP---VELRRK-IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVL-PAQKGNEKQ-----ADNLMKkgqtlMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQ 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALvPKLLKWPKEkirerADELLA-----LVGLDPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-200 |
1.15e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 132.68 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenalADlrRkqmGFVFQQPTLLKNLN 98
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----AD--R---GVVFQKDALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQ-KGNEKQADNlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSA 177
Cdd:COG4525 93 VLDNVAFGLRlRGVPKAERR--ARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTR 170
|
170 180
....*....|....*....|....
gi 2519204862 178 QEIMTLLSEI-NQQGTAICLVTHD 200
Cdd:COG4525 171 EQMQELLLDVwQRTGKGVFLITHS 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-219 |
3.43e-37 |
|
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: 137.20 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLL 94
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQNPYLF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KnLNVLDNIVLpaqkGNEKQADNLMkkgQTLMEKMGIA--------GLEqrdiTQV-------SGGQLQRAGICRALMGD 159
Cdd:COG4988 424 A-GTIRENLRL----GRPDASDEEL---EAALEAAGLDefvaalpdGLD----TPLgeggrglSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAKGRTVI-LITHRLALLAQADRILVLDDGRIV 550
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-219 |
7.73e-37 |
|
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: 136.05 E-value: 7.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLL 94
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL----RRRIAVVPQRPHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 kNLNVLDNIVLPAQKGNEKQ----------ADNLMKKGQTLMEKMGIAGleqrdiTQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:COG4987 422 -DTTLRENLRLARPDATDEElwaalervglGDWLAALPDGLDTWLGEGG------RRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALAGRTVL-LITHRLAGLERMDRILVLEDGRIV 548
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-219 |
1.43e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 129.21 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenalaDLRRKQ 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-----REARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLPAqKGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQII 163
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFA-ELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAK-VAAQTQRVLFMSDGQIV 219
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQeVEALCDRVVILHKGKVV 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-221 |
2.03e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 128.32 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrRKQMGFVF 88
Cdd:cd03224 5 NLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---RAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQKGNEkqadnlmKKGQTLMEKMgiagLE---------QRDITQVSGGQLQRAGICRALMGD 159
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYARRR-------AKRKARLERV----YElfprlkerrKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLE 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-223 |
6.08e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 127.89 E-value: 6.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaladlrrKQ 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG---------AE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLPAQKGNEKQADNLMKKGQTLmEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQII 163
Cdd:PRK11248 72 RGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQML-KKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVTHDAKVAA--QTQRVLFMSD-GQIVSEMQ 223
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQeTGKQVLLITHDIEEAVfmATELVLLSPGpGRVVERLP 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-221 |
8.66e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.56 E-value: 8.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATL----SENALADL 79
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRKQMGFVFQQPTLLKNLNVLDNIVL-PAQ-KGNEKQAdnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALM 157
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEgPVIvKGEPKEE--ATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-219 |
1.65e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKIlrNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenalADLRRKQ 83
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----PAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MgfVFQQPTLLKNLNVLDNIVL---PAQKGNEKQADNLmkkgQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:COG3840 75 M--LFQENNLFPHLTVAQNIGLglrPGLKLTAEQRAQV----EQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDpEDAARIADRVLLVADGRIA 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-219 |
2.60e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 125.90 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSV-----QFDGKelATLSENALADLRRKq 83
Cdd:PRK11124 7 GINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDFS--KTPSDKAIRELRRN- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLPAQK--G-NEKQAdnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNLIEAPCRvlGlSKDQA---LARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTaSRVVYMENGHIV 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-169 |
3.40e-35 |
|
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: 122.76 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnalaDLRRKQMGFVFQQPTLLKNLNV 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 100 LDNIVLPAQ-KGNEKQADNlmKKGQTLMEKMGIAGLEQR----DITQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:pfam00005 77 RENLRLGLLlKGLSKREKD--ARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-219 |
4.66e-35 |
|
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: 125.14 E-value: 4.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKiLRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlrRKQMGFVF 88
Cdd:cd03299 5 NLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIV--LPAQKGNEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:cd03299 78 QNYALFPHMTVYKNIAygLKKRKVDKKEIE---RKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDfEEAWALADKVAIMLNGKLI 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-211 |
2.70e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 122.21 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID---EGSVQFDGKELATLSenaladLRRKQMGFVFQQP 91
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP------AEQRRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 92 TLLKNLNVLDNIV--LPAQ-KGNEKQAdnlmkKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:COG4136 86 LLFPHLSVGENLAfaLPPTiGRAQRRA-----RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2519204862 169 TGALNSKSAQEIMTL-LSEINQQGTAICLVTHDAKVAAQTQRVL 211
Cdd:COG4136 161 FSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-218 |
2.25e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 121.66 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGM---DEIDEGSVQFDGKELAtlSENALA 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQ--REGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 78 -DLR--RKQMGFVFQQPTLLKNLNVLDNIVL-----------------PAQKGNEKQAdnlmkkgqtlMEKMGIAGLEQR 137
Cdd:PRK09984 79 rDIRksRANTGYIFQQFNLVNRLSVLENVLIgalgstpfwrtcfswftREQKQRALQA----------LTRVGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 138 DITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSD 215
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRyCERIVALRQ 228
|
...
gi 2519204862 216 GQI 218
Cdd:PRK09984 229 GHV 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
10-220 |
2.32e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 120.09 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 10 IEKSFGQEKIlrNVSVEIEaGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQ 89
Cdd:cd03297 6 IEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 90 QPTLLKNLNVLDNIVLpaqkGNEKQADNLMK-KGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03297 83 QYALFPHLNVRENLAF----GLKRKRNREDRiSVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQ--QGTAIcLVTHDAKVAAQ-TQRVLFMSDGQIVS 220
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKnlNIPVI-FVTHDLSEAEYlADRIVVMEDGRLQY 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-219 |
2.63e-33 |
|
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: 119.92 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQE--KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAladlrRKQMGF 86
Cdd:cd03263 5 NLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-----RQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 VFQQPTLLKNLNVLDNIVLPAQ-KG-NEKQADNLMKKgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARlKGlPKSEIKEEVEL---LLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEInQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-219 |
3.46e-33 |
|
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: 119.28 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFG-QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelatlseNALADLRRKQMGFV 87
Cdd:cd03226 4 NISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-------PIKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTL-LKNLNVLDNIVLPAqkgneKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:cd03226 77 MQDVDYqLFTDSVREELLLGL-----KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-219 |
4.86e-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: 125.18 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 13 SFGQEK----ILRNVSVEIEAGEFVSIMGPSGSGKTtlMFALSGM------DEIDEGSVQFDGKELATLSENALADLRRK 82
Cdd:COG4172 15 AFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKS--VTALSILrllpdpAAHPSGSILFDGQDLLGLSERELRRIRGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 83 QMGFVFQQPtlLKNLNVLDNI------VLPAQKG-NEKQAdnlMKKGQTLMEKMGIAGLEQRdIT----QVSGGQLQRAG 151
Cdd:COG4172 93 RIAMIFQEP--MTSLNPLHTIgkqiaeVLRLHRGlSGAAA---RARALELLERVGIPDPERR-LDayphQLSGGQRQRVM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 152 ICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHD----AKVAaqtQRVLFMSDGQIV 219
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDlgvvRRFA---DRVAVMRQGEIV 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-218 |
7.38e-33 |
|
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: 117.32 E-value: 7.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLL 94
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL----GDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNlNVLDNIVlpaqkgnekqadnlmkkgqtlmekmgiagleqrditqvSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:cd03246 89 SG-SIAENIL--------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2519204862 175 KSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:cd03246 130 EGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-247 |
2.49e-32 |
|
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: 119.09 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKqMGFVFQQP---- 91
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKK-VGLVFQFPehql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 92 ---TLLK-------NLNVldnivlpaqkgNEKQADNLMKKgqtLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:TIGR04521 96 feeTVYKdiafgpkNLGL-----------SEEEAEERVKE---ALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAK-VAAQTQRVLFMSDGQIVSE---MQFFPEDDLnLEEK 235
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEdVAEYADRVIVMHKGKIVLDgtpREVFSDVDE-LEKI 240
|
250
....*....|....*
gi 2519204862 236 MV---QVTEKMREIE 247
Cdd:TIGR04521 241 GLdvpEITELARKLK 255
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
8-218 |
5.62e-32 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 117.59 E-value: 5.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAL----ADLR--- 80
Cdd:COG4598 12 RDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGelvpADRRqlq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 --RKQMGFVFQQPTLLKNLNVLDNIV---LPAQKGNEKQAdnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRA 155
Cdd:COG4598 92 riRTRLGMVFQSFNLWSHMTVLENVIeapVHVLGRPKAEA---IERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQI 218
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDvSSHVVFLHQGRI 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-221 |
6.34e-32 |
|
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: 116.87 E-value: 6.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrRKQMGFVF 88
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA---RLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNI--VLPAQKGNEKQadnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:cd03218 82 QEASIFRKLTVEENIlaVLEIRGLSKKE---REEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAK-VAAQTQRVLFMSDGQIVSE 221
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAE 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-219 |
8.39e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.20 E-value: 8.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRkQMGFVFQQPTLL 94
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRR-QIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 kNLNVLDNIVLpaqkGNEKQADnlmkkgQTLMEKMGIAGLEQrDI--------TQV-------SGGQLQRAGICRALMGD 159
Cdd:COG1132 427 -SGTIRENIRY----GRPDATD------EEVEEAAKAAQAHE-FIealpdgydTVVgergvnlSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGRTTI-VIAHRLSTIRNADRILVLDDGRIV 553
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-219 |
9.36e-31 |
|
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: 113.45 E-value: 9.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRkQMGFVFQQPTLLK 95
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRR-NIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 NlNVLDNIVLPAQKGNEkqadnlmkkgQTLMEKMGIAGLEQ----------RDI----TQVSGGQLQRAGICRALMGDPQ 161
Cdd:cd03245 92 G-TLRDNITLGAPLADD----------ERILRAAELAGVTDfvnkhpngldLQIgergRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLI-IITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-219 |
1.05e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.43 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSF-GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRk 82
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 83 QMGFVFQQPTLLKNLNVLDNIVLPAQKGNeKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAG-ASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDiGLISRRSYRMLTLSDGHLH 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-219 |
1.10e-30 |
|
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: 112.64 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 2 KKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSG--MDEIDEGSVQFDGKelaTLSENALadl 79
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGR---PLDKRSF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 rRKQMGFVFQQPTLLKNLNVLDNIVLPAQkgnekqadnlmkkgqtlmekmgiagleqrdITQVSGGQLQRAGICRALMGD 159
Cdd:cd03213 81 -RKIIGYVPQDDILHPTLTVRETLMFAAK------------------------------LRGLSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD--AKVAAQTQRVLFMSDGQIV 219
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpsSEIFELFDKLLLLSQGRVI 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-219 |
1.86e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 113.64 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQ 83
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDnivL------PAQKGNEKQADNlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALM 157
Cdd:COG4604 77 LAILRQENHINSRLTVRE---LvafgrfPYSKGRLTAEDR--EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEI-NQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-219 |
3.56e-30 |
|
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: 112.38 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrRKQMGFVF 88
Cdd:COG0410 8 NLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA---RLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQKGNEKqadnlmKKGQTLMEKmgIAGL-----EQRDI--TQVSGGQLQRAGICRALMGDPQ 161
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYARRDR------AEVRADLER--VYELfprlkERRRQraGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEiADRAYVLERGRIV 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-219 |
3.77e-30 |
|
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: 112.32 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 17 EKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRkQMGFVfQQPTLLKN 96
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRR-QIGLV-SQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 97 LNVLDNIVLPAQKGNEKQA----------DNLMKKGQTLMEKMGIAGleqrdiTQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:cd03251 90 DTVAENIAYGRPGATREEVeeaaraanahEFIMELPEGYDTVIGERG------VKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:cd03251 164 EATSALDTESERLVQAALERLMKNRTTF-VIAHRLSTIENADRIVVLEDGKIV 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-219 |
3.81e-30 |
|
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: 111.82 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 24 SVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATlsenalADLRRKQMGFVFQQPTLLKNLNVLDNI 103
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA------APPADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 104 VL---PAQKGNEKQadnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEI 180
Cdd:cd03298 92 GLglsPGLKLTAED----RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2519204862 181 MTLLSEIN-QQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:cd03298 168 LDLVLDLHaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-247 |
4.22e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRKQMGFV 87
Cdd:COG1129 8 RGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS---PRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVL---PAQKG--NEKQadnLMKKGQTLMEKMGIagleqrDI---TQVSG---GQLQRAGICRAL 156
Cdd:COG1129 85 HQELNLVPNLSVAENIFLgrePRRGGliDWRA---MRRRARELLARLGL------DIdpdTPVGDlsvAQQQLVEIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 157 MGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSEmqfFPEDDLNLEEk 235
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRlDEVFEIADRVTVLRDGRLVGT---GPVAELTEDE- 231
|
250
....*....|....
gi 2519204862 236 mvqVTEKM--REIE 247
Cdd:COG1129 232 ---LVRLMvgRELE 242
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-221 |
6.23e-30 |
|
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: 111.55 E-value: 6.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVfQQPTLLKNL 97
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVV-PQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 98 NVLDNIVLPAQKGNEKQADNLMKKGQtLMEKmgIAGLEQRDITQV-------SGGQLQRAGICRALMGDPQIIFGDEPTG 170
Cdd:cd03253 90 TIGYNIRYGRPDATDEEVIEAAKAAQ-IHDK--IMRFPDGYDTIVgerglklSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 171 ALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGRTTI-VIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-219 |
7.47e-30 |
|
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: 111.71 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 13 SFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTL-------MFALSGMDeidegsVQFDGKELATLSenaLADLRRKqMG 85
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLlslitgdLPPTYGND------VRLFGERRGGED---VWELRKR-IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 86 FV--FQQPTLLKNLNVLDnIVLPA--------QKGNEKQADnlmkKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRA 155
Cdd:COG1119 82 LVspALQLRFPRDETVLD-VVLSGffdsiglyREPTDEQRE----RARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQG-TAICLVTHDAK-VAAQTQRVLFMSDGQIV 219
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEeIPPGITHVLLLKDGRVV 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-221 |
9.75e-30 |
|
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: 109.06 E-value: 9.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRKQMGFVF 88
Cdd:cd03216 5 GITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---PRDARRAGIAMVY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 qqptllknlnvldnivlpaqkgnekqadnlmkkgqtlmekmgiagleqrditQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03216 82 ----------------------------------------------------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQGTAICLVTHDAK-VAAQTQRVLFMSDGQIVSE 221
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVTVLRDGRVVGT 163
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-219 |
1.10e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 22 NVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRK-QMgfVFQQPtlLKNLN-- 98
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRmQM--VFQDP--YASLNpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 --VLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGiagLEQRDIT----QVSGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:COG4608 112 mtVGDIIAEPLRIHGLASKAERRERVAELLELVG---LRPEHADryphEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 173 N-SKSAQeIMTLLSEINQQ-GTAICLVTHDAKVaaqtqrVLFMSD-------GQIV 219
Cdd:COG4608 189 DvSIQAQ-VLNLLEDLQDElGLTYLFISHDLSV------VRHISDrvavmylGKIV 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-219 |
1.17e-29 |
|
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: 110.45 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAladlrrkqMGFVF 88
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR--------IGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQ-KGNEKQAdnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDE 167
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQlKGLKKEE--ARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 168 PTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-221 |
1.51e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 111.70 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRK-QMgfVFQQP------ 91
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDiQM--VFQDSisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 92 ---------TLLKNLNVLDNivlpaqkgNEKQAdnlmkKGQTLMEKMGIA-GLEQRDITQVSGGQLQRAGICRALMGDPQ 161
Cdd:PRK10419 105 rktvreiirEPLRHLLSLDK--------AERLA-----RASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAK-VAAQTQRVLFMSDGQIVSE 221
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRlVERFCQRVMVMDNGQIVET 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-219 |
1.87e-29 |
|
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: 113.27 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 22 NVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELatLSENALADL--RRKQMGFVFQQPTLLKNLNV 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLppHRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNI-----VLPAQKGNEKQADnlmkkgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:COG4148 95 RGNLlygrkRAPRAERRISFDE--------VVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2519204862 175 KSAQEIMTLLSEINQQ-GTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:COG4148 167 ARKAEILPYLERLRDElDIPILYVSHSlDEVARLADHVVLLEQGRVV 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-218 |
2.17e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.50 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVG-TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenalADL 79
Cdd:PRK09452 10 SLSPLVElRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----AEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RrkQMGFVFQQPTLLKNLNVLDNIV-------LPAQKGNEKQADNLmkkgqtlmeKM-GIAGLEQRDITQVSGGQLQRAG 151
Cdd:PRK09452 86 R--HVNTVFQSYALFPHMTVFENVAfglrmqkTPAAEITPRVMEAL---------RMvQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 152 ICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVA-AQTQRVLFMSDGQI 218
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-219 |
2.21e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.79 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGK-----ELATLSENALADLRRKQ 83
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLRTE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPT--LLKNLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGLEQRDI-TQVSGGQLQRAGICRALMGDP 160
Cdd:PRK11701 91 WGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLpTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 161 QIIFGDEPTGALN-SKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:PRK11701 171 RLVFMDEPTGGLDvSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVV 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-237 |
2.25e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.91 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADL--RRKQMGFVFQQPTLLKN 96
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAikLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 97 LNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGlEQRD-----ITQVSGGQLQRAGICRALMGDPQIIFGDEPTGA 171
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWK-EVYDrlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 172 LNSKSAQEIMTLLSEINQQgTAICLVTHDAKVAAQ-TQRVLFMSDGQIV---SEMQFFPEDDLNLEEKMV 237
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARvADYVAFLYNGELVewgSSNEIFTSPKNELTEKYV 252
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-219 |
2.29e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.90 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 14 FGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGM-DEID----EGSVQFDGKELATLSENaLADLRRKqMGFVF 88
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDGEDIYDPDVD-VVELRRR-VGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLL-----------------KNLNVLDNIVlpaqkgnE---KQA-------DNLMKKGQTLmekmgiagleqrditq 141
Cdd:COG1117 99 QKPNPFpksiydnvayglrlhgiKSKSELDEIV-------EeslRKAalwdevkDRLKKSALGL---------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 142 vSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTaICLVTHD----AKVAaqtQRVLFMSDGQ 217
Cdd:COG1117 156 -SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYT-IVIVTHNmqqaARVS---DYTAFFYLGE 230
|
..
gi 2519204862 218 IV 219
Cdd:COG1117 231 LV 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
4.50e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.55 E-value: 4.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELaTLSENALADLRRKqMGFVFQQP-TLLKNLN 98
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT-VGIVFQNPdDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVL-PAQKGNEKqaDNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSA 177
Cdd:PRK13639 96 VEEDVAFgPLNLGLSK--EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2519204862 178 QEIMTLLSEINQQGTAICLVTHDAK-VAAQTQRVLFMSDGQIVSE 221
Cdd:PRK13639 174 SQIMKLLYDLNKEGITIIISTHDVDlVPVYADKVYVMSDGKIIKE 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-213 |
5.85e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 113.92 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenalADLRRKQMGFVFQQPTLL 94
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 kNLNVLDNIVL--PAQKGNE-KQAdnLMKKGqtLMEKmgIAGLEQRDITQV-------SGGQLQRAGICRALMGDPQIIF 164
Cdd:TIGR02857 409 -AGTIAENIRLarPDASDAEiREA--LERAG--LDEF--VAALPQGLDTPIgeggaglSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFM 213
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQGRTVL-LVTHRLALAALADRIVVL 529
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
1.03e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 110.18 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQE-----KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQF-----DGKELATLSEN 74
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 75 ALADLR---------------RKQMGFVFQ-------QPTLLKnlnvlDNIVLPAQKGNEKQ-ADNLMKKgqtlmeKMGI 131
Cdd:PRK13651 83 VLEKLViqktrfkkikkikeiRRRVGVVFQfaeyqlfEQTIEK-----DIIFGPVSMGVSKEeAKKRAAK------YIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 132 AGLE----QRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDA-KVAAQ 206
Cdd:PRK13651 152 VGLDesylQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEW 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2519204862 207 TQRVLFMSDGQIVSEMQFFP--EDDLNLEE------KMVQVTEKMREIEI 248
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDilSDNKFLIEnnmeppKLLNFVNKLEKKGI 281
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-218 |
1.13e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.00 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGsvqfdgkELatLSENALADLRRKQMGFVF 88
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------EL--LAGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLpAQKGNEKQAdnlmkkGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:PRK11247 88 QDARLLPWKKVIDNVGL-GLKGQWRDA------ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVA-AQTQRVLFMSDGQI 218
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-221 |
1.39e-28 |
|
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: 106.63 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 17 EKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlRRKQMGFVFQQPTLLKN 96
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQRPYLFDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 97 lnvldnivlpaqkgnekqadnlmkkgqTLMEKMGiagleqrdiTQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKS 176
Cdd:cd03247 90 ---------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2519204862 177 AQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:cd03247 134 ERQLLSLIFEVLKDKTLI-WITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-219 |
1.95e-28 |
|
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: 112.47 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEiDEGSVQFDGKELATLSENALADLRRkQMGFVFQQP--TLLK 95
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQDPfgSLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 NLNVLDnIVL-------PAQKGNEKQAdnlmkKGQTLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDE 167
Cdd:COG4172 378 RMTVGQ-IIAeglrvhgPGLSAAERRA-----RVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 168 PTGALN-SKSAQeIMTLLSEINQQ-GTAICLVTHDAKV-AAQTQRVLFMSDGQIV 219
Cdd:COG4172 452 PTSALDvSVQAQ-ILDLLRDLQREhGLAYLFISHDLAVvRALAHRVMVMKDGKVV 505
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-219 |
2.00e-28 |
|
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: 107.96 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLkNLN 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVL--PAQKGNEKQADNLMKKGQTLMEKM--GIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:cd03252 92 IRDNIALadPGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2519204862 175 KSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:cd03252 172 ESEHAIMRNMHDICAGRTVI-IIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-221 |
4.20e-28 |
|
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: 107.58 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRK-QMgfVFQQPTL 93
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDvQL--VFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKN--LNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTG 170
Cdd:TIGR02769 100 AVNprMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 171 ALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-219 |
5.95e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.50 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnalADLRRkQMGFVFQQPTLLkNLNV 99
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDP---ADLRR-NIGYVPQDPRLF-YGTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNIVLPAQKGNEkqadnlmkkgQTLMEKMGIAGLEqrDITQ----------------VSGGQLQRAGICRALMGDPQII 163
Cdd:TIGR03375 556 RDNIALGAPYADD----------EEILRAAELAGVT--EFVRrhpdgldmqigergrsLSGGQRQAVALARALLRDPPIL 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:TIGR03375 624 LLDEPTSAMDNRSEERFKDRLKRWLAGKTLV-LVTHRTSLLDLVDRIIVMDNGRIV 678
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-219 |
6.55e-28 |
|
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: 106.20 E-value: 6.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 17 EKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDE---GSVQFDGKELAtlsenalADLRRKQMGFVFQQPTL 93
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK-------PDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNLNVLDNIVLPAQ-KGNEKQADNLMKK--GQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTG 170
Cdd:cd03234 93 LPGLTVRETLTYTAIlRLPRKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 171 ALNSKSAQEIMTLLSEINQQGTAICLVTHD--AKVAAQTQRVLFMSDGQIV 219
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEIV 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-201 |
9.18e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.95 E-value: 9.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLL 94
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNlNVLDNIVLPAQKGNE-----KQADNLMKKGqtLMEKMgiagLEQRdITQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:PRK10247 94 GD-TVYDNLIFPWQIRNQqpdpaIFLDDLERFA--LPDTI----LTKN-IAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|....*
gi 2519204862 170 GAL---NSKSAQEIMTLLSEinQQGTAICLVTHDA 201
Cdd:PRK10247 166 SALdesNKHNVNEIIHRYVR--EQNIAVLWVTHDK 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-221 |
1.24e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.88 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrRKQ 83
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA---RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNI--VLPAQKGNEKQAdnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQ 161
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNIlaVLELRKLSKKER---EERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVT-HDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIGV-LITdHNVRETLGiCDRAYIISEGKVLAE 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-224 |
1.39e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 110.32 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 22 NVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIdEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLKNlNVLD 101
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESW----RKHLSWVGQNPQLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 102 NIVLPAQKGNEKQADNLMKKGQTL----MEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSA 177
Cdd:PRK11174 442 NVLLGNPDASDEQLQQALENAWVSeflpLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2519204862 178 QEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIVSEMQF 224
Cdd:PRK11174 522 QLVMQALNAASRRQTTL-MVTHQLEDLAQWDQIWVMQDGQIVQQGDY 567
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-221 |
1.48e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID-----EGSVQFDGKELATLSenaLADL 79
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMD---VIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRK-QMgfVFQQPTLLKNLNVLDNIVLPAQkgnekqADNLMKKGQTLMEKMGIAgLEQRDI------------TQVSGGQ 146
Cdd:PRK14247 81 RRRvQM--VFQIPNPIPNLSIFENVALGLK------LNRLVKSKKELQERVRWA-LEKAQLwdevkdrldapaGKLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 147 LQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTaICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT-IVLVTHFPQQAARiSDYVAFLYKGQIVEW 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-221 |
1.49e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 107.89 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 23 VSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQQPTLLKNLNVLDN 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 103 IVLPAQKGNEKQADNLMKKgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMT 182
Cdd:TIGR02142 96 LRYGMKRARPSERRISFER---VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2519204862 183 LLSEINQQ-GTAICLVTHD-AKVAAQTQRVLFMSDGQIVSE 221
Cdd:TIGR02142 173 YLERLHAEfGIPILYVSHSlQEVLRLADRVVVLEDGRVAAA 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-245 |
1.70e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 106.25 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelaTLSENALADLRRKqMGFVFQQP-TLLKNLN 98
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ-VGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLpaqkGNEKQA---DNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSK 175
Cdd:PRK13635 99 VQDDVAF----GLENIGvprEEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 176 SAQEIMTLLSEINQQGTAICL-VTHDAKVAAQTQRVLFMSDGQIVSEMQffPEDDLNLEEKMVQV------TEKMRE 245
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGT--PEEIFKSGHMLQEIgldvpfSVKLKE 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-244 |
1.89e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.36 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrRKQM 84
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA---RRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 85 GFVFQQPTLLKNLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAK-VAAQTQRVLFMSDGQIVSEMQffPEDDLNLEE-KMVQVTEK 242
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVReTLAVCERAYIVSQGHLIAHGT--PTEILQDEHvKRVYLGED 238
|
..
gi 2519204862 243 MR 244
Cdd:PRK10895 239 FR 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-219 |
6.89e-27 |
|
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: 103.04 E-value: 6.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVsIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAladlrRKQMGFV 87
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-----RRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNI-VLPAQKG-NEKQADnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:cd03264 78 PQEFGVYPNFTVREFLdYIAWLKGiPSKEVK---ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 166 DEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAK-VAAQTQRVLFMSDGQIV 219
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDRIVI-LSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-221 |
6.93e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 104.28 E-value: 6.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEN----ALAD----- 78
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlKVADknqlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 79 LRRKQMGFVFQQPTLLKNLNVLDNIV-LPAQKGNEKQADnLMKKGQTLMEKMGIAGLEQRDI-TQVSGGQLQRAGICRAL 156
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQE-ARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 157 MGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-221 |
8.35e-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: 103.22 E-value: 8.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEK----ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGkeLATLSENALAdl 79
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 rRKQMGFVFQQPTLLKNLNVLDNIV----LPAQKGnekqaDNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRA 155
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEyfagLYGLKG-----DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSE 221
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
26-217 |
8.68e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.58 E-value: 8.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 26 EIEAGEFVSIMGPSGSGKTTLMFALSGM---DEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQQPtlLKNLN---- 98
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQDP--MTSLNpymr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNI--VLPAQKGnekqadnlMKKGQTLME--------KMGIAgleQRDIT----QVSGGQLQRAGICRALMGDPQIIF 164
Cdd:PRK09473 116 VGEQLmeVLMLHKG--------MSKAEAFEEsvrmldavKMPEA---RKRMKmyphEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHD-AKVAAQTQRVLFMSDGQ 217
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDlGVVAGICDKVLVMYAGR 239
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-219 |
1.61e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.22 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLL 94
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL----RQAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 kNLNVLDNIVLPAQKGNEKQ-ADNLMKKG-QTLMEkmGIAGLEQ------RditQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:PRK11160 427 -SATLRDNLLLAAPNASDEAlIEVLQQVGlEKLLE--DDKGLNAwlgeggR---QLSGGEQRRLGIARALLHDAPLLLLD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:PRK11160 501 EPTEGLDAETERQILELLAEHAQNKTVL-MITHRLTGLEQFDRICVMDNGQII 552
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-219 |
2.47e-26 |
|
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: 102.23 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLkNL 97
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLF-DG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 98 NVLDNIVLPAQKGNEKQAD-------------NLMKKGQTLMEKMGiagleqrdiTQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:cd03249 92 TIAENIRYGKPDATDEEVEeaakkanihdfimSLPDGYDTLVGERG---------SQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKGRTTI-VIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-221 |
2.64e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKqMGFVFQQPTLL 94
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:PRK11831 97 TDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2519204862 175 KSAQEIMTLLSEINQQ-GTAICLVTHDA-KVAAQTQRVLFMSDGQIVSE 221
Cdd:PRK11831 177 ITMGVLVKLISELNSAlGVTCVVVSHDVpEVLSIADHAYIVADKKIVAH 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
9-221 |
2.66e-26 |
|
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: 101.83 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrRKQMGFVF 88
Cdd:TIGR03410 5 NLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA---RAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNI--VLPAQKGNEKQA------------DNLMKKGQTLmekmgiagleqrditqvSGGQLQRAGICR 154
Cdd:TIGR03410 82 QGREIFPRLTVEENLltGLAALPRRSRKIpdeiyelfpvlkEMLGRRGGDL-----------------SGGQQQQLAIAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 155 ALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGT-AICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARElADRYYVMERGRVVAS 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-204 |
2.93e-26 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 100.96 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELAtLSENALADlRRKQMGFVFQQP-TL 93
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLLE-RRQRVGLVFQDPdDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNLNVLDNIVL-PAQKGNEKqaDNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:TIGR01166 81 LFAADVDQDVAFgPLNLGLSE--AEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 2519204862 173 NSKSAQEIMTLLSEINQQGTAICLVTHDAKVA 204
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-221 |
4.64e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.01 E-value: 4.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQ 83
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLPAQK-----GNEKQADNlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMG 158
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYGRSPwlslwGRLSAEDN--ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 159 DPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQ 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-211 |
5.69e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.00 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSV-QFDGKELATLSE-NALAD---LRRKQ---MGFvFQQP 91
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrRAGGARVAYVPQrSEVPDslpLTVRDlvaMGR-WARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 92 TLLKNLNVLDNIVLpaqkgnekqadnlmkkgQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGA 171
Cdd:NF040873 87 GLWRRLTRDDRAAV-----------------DDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2519204862 172 LNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVL 211
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-219 |
6.19e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 24 SVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlrRKQMGFVFQQPTLLKNLNVLDNI 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 104 VL---PAQKGNEKQADNLmkkgQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEI 180
Cdd:PRK10771 93 GLglnPGLKLNAAQREKL----HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2519204862 181 MTLLSEI-NQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:PRK10771 169 LTLVSQVcQERQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-222 |
6.73e-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: 100.37 E-value: 6.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlrRKQMGFVF 88
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------LRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAqkgneKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03268 79 EAPGFYPNLTARENLRLLA-----RLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQGTAICLVTHD----AKVAaqtQRVLFMSDGQIVSEM 222
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLlseiQKVA---DRIGIINKGKLIEEG 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-217 |
2.09e-25 |
|
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: 99.43 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSF-----GQEKI--LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSV----QFDGKELA 69
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 70 TLSENALADLRRKQMGFVFQ-------QPTLlknlnvldNIV---LPAQKGNEKQADnlmKKGQTLMEKMGIaglEQR-- 137
Cdd:COG4778 81 QASPREILALRRRTIGYVSQflrviprVSAL--------DVVaepLLERGVDREEAR---ARARELLARLNL---PERlw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 138 DI--TQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMS 214
Cdd:COG4778 147 DLppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVT 226
|
...
gi 2519204862 215 DGQ 217
Cdd:COG4778 227 PFS 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-234 |
2.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.45 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 2 KKMIVGTNIEKSFGQEK--ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELAtlSENaLADL 79
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--KEN-LKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRKqMGFVFQQPtllKNLNV-----------LDNIVLPAQKGNEKQADnlmkkgqtLMEKMGIAGLEQRDITQVSGGQLQ 148
Cdd:PRK13632 82 RKK-IGIIFQNP---DNQFIgatveddiafgLENKKVPPKKMKDIIDD--------LAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 149 RAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGT-AICLVTHDAKVAAQTQRVLFMSDGQIVSemQFFPE 227
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLIA--QGKPK 227
|
....*..
gi 2519204862 228 DDLNLEE 234
Cdd:PRK13632 228 EILNNKE 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-218 |
2.79e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 98.78 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 24 SVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlrRKQMGFVFQQPTLLKNLNVLDNI 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY------QRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 104 VL---PAQKGNEKQADNLMKKGQtlmeKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEI 180
Cdd:TIGR01277 92 GLglhPGLKLNAEQQEKVVDAAQ----QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2519204862 181 MTLLSEI-NQQGTAICLVTHD-AKVAAQTQRVLFMSDGQI 218
Cdd:TIGR01277 168 LALVKQLcSERQRTLLMVTHHlSDARAIASQIAVVSQGKI 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-219 |
5.18e-25 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 100.65 E-value: 5.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 35 IMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlrRKQMGFVFQQPTLLKNLNVLDNIVLPAQKGNEKQ 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 115 ADnlmkKGQTLMEKMGIAGLE---QRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ- 190
Cdd:TIGR01187 75 AE----IKPRVLEALRLVQLEefaDRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQl 150
|
170 180 190
....*....|....*....|....*....|
gi 2519204862 191 GTAICLVTHDAKVA-AQTQRVLFMSDGQIV 219
Cdd:TIGR01187 151 GITFVFVTHDQEEAmTMSDRIAIMRKGKIA 180
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-221 |
6.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.85 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQQP-TLL 94
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPeSQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIVLpAQKGNEKQADNLMKKGQTLMEKMGIAgleqRDIT-----QVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:PRK13646 99 FEDTVEREIIF-GPKNFKMNLDEVKNYAHRLLMDLGFS----RDVMsqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 170 GALNSKSAQEIMTLLSEIN-QQGTAICLVTHDA-KVAAQTQRVLFMSDGQIVSE 221
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQ 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-221 |
1.22e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPT-LLKN 96
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV----RSKVGLVFQDPDdQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 97 LNVLDNIVL-PAQKGNEKqaDNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSK 175
Cdd:PRK13647 95 STVWDDVAFgPVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2519204862 176 SAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAE 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-230 |
1.36e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.79 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaladLRRKQMGFVF 88
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS------IQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIV--LPAQKGNEKQADNLMKKGQTLMEkmgIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:PRK11432 85 QSYALFPHMSLGENVGygLKMLGVPKEERKQRVKEALELVD---LAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQGTAICL-VTHDAKVA-AQTQRVLFMSDGQIvseMQFFPEDDL 230
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLyVTHDQSEAfAVSDTVIVMNKGKI---MQIGSPQEL 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-219 |
1.44e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.40 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADlRRKQMGFVFQQPtlLKNL 97
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA-VRSDIQMIFQDP--LASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 98 N----VLDNIVLPAQKGNEK-QADNLMKKGQTLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGA 171
Cdd:PRK15079 112 NprmtIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 172 LN-SKSAQeIMTLLSEINQQ-GTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:PRK15079 192 LDvSIQAQ-VVNLLQQLQREmGLSLIFIAHDlAVVKHISDRVLVMYLGHAV 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-239 |
1.69e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.28 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQQP-TLLKNLN 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPeSQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQKG--NEKQADNLMKkgqtlmEKMGIAGLEQ----RDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:PRK13649 103 VLKDVAFGPQNFgvSQEEAEALAR------EKLALVGISEslfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 173 NSKSAQEIMTLLSEINQQGTAICLVTHDA-KVAAQTQRVLFMSDGQIV---SEMQFFPEDDLnLEEKMVQV 239
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVlsgKPKDIFQDVDF-LEEKQLGV 246
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-219 |
2.21e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.45 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMD--EIDEGSVQFDGKELATLSenalADLR-RKQMGFVFQQPTLL 94
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELS----PDERaRAGIFLAFQYPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLD--NIVLPAQKGNEKQADNLMKKGQTLMEKMGI-AGLEQRDITQ-VSGGQLQRAGICRALMGDPQIIFGDEP-T 169
Cdd:COG0396 90 PGVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETdS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 170 G----ALNsKSAQEIMTLLSEinqqGTAICLVTH-----DAKVAaqtQRVLFMSDGQIV 219
Cdd:COG0396 170 GldidALR-IVAEGVNKLRSP----DRGILIITHyqrilDYIKP---DFVHVLVDGRIV 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-219 |
2.67e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.89 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID---EGSVQFDGKELAtlsenalADLRRKQMGFVFQQP 91
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID-------AKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 92 TLLKNLNVLDNIVLPA--QKGNEKQADNLMKKGQTLMEKMG-------IAGLEQRdITQVSGGQLQRAGICRALMGDPQI 162
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAhlRMPRRVTKKEKRERVDEVLQALGlrkcantRIGVPGR-VKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD--AKVAAQTQRVLFMSDGQIV 219
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRVA 246
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-221 |
2.90e-24 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 96.28 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGkeLATLSEnalADLRRKQM 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVRE---PREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 85 GFVFQQPTLLKNLNVLDNIVLPAQKGNEKQADnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAE-RRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAE 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-230 |
2.93e-24 |
|
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: 100.67 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID--EGSVQFDGKELATLSenaLADLRRKQMGF 86
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASN---IRDTERAGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 VFQQPTLLKNLNVLDNIVLpaqkGNE------KQADNLM-KKGQTLMEKMGIAGL-EQRDITQVSGGQLQRAGICRALMG 158
Cdd:TIGR02633 83 IHQELTLVPELSVAENIFL----GNEitlpggRMAYNAMyLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 159 DPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVS--EMQFFPEDDL 230
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQHVAtkDMSTMSEDDI 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-219 |
3.09e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.87 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELatlsenALADLRRkq 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL------DPEDRRR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLPAQ-KGNEKQAdnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARlKGLSKAE--AKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVEELCDRIVIINKGRKV 208
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-218 |
4.24e-24 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 100.11 E-value: 4.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQMGFVFQQPTLL 94
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNlNVLDNIvlpAQKGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQV-------SGGQLQRAGICRALMGDPQIIFGDE 167
Cdd:TIGR01842 405 PG-TVAENI---ARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIgpggatlSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 168 PTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-199 |
4.46e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnalADLRRKQMGFVF 88
Cdd:COG3845 10 GITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP---RDAIALGIGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVL-----PAQKGNEKQADnlmKKGQTLMEKMgiaGLE---QRDITQVSGGQLQRAGICRALMGDP 160
Cdd:COG3845 87 QHFMLVPNLTVAENIVLgleptKGGRLDRKAAR---ARIRELSERY---GLDvdpDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2519204862 161 QI-IFgDEPTGALnskSAQEIMTLLSEINQ---QGTAICLVTH 199
Cdd:COG3845 161 RIlIL-DEPTAVL---TPQEADELFEILRRlaaEGKSIIFITH 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-200 |
4.61e-24 |
|
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: 100.13 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQP--- 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV----RRRVSVCAQDAhlf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 92 --TLLKNL-----NVLDNIVLPA--QKGNEKQADNLMKKGQTLMEKMGIAgleqrditqVSGGQLQRAGICRALMGDPQI 162
Cdd:TIGR02868 422 dtTVRENLrlarpDATDEELWAAleRVGLADWLRALPDGLDTVLGEGGAR---------LSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINqQGTAICLVTHD 200
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-218 |
6.16e-24 |
|
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: 94.42 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLR-------RKQMGfvfqqpt 92
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGiayvpedRKREG------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 LLKNLNVLDNIVLPAqkgnekqadnlmkkgqtlmekmgiagleqrditQVSGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:cd03215 89 LVLDLSVAENIALSS---------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2519204862 173 NSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQI 218
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-219 |
7.13e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 99.82 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEK-ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQMGFVFQQPTL 93
Cdd:COG4618 342 GSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG----RHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LkNLNVLDNI-----------VLPAQKgnekqADnlmkkgqtlMEKMgIAGLEQRDITQV-------SGGQLQRAGICRA 155
Cdd:COG4618 418 F-DGTIAENIarfgdadpekvVAAAKL-----AG---------VHEM-ILRLPDGYDTRIgeggarlSGGQRQRIGLARA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-219 |
7.15e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 95.86 E-value: 7.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrrKQMGFVF-QQPTLLKNLN 98
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-----RRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQKGN--EKQADNLMKKgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKS 176
Cdd:cd03267 112 VIDSFYLLAAIYDlpPARFKKRLDE---LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2519204862 177 AQEIMTLLSEINQQ-GTAICLVTHDAK-VAAQTQRVLFMSDGQIV 219
Cdd:cd03267 189 QENIRNFLKEYNRErGTTVLLTSHYMKdIEALARRVLVIDKGRLL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-221 |
1.15e-23 |
|
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: 94.98 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEK-ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFV 87
Cdd:cd03254 7 NVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLkNLNVLDNI-----------VLPAQKgnEKQADNL-MKKGQTLMEKMGIAGleqrdiTQVSGGQLQRAGICRA 155
Cdd:cd03254 83 LQDTFLF-SGTIMENIrlgrpnatdeeVIEAAK--EAGAHDFiMKLPNGYDTVLGENG------GNLSQGERQLLAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSI-IIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-216 |
1.28e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.44 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 22 NVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrkQMGFV--FQQPTLLKNLNV 99
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-----RMGVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNIVL-----------------PAQKGNEKQAdnlMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:PRK11300 98 IENLLVaqhqqlktglfsgllktPAFRRAESEA---LDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEI-NQQGTAICLVTHDAK-VAAQTQRVLFMSDG 216
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKlVMGISDRIYVVNQG 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
14-219 |
2.06e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 14 FGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID-----EGSVQFDGKELATLSENALaDLRrKQMGFVF 88
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTV-DLR-KEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKnLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGlEQRDITQ-----VSGGQLQRAGICRALMGDPQII 163
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWD-EVKDRLHdsalgLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEINQQGTaICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRiSDRTGFFLDGDLI 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-216 |
2.64e-23 |
|
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: 94.07 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrkqmgfVFQQPTLLKNLNV 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNI------VLPAQKGNEKQadnlmkkgQTLMEKMGIAGLEQ---RDITQVSGGQLQRAGICRALMGDPQIIFGDEPTG 170
Cdd:TIGR01184 72 RENIalavdrVLPDLSKSERR--------AIVEEHIALVGLTEaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2519204862 171 ALNSKSAQEIMTLLSEINQQGTAICL-VTHDAKVAA-QTQRVLFMSDG 216
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLmVTHDVDEALlLSDRVVMLTNG 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-236 |
3.08e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKE-------------LATLSENaladlrRKQMGf 86
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvrirsprdairagIAYVPED------RKGEG- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 vfqqptLLKNLNVLDNIVLPAQKG-------NEKQADNLMKKgqtLMEKMGI--AGLEQRdITQVSGGQLQRAGICRALM 157
Cdd:COG1129 341 ------LVLDLSIRENITLASLDRlsrggllDRRRERALAEE---YIKRLRIktPSPEQP-VGNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 158 GDPQIIFGDEPT-----GAlnsKsaQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSEmqfFPEDDLN 231
Cdd:COG1129 411 TDPKVLILDEPTrgidvGA---K--AEIYRLIRELAAEGKAVIVISSElPELLGLSDRILVMREGRIVGE---LDREEAT 482
|
....*
gi 2519204862 232 LEEKM 236
Cdd:COG1129 483 EEAIM 487
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-207 |
5.10e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.87 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELatlseNALADLRRkQMGFVF 88
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-----NDVPPAER-GVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQKGNEKQADnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEE-INQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDaKVAAQT 207
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRlGRTMIYVTHD-QVEAMT 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-221 |
5.65e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 94.28 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 7 GTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQMGF 86
Cdd:PRK10253 10 GEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 VFQQPTLLKNLNVLDNIV---LPAQ----KGNEKQADNLMKKgqtlMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGD 159
Cdd:PRK10253 86 LAQNATTPGDITVQELVArgrYPHQplftRWRKEDEEAVTKA----MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEIN-QQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRyASHLIALREGKIVAQ 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-209 |
1.00e-22 |
|
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: 91.65 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATlsenaLADLRRKQMGFVFQQPTLL 94
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-----QRDEPHENILYLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIVLPAQKGNEKQADNLmkkgqTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:TIGR01189 86 PELSALENLHFWAAIHGGAQRTIE-----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2519204862 175 KSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQR 209
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQDLGLVEARE 195
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-203 |
1.21e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.26 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRK-QMgfVFQQPtl 93
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKiQI--VFQNP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNLN------------VLDNIVLPAQKGNEKQADnlmkkgqtLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:PRK11308 102 YGSLNprkkvgqileepLLINTSLSAAERREKALA--------MMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2519204862 161 QIIFGDEPTGALN-SKSAQeIMTLLSEINQQ-GTAICLVTHDAKV 203
Cdd:PRK11308 174 DVVVADEPVSALDvSVQAQ-VLNLMMDLQQElGLSYVFISHDLSV 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-248 |
1.28e-22 |
|
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: 96.02 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEI--DEGSV----------------QFDGK---- 66
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpSKVGEpcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 67 ----------ELATLSENALADLRRKqMGFVFQQP-TLLKNLNVLDNiVLPAQKGNEKQADNLMKKGQTLMEKMGiagLE 135
Cdd:TIGR03269 85 cggtlepeevDFWNLSDKLRRRIRKR-IAIMLQRTfALYGDDTVLDN-VLEALEEIGYEGKEAVGRAVDLIEMVQ---LS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 136 QRdITQV----SGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSE-INQQGTAICLVTHDAKVAAQ-TQR 209
Cdd:TIGR03269 160 HR-ITHIardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDlSDK 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 2519204862 210 VLFMSDGQIVSEMQffPEDDLNLEEKMVQVTEKMREIEI 248
Cdd:TIGR03269 239 AIWLENGEIKEEGT--PDEVVAVFMEGVSEVEKECEVEV 275
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-219 |
1.85e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.97 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKEL-ATLSENALADLRRKqMGFVFQQP--T 92
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKK-VSLVFQFPeaQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 LLKNlNVLDNIVL-PAQKG-NEKQADNLMKKgqtLMEKMGIA-GLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:PRK13641 98 LFEN-TVLKDVEFgPKNFGfSEDEAKEKALK---WLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 170 GALNSKSAQEIMTLLSEINQQGTAICLVTHDA-KVAAQTQRVLFMSDGQIV 219
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-246 |
2.18e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 7 GTNIEKsfgqeKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaLADLrRKQMGF 86
Cdd:PRK13637 15 GTPFEK-----KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI-RKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 VFQQP-------TLLKnlnvlDNIVLPAQKG-NEKQADNLMKkgqtlmEKMGIAGLEQRDIT-----QVSGGQLQRAGIC 153
Cdd:PRK13637 88 VFQYPeyqlfeeTIEK-----DIAFGPINLGlSEEEIENRVK------RAMNIVGLDYEDYKdkspfELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 154 RALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAK-VAAQTQRVLFMSDGQIV---SEMQFFPED 228
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEdVAKLADRIIVMNKGKCElqgTPREVFKEV 236
|
250 260
....*....|....*....|.
gi 2519204862 229 DLnLEE---KMVQVTEKMREI 246
Cdd:PRK13637 237 ET-LESiglAVPQVTYLVRKL 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-219 |
2.69e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.31 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 22 NVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRkQMGFVFQQP--TLLKNLNV 99
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDPyaSLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGLEQ-RDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQ 178
Cdd:PRK10261 421 GDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2519204862 179 EIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:PRK10261 501 QIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIV 543
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-218 |
3.09e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQ 83
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVlDNIVLPAQKGNEKQADNLMKKGQTL----MEKMGIAGLEQRDITQVSGGQLQRAGICRALMGD 159
Cdd:PRK09536 79 VASVPQDTSLSFEFDV-RQVVEMGRTPHRSRFDTWTETDRAAveraMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQI 218
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRV 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-239 |
5.51e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.69 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELAtlSENaLADLRRKqMGFVFQQP-TLLKNLN 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AEN-VWNLRRK-IGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLpaqkGNEKQA---DNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSK 175
Cdd:PRK13642 99 VEDDVAF----GMENQGiprEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 176 SAQEIMTLLSEINQQGTAICL-VTHDAKVAAQTQRVLFMSDGQIVSEMQffPEDDLNLEEKMVQV 239
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLsITHDLDEAASSDRILVMKAGEIIKEAA--PSELFATSEDMVEI 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-219 |
6.22e-22 |
|
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: 94.12 E-value: 6.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 13 SFGQE---KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVfQ 89
Cdd:COG5265 364 SFGYDperPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIV-P 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 90 QPTLLKNLNVLDNI-----------VLPAQKGneKQADNLmkkgqtlmekmgIAGLEQRDITQV-------SGGQLQRAG 151
Cdd:COG5265 439 QDTVLFNDTIAYNIaygrpdaseeeVEAAARA--AQIHDF------------IESLPDGYDTRVgerglklSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 152 ICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTH------DAkvaaqtQRVLFMSDGQIV 219
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTL-VIAHrlstivDA------DEILVLEAGRIV 571
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-221 |
7.58e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 90.30 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 25 VEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKElatlsenalADLRRKQMGFVFQQPTLLKNLNV-LDNI 103
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---------PGKGWRHIGYVPQRHEFAWDFPIsVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 104 VLPAQKG------NEKQADNLMKKGQtlMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSA 177
Cdd:TIGR03771 72 VMSGRTGhigwlrRPCVADFAAVRDA--LRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2519204862 178 QEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:TIGR03771 150 ELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIAD 193
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-219 |
1.04e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.29 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID-----EGSVQFDGKELATLSENA 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 76 LAdlRRKQMGFVFQQPTLLKNLNVLDNIVLPAQ-KGNEKQADNLMKKGQTLMEKMGIAGlEQRD-----ITQVSGGQLQR 149
Cdd:PRK14267 81 IE--VRREVGMVFQYPNPFPHLTIYDNVAIGVKlNGLVKSKKELDERVEWALKKAALWD-EVKDrlndyPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 150 AGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTaICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT-IVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-219 |
1.25e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.40 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 10 IEKSFGQEKIL---------RNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLR 80
Cdd:PRK10070 25 IEQGLSKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 RKQMGFVFQQPTLLKNLNVLDNIV-------LPAQKGNEKQADNLmkkgqtlmEKMGIAGLEQRDITQVSGGQLQRAGIC 153
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAfgmelagINAEERREKALDAL--------RQVGLENYAHSYPDELSGGMRQRVGLA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 154 RALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEIN-QQGTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:PRK10070 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVV 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
1.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.18 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEK---ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKElatLSENALA 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 78 DLRRKqMGFVFQQP-TLLKNLNVLDNIVLpaqkGNEKQA---DNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGIC 153
Cdd:PRK13650 78 DIRHK-IGMVFQNPdNQFVGATVEDDVAF----GLENKGiphEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 154 RALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQTQRVLFMSDGQIVS 220
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-230 |
1.82e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.68 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID--EGSVQFDGKELATLSenaLADLRRKQMGF 86
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASN---IRDTERAGIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 VFQQPTLLKNLNVLDNIVLpaqkGNEKQA------DNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:PRK13549 87 IHQELALVKELSVLENIFL----GNEITPggimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDA-KVAAQTQRVLFMSDGQIVSE--MQFFPEDDL 230
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLnEVKAISDTICVIRDGRHIGTrpAAGMTEDDI 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-169 |
1.98e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGkelatlsenalaDLRrkqMGFV 87
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLR---IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNI--VLPAQKGNEKQADNLMKKG-----------------------------QTLMEKMGIAGLE- 135
Cdd:COG0488 67 PQEPPLDDDLTVLDTVldGDAELRALEAELEELEAKLaepdedlerlaelqeefealggweaearaEEILSGLGFPEEDl 146
|
170 180 190
....*....|....*....|....*....|....
gi 2519204862 136 QRDITQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
14-221 |
3.38e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.19 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 14 FGQEKI----LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMdeID------EGSVQFDGKELATLSENALADLRRKQ 83
Cdd:PRK11022 13 FGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL--IDypgrvmAEKLEFNGQDLQRISEKERRNLVGAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQP-TLLKNLNVLDNIVLPA----QKGNEKQadnLMKKGQTLMEKMGIAGLEQR-DIT--QVSGGQLQRAGICRA 155
Cdd:PRK11022 91 VAMIFQDPmTSLNPCYTVGFQIMEAikvhQGGNKKT---RRQRAIDLLNQVGIPDPASRlDVYphQLSGGMSQRVMIAMA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHD-AKVAAQTQRVLFMSDGQIVSE 221
Cdd:PRK11022 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDlALVAEAAHKIIVMYAGQVVET 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-220 |
3.89e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSV---------EIEAGEFVSIMGPSGSGKTTLMFALSGMDEiDEGSVQFDGKELATLSENALADLRrkqmGFVFQQ 90
Cdd:PRK03695 3 LNDVAVstrlgplsaEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHR----AYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 91 PTLLKNLNVLDNIVL--PAQKGNEKQADNLMKkgqtLMEKMGIAGLEQRDITQVSGGQLQR---AGIC----RALMGDPQ 161
Cdd:PRK03695 78 QTPPFAMPVFQYLTLhqPDKTRTEAVASALNE----VAEALGLDDKLGRSVNQLSGGEWQRvrlAAVVlqvwPDINPAGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 162 IIFGDEPTGALNskSAQEIM--TLLSEINQQGTAICLVTHDA-KVAAQTQRVLFMSDGQIVS 220
Cdd:PRK03695 154 LLLLDEPMNSLD--VAQQAAldRLLSELCQQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLA 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-221 |
5.65e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSF-----GQEKI-LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGkeLATLSEN 74
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneeSTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 75 ALADLRRKQmGFVFQQPtllknlnvlDNIVLPA------QKGNEK---QADNLMKKGQTLMEKMGIAGLEQRDITQVSGG 145
Cdd:PRK13633 79 NLWDIRNKA-GMVFQNP---------DNQIVATiveedvAFGPENlgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 146 QLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-219 |
5.87e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEiDEGSVQFDGKELATLSENALADLRRkQMGFVFQQP--T 92
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPnsS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 LLKNLNVLdNIVLPAQKGNEKQADNLMKKGQTL--MEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:PRK15134 375 LNPRLNVL-QIIEEGLRVHQPTLSAAQREQQVIavMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 170 GALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVA-AQTQRVLFMSDGQIV 219
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVrALCHQVIVLRQGEVV 505
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-220 |
6.49e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQQP-TLLKN 96
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPeSQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 97 LNVLDNIVL-PAQKGNEKQadnlmKKGQTLMEKMGIAGLE----QRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGA 171
Cdd:PRK13643 100 ETVLKDVAFgPQNFGIPKE-----KAEKIAAEKLEMVGLAdefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2519204862 172 LNSKSAQEIMTLLSEINQQGTAICLVTHDA-KVAAQTQRVLFMSDGQIVS 220
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIIS 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-219 |
7.68e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 7.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTtlMFALSGMD-------EIDEGSVQFDGKELATLSENALADLRRKQMGFVF 88
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSILRllpsppvVYPSGDIRFHGESLLHASEQTLRGVRGNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLlkNLNVLDNI------VLPAQKGNEKQAdnlmKKGQTL--MEKMGIAGLEQR--DIT-QVSGGQLQRAGICRALM 157
Cdd:PRK15134 99 QEPMV--SLNPLHTLekqlyeVLSLHRGMRREA----ARGEILncLDRVGIRQAAKRltDYPhQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
1.14e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELaTLSENALADLRrKQMGFVFQQP-TLLKNLN 98
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR-ESVGMVFQDPdNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQKGNEKQaDNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQ 178
Cdd:PRK13636 100 VYQDVSFGAVNLKLPE-DEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2519204862 179 EIMTLLSEINQQ-GTAICLVTHDAK-VAAQTQRVLFMSDGQIVSE 221
Cdd:PRK13636 179 EIMKLLVEMQKElGLTIIIATHDIDiVPLYCDNVFVMKEGRVILQ 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-221 |
1.75e-20 |
|
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: 86.04 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMD--EIDEGSVQFDGKELATLSENALAdlrRKQMGFVFQQP---T 92
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQYPpeiP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 LLKNLNVLDNIvlpaqkgNEkqadnlmkkgqtlmekmgiaGLeqrditqvSGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:cd03217 91 GVKNADFLRYV-------NE--------------------GF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 173 NSKSAQEIMTLLSEINQQGTAICLVTHDAKVAA--QTQRVLFMSDGQIVSE 221
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKS 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-230 |
2.01e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENaladlR 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-----K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 RKQMG--FVFQQPTLLKNLNVLDNIV--LPAQKGNEKQADNLMKK-GQTLMEKMGIAGLEQRDitqvsggqLQRAGICRA 155
Cdd:PRK15439 83 AHQLGiyLVPQEPLLFPNLSVKENILfgLPKRQASMQKMKQLLAAlGCQLDLDSSAGSLEVAD--------RQIVEILRG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIV--SEMQFFPEDDL 230
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTIAlsGKTADLSTDDI 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-199 |
2.30e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELA-TLSENALAdlrrKQMGFV 87
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALA----AGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVL---PAQKG--NEKQadnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQI 162
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLgqlPHKGGivNRRL---LNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTH 199
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-218 |
2.88e-20 |
|
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: 85.99 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLKNlN 98
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNI------------VLPAQKGNEKqaDNLMKKGQTLMEKMGIAGleqrdiTQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:cd03248 104 LQDNIayglqscsfecvKEAAQKAHAH--SFISELASGYDTEVGEKG------SQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQGTaICLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRT-VLVIAHRLSTVERADQILVLDGGRI 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-219 |
4.01e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.97 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnaladlRRKQMGFVF 88
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------YQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLpAQKGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:PRK11607 98 QSYALFPHMTVEQNIAF-GLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQGTAIC-LVTHDAKVA-AQTQRVLFMSDGQIV 219
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCvMVTHDQEEAmTMAGRIAIMNRGKFV 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-219 |
6.63e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLr 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 rkQMGFVFQQPTLLKNLNVLDNIV---LPAQKG---NEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICR 154
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYigrHLTKKVcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 155 ALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSSV 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-220 |
6.76e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 84.39 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 17 EKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRKqMGFVFQQPTLL-- 94
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSS-LTIIPQDPTLFsg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 ---KNLNVLDnivlpaqkgneKQADnlmkkgQTLMEKMGIA--GLeqrditQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:cd03369 97 tirSNLDPFD-----------EYSD------EEIYGALRVSegGL------NLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 170 GALNSKSAQEIMTLLSEiNQQGTAICLVTHDAKVAAQTQRVLFMSDGQIVS 220
Cdd:cd03369 154 ASIDYATDALIQKTIRE-EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-213 |
8.63e-20 |
|
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: 84.08 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenalaDLRRKQMGFVFQQPTLL 94
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-----DSIARGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIVLPAQKGNEKQAdnlmkkgQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:cd03231 86 TTLSVLENLRFWHADHSDEQV-------EEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2519204862 175 KSAQEIMTLLSEINQQGTAICLVTH-DAKVAAQTQRVLFM 213
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAGARELDL 198
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
9-207 |
9.38e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.22 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEI-----DEGSVQFDGKELATlSENALADLRRKq 83
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYA-PDVDPVEVRRR- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNlNVLDNIVLPAQ-KGNEKQADNLMKKG-------QTLMEKMGIAGLeqrditQVSGGQLQRAGICRA 155
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYGARiNGYKGDMDELVERSlrqaalwDEVKDKLKQSGL------SLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTaICLVTHDAKVAAQT 207
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQAARV 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-219 |
1.01e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDG----KElatlsENALAdlrrKQMGFVFQQPT-LL 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKR-----RKEFA----RRIGVVFGQRSqLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIVLPAQ--KGNEKQADNLMKKgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:COG4586 109 WDLPAIDSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2519204862 173 NSKSAQEIMTLLSEINQQ-GTAICLVTHD-AKVAAQTQRVLFMSDGQIV 219
Cdd:COG4586 186 DVVSKEAIREFLKEYNRErGTTILLTSHDmDDIEALCDRVIVIDHGRII 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-217 |
1.74e-19 |
|
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: 83.29 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 11 EKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelatlsenaladlrrkqMGFVFQQ 90
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 91 PTLLkNLNVLDNIVLPAQKGNEK----------QAD-NLMKKG-QTLMEKMGIAgleqrditqVSGGQLQRAGICRALMG 158
Cdd:cd03250 75 PWIQ-NGTIRENILFGKPFDEERyekvikacalEPDlEILPDGdLTEIGEKGIN---------LSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 159 DPQIIFGDEPTGALNSKSAQEIMT--LLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQ 217
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRI-LVTHQLQLLPHADQIVVLDNGR 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-227 |
1.88e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.08 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLkNLN 98
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQKGNEKQA----------DNLMKKGQTLMEKMGIAGleqrdiTQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEImaaakaanahDFIMEFPNGYDTEVGEKG------SQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 169 TGALNSKSAQeimTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQIVsEMQFFPE 227
Cdd:TIGR00958 645 TSALDAECEQ---LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVV-EMGTHKQ 699
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
2.04e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.77 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKElatLSENALADLR 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 RKQMGFVFQQPTLLKNLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKmgiagLEQRDITQ---VSGGQLQRAGICRALM 157
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR-----LHERRIQRagtMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHVVLE 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-219 |
3.30e-19 |
|
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: 82.93 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRkQMGFVFQQPTLL 94
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRS-RISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 -----KNL------------NVLDNIVLpaqkgneKQADNLMKKGQTLMEKMGIAGLeqrditqvSGGQLQRAGICRALM 157
Cdd:cd03244 91 sgtirSNLdpfgeysdeelwQALERVGL-------KEFVESLPGGLDTVVEEGGENL--------SVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIClVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLT-IAHRLDTIIDSDRILVLDKGRVV 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-248 |
4.28e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.88 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnaLADLRrKQMGFVFQQP-------T 92
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIR-KLVGIVFQNPetqfvgrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 LLKNLNV-LDNIVLPAQKgnekqadnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGA 171
Cdd:PRK13644 95 VEEDLAFgPENLCLPPIE--------IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 172 LNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQIVSEMQffPED---DLNLEE------KMVQVTE- 241
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE--PENvlsDVSLQTlgltppSLIELAEn 244
|
....*...
gi 2519204862 242 -KMREIEI 248
Cdd:PRK13644 245 lKMHGVVI 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
5.05e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.92 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKEL-ATLSENALADLRRKqMGFVFQQP-TLLKNL 97
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKK-VGIVFQFPeHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 98 NVLDNIVLPAQKGNEKQADNLmKKGQTLMEKMGI-AGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKS 176
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAK-QKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2519204862 177 AQEIMTLLSEINQ-QGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:PRK13634 181 RKEMMEMFYKLHKeKGLTTVLVTHSMEDAARyADQIVVMHKGTVF 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-219 |
6.66e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.83 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGM----DEIDEGSVQFDGKELAtlsenaLADLRRKQMGFVFQQPTll 94
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVA------PCALRGRKIATIMQNPR-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIvlpAQKGNE------KQADNlmkkgQTLMEKMGIAGLEQRDIT------QVSGGQLQRAGICRALMGDPQI 162
Cdd:PRK10418 90 SAFNPLHTM---HTHAREtclalgKPADD-----ATLTAALEAVGLENAARVlklypfEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEI-NQQGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARlADDVAVMSHGRIV 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-227 |
1.43e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.24 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLkNLNV 99
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNI-----------VLPAQKGneKQA-DNLMKKGQTLMEKMGIAGLeqrditQVSGGQLQRAGICRALMGDPQIIFGDE 167
Cdd:PRK13657 426 EDNIrvgrpdatdeeMRAAAER--AQAhDFIERKPDGYDTVVGERGR------QLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 168 PTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIVsEMQFFPE 227
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGRTTF-IIAHRLSTVRNADRILVFDNGRVV-ESGSFDE 555
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-234 |
1.77e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.92 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSenaLADLRRKQMGFVfqqPT------L 93
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRLGVAYI---PEdrlgrgL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNLNVLDNIVLPAQKGNEKQADNLMKKG------QTLMEKMGI--AGLEQRdITQVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:COG3845 348 VPDMSVAENLILGRYRRPPFSRGGFLDRKairafaEELIEEFDVrtPGPDTP-ARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 166 DEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD----AKVAaqtQRVLFMSDGQIVSEmqfFPEDDLNLEE 234
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDldeiLALS---DRIAVMYEGRIVGE---VPAAEATREE 493
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-211 |
4.05e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQF-DGKELAtlsenaladlrrkqmgFVFQQP-----T 92
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----------------FLPQRPylplgT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 LlknlnvLDNIVLPAQKGNEKQADnlmkkGQTLMEKMGIAGL-----EQRDITQV-SGGQLQRAGICRALMGDPQIIFGD 166
Cdd:COG4178 442 L------REALLYPATAEAFSDAE-----LREALEAVGLGHLaerldEEADWDQVlSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEiNQQGTAICLVTHDAKVAAQTQRVL 211
Cdd:COG4178 511 EATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-199 |
4.71e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAladlrRKQMGFVF 88
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-----RQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIV-------LPAQkgnekQADNLMkkgQTLMEkmgIAGLEQRDITQV---SGGQLQRAGICRALMG 158
Cdd:PRK13537 87 QFDNLDPDFTVRENLLvfgryfgLSAA-----AARALV---PPLLE---FAKLENKADAKVgelSGGMKRRLTLARALVN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2519204862 159 DPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTH 199
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-200 |
5.57e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 5.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVG---TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID-----EGSVQFDGKELATLS 72
Cdd:PRK14258 1 MSKLIPAikvNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 73 ENaLADLRRkQMGFVFQQPTLLKnLNVLDNIVLPAQKGN---EKQADNLMK---KGQTLMEKmgIAGLEQRDITQVSGGQ 146
Cdd:PRK14258 81 VN-LNRLRR-QVSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpKLEIDDIVEsalKDADLWDE--IKHKIHKSALDLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 147 LQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGT-AICLVTHD 200
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-219 |
1.05e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.99 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKElatLSENALADLrRKQMGFVFQQPTLLkNLNV 99
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASL-RNQVALVSQNVHLF-NDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNIVLPAqkgNEKQADNLMKKGQTLMEKMG-IAGLEQRDITQV-------SGGQLQRAGICRALMGDPQIIFGDEPTGA 171
Cdd:PRK11176 434 ANNIAYAR---TEQYSREQIEEAARMAYAMDfINKMDNGLDTVIgengvllSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2519204862 172 LNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:PRK11176 511 LDTESERAIQAALDELQKNRTSL-VIAHRLSTIEKADEILVVEDGEIV 557
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
1.31e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelatlsenaladLR 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 rkqMGFVFQQ----PTLlkNLNVLDNIVLpaqKGNEKQADNLmkkgqTLMEKMGIAGLEQRDITQVSGGQLQRAGICRAL 156
Cdd:PRK09544 69 ---IGYVPQKlyldTTL--PLTVNRFLRL---RPGTKKEDIL-----PALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 157 MGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAK-VAAQTQRVL 211
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHlVMAKTDEVL 192
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-221 |
1.66e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.46 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGM---DEIDEGSVQFDGkelATLSENALADLRRKqMGFVFQQPt 92
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG---ITLTAKTVWDIREK-VGIVFQNP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 llknlnvlDNIVLPAQKG--------NEKQADNLMKK-GQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQII 163
Cdd:PRK13640 94 --------DNQFVGATVGddvafgleNRAVPRPEMIKiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEI-NQQGTAICLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-219 |
1.87e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 2 KKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFdGKELatlsenaladlrr 81
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 82 kQMGFVFQQPTLLK-NLNVLDNIVLPAQKGNEKQAdnlmkkgQTLMEKMGIAGLEQRD-ITQVSGGQLQRAGICRALMGD 159
Cdd:COG0488 379 -KIGYFDQHQEELDpDKTVLDELRDGAPGGTEQEV-------RGYLGRFLFSGDDAFKpVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLseINQQGTAIcLVTHD----AKVAaqTQRVLFmSDGQIV 219
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEAL--DDFPGTVL-LVSHDryflDRVA--TRILEF-EDGGVR 508
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-221 |
1.88e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGsVQFDGKELatLSENALADLR---- 80
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVL--LGGRSIFNYRdvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 -RKQMGFVFQQPTLLKnLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGLEQRDIT----QVSGGQLQRAGICRA 155
Cdd:PRK14271 99 fRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLART 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHD-AKVAAQTQRVLFMSDGQIVSE 221
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVI-IVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-199 |
2.72e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.49 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELAtlsenALADLRRKQMGFV 87
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-----ARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVLPAQ--KGNEKQADNLMKkgqTLMEkmgIAGLEQR---DITQVSGGQLQRAGICRALMGDPQI 162
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRyfGMSTREIEAVIP---SLLE---FARLESKadaRVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTH 199
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-221 |
5.17e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.94 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGmdEIDE----------GSVQFDGKELATLSENALADLR-----RKQ 83
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAPRLARLRavlpqAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQqptllknlnvLDNIVLPAQKGNEKQADNLMKKGQTL----MEKMGIAGLEQRDITQVSGGQLQRAGICRAL--- 156
Cdd:PRK13547 94 PAFAFS----------AREIVLLGRYPHARRAGALTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 157 ------MGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMSDGQIVSE 221
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARhADRIAMLADGAIVAH 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
6.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.87 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelaTLSENALADLrRKQMGFVFQQPtllKNLNV 99
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKL-RKHIGIVFQNP---DNQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNIVLPAQKGNEKQA---DNLMKKGQTLMEKMGIagLEQRDI--TQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:PRK13648 98 GSIVKYDVAFGLENHAvpyDEMHRRVSEALKQVDM--LERADYepNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2519204862 175 KSAQEIMTLLSEINQ-QGTAICLVTHDAKVAAQTQRVLFMSDGQIVSE 221
Cdd:PRK13648 176 DARQNLLDLVRKVKSeHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-239 |
1.00e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.00 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELA-TLSENALADlrrkQMGF 86
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALEN----GISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 VFQQPTLLKNLNVLDNIVLP--AQKGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLGryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTH----------------DAKVAAqTQRVLFMSDGQIVSEM------ 222
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHkmeeifqlcdeitilrDGQWIA-TQPLAGLTMDKIIAMMvgrslt 236
|
250
....*....|....*..
gi 2519204862 223 QFFPEDDLNLEEKMVQV 239
Cdd:PRK10982 237 QRFPDKENKPGEVILEV 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-237 |
1.39e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEnalADLRRKQMGFV---------F 88
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP---LDAVKKGMAYItesrrdngfF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQKG-----NEKQADNLMKKGQTLMEkMGIAGLEQrDITQVSGGQLQRAGICRALMGDPQII 163
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDGGYKGamglfHEVDEQRTAENQRELLA-LKCHSVNQ-NITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSEMQffPEDDLNLEEKMV 237
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRLTQILT--NRDDMSEEEIMA 504
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-217 |
1.45e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 7 GTNIEKSFG------------QEK-ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEidegSVQFDGKELATLSE 73
Cdd:PLN03211 58 GSNIKRILGhkpkisdetrqiQERtILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ----GNNFTGTILANNRK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 74 NALADLRRkqMGFVFQQPTLLKNLNVLDNIV----LPAQKGNEKQADNLMkkGQTLMEKMGIAGLEQRDITQ-----VSG 144
Cdd:PLN03211 134 PTKQILKR--TGFVTQDDILYPHLTVRETLVfcslLRLPKSLTKQEKILV--AESVISELGLTKCENTIIGNsfirgISG 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 145 GQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTH--DAKVAAQTQRVLFMSDGQ 217
Cdd:PLN03211 210 GERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHqpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-211 |
2.24e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 17 EKIL-RNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRrkqmgFVFQQPTLLK 95
Cdd:PRK13538 13 ERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL-----YLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 NLNVLDNIVLPAQKGNEKQADNLMkkgQTLmEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSK 175
Cdd:PRK13538 88 ELTALENLRFYQRLHGPGDDEALW---EAL-AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 2519204862 176 SAQEIMTLLSEINQQGTAICLVTH-DAKVAAQTQRVL 211
Cdd:PRK13538 164 GVARLEALLAQHAEQGGMVILTTHqDLPVASDKVRKL 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-219 |
4.65e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLL 94
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNlNVLDNIVLpAQKGNEKQADNLMKKGQ--TLMEKMGiAGLEQRDITQ---VSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:PRK10790 428 AD-TFLANVTL-GRDISEEQVWQALETVQlaELARSLP-DGLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2519204862 170 GALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAVREHTTLV-VIAHRLSTIVEADTILVLHRGQAV 553
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-237 |
5.08e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATlseNALADLRRKQMGFV 87
Cdd:PRK10762 8 KGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF---NGPKSSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLKNLNVLDNIVLPAQKGNE----------KQADNLMKkgqtlmeKMGIAGLEQRDITQVSGGQLQRAGICRALM 157
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLGREFVNRfgridwkkmyAEADKLLA-------RLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQIVSEMQFFPEDDLNLEEKM 236
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEIcDDVTVFRDGQFIAEREVADLTEDSLIEMM 237
|
.
gi 2519204862 237 V 237
Cdd:PRK10762 238 V 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-219 |
5.94e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.66 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 11 EKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQ----FDGKELATLSENALADLR------ 80
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELITNPYSKkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 81 --RKQMGFVFQQP--TLLKNLNVLDNIVLPAQKGNEKQADNlmKKGQTLMEKMGI-AGLEQRDITQVSGGQLQRAGICRA 155
Cdd:PRK13631 113 elRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAK--KLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDA-KVAAQTQRVLFMSDGQIV 219
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKIL 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-219 |
1.55e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 2 KKMIVGTNIEKSFGQEK----ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGK----------E 67
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 68 LATLSENALADLRRKQMGFVFQQPtlLKNLN--------VLDNIVLPAQKGNEKQadnlMKKGQTLMEKMGIAGLEQ--- 136
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQEP--MTSLNpvftvgeqIAESIRLHQGASREEA----MVEAKRMLDQVRIPEAQTils 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 137 RDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ-TQRVLFMS 214
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEiADRVLVMY 243
|
....*
gi 2519204862 215 DGQIV 219
Cdd:PRK10261 244 QGEAV 248
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-216 |
1.92e-15 |
|
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: 72.75 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALADLRRKQMGFVFQQPTLLkNLNV 99
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNIVL--PAQKGNEK--------QAD-NLMKKG-QTLMEKMGIagleqrditQVSGGQLQRAGICRALMGDPQIIFGDE 167
Cdd:cd03290 96 EENITFgsPFNKQRYKavtdacslQPDiDLLPFGdQTEIGERGI---------NLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 168 PTGALNSKSAQEIMT--LLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDG 216
Cdd:cd03290 167 PFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-203 |
3.53e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 72.78 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 30 GEFVSIMGPSGSGKTTLMFALSGM-----------DEIDEGSVQFDGKELatlsENALADLRRKQMGfVFQQPtllknlN 98
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKlkpnlgkfddpPDWDEILDEFRGSEL----QNYFTKLLEGDVK-VIVKP------Q 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIvlPAQ-KGneKQADNLMKKGQT-----LMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:cd03236 95 YVDLI--PKAvKG--KVGELLKKKDERgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|.
gi 2519204862 173 NSKSAQEIMTLLSEINQQGTAICLVTHDAKV 203
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVEHDLAV 201
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-216 |
5.33e-15 |
|
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: 71.12 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID--EGSVQFDGKELAtlsenalADLRRkQMGFVFQQPTLLK 95
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD-------KNFQR-STGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 NLNVLDNIVLPAqkgnekqadNLmkkgqtlmekMGIaGLEQRditqvsggqlQRAGICRALMGDPQIIFGDEPTGALNSK 175
Cdd:cd03232 93 NLTVREALRFSA---------LL----------RGL-SVEQR----------KRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2519204862 176 SAQEIMTLLSEINQQGTAICLVTH--DAKVAAQTQRVLFMSDG 216
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-219 |
5.72e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.68 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFD-GKELATLSENALaDLR---RKQMGFVFQQPTL 93
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGP-DGRgraKRYIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNLNVLDNIV------LPAQKGNEKQADNLM------KKGQTLMEKMGiagleqrdiTQVSGGQLQRAGICRALMGDPQ 161
Cdd:TIGR03269 377 YPHRTVLDNLTeaigleLPDELARMKAVITLKmvgfdeEKAEEILDKYP---------DELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 162 IIFGDEPTGALNS----KSAQEIMTLLSEINQqgtAICLVTHDAK-VAAQTQRVLFMSDGQIV 219
Cdd:TIGR03269 448 IVILDEPTGTMDPitkvDVTHSILKAREEMEQ---TFIIVSHDMDfVLDVCDRAALMRDGKIV 507
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-236 |
1.13e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDE-IDEGSVQFDGKELATLS-ENALA--------DlrRKQMGFV 87
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAqgiamvpeD--RKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQqptllknLNVLDNIVLPA----QKGNEKQADNLMKKGQTLMEKMGI--AGLEQRdITQVSGGQLQRAGICRALMGDPQ 161
Cdd:PRK13549 354 PV-------MGVGKNITLAAldrfTGGSRIDDAAELKTILESIQRLKVktASPELA-IARLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSEmqfFPEDDLNLEEKM 236
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGD---LINHNLTQEQVM 498
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-211 |
2.23e-14 |
|
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: 68.72 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFdgkelatlsenaladLRRKQMGFVFQQPtLLKNLN 98
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQRP-YLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQkgnekqaDNLmkkgqtlmekmgiagleqrditqvSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQ 178
Cdd:cd03223 80 LREQLIYPWD-------DVL------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|...
gi 2519204862 179 EIMTLLseiNQQGTAICLVTHDAKVAAQTQRVL 211
Cdd:cd03223 129 RLYQLL---KELGITVISVGHRPSLWKFHDRVL 158
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-220 |
5.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEG-SVQFDGKELATLSENALADLRRKQMGFVFQQP--TLL 94
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPeyQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIVLPAQKGNEKQadNLMKKGQTLMEKMGIA-GLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALN 173
Cdd:PRK13645 105 QETIEKDIAFGPVNLGENKQ--EAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2519204862 174 SKSAQEIMTLLSEINQ-QGTAICLVTHDA-KVAAQTQRVLFMSDGQIVS 220
Cdd:PRK13645 183 PKGEEDFINLFERLNKeYKKRIIMVTHNMdQVLRIADEVIVMHEGKVIS 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-200 |
6.85e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.27 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELaTLSENALADLRrKQ 83
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALR-QQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTL--------------LKNLNVldnivlpAQKGNEKQADNLMkkgqTLMEKMGiagLEQRDITQVSGGQLQR 149
Cdd:PRK13638 79 VATVFQDPEQqifytdidsdiafsLRNLGV-------PEAEITRRVDEAL----TLVDAQH---FRHQPIQCLSHGQKKR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 150 AGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD 200
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-218 |
9.62e-14 |
|
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: 70.24 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID-EGSVQFDGKELATLSEN-------ALADLRRKQMGFVfQ 89
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqairagiAMVPEDRKRHGIV-P 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 90 QPTLLKN--LNVLDNIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGLEqrdITQVSGGQLQRAGICRALMGDPQIIFGDE 167
Cdd:TIGR02633 353 ILGVGKNitLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP---IGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 168 PTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQI 218
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-236 |
1.04e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLS-ENALA--------DlrRKQMGFVFqq 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLAngivyiseD--RKRDGLVL-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 91 ptllkNLNVLDNIVLPA------QKGNEKQADNLMKKGQTL-MEKMGIAGLEQRdITQVSGGQLQRAGICRALMGDPQII 163
Cdd:PRK10762 344 -----GMSVKENMSLTAlryfsrAGGSLKHADEQQAVSDFIrLFNIKTPSMEQA-IGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSEmqfFPEDDLNLEEKM 236
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRISGE---FTREQATQEKLM 488
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-227 |
1.14e-13 |
|
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: 70.36 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSG-MDEIdEGSVQFDGkelatlsenaladlrrkQMGFVFQQpTLLKNLN 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKV-EGHVHMKG-----------------SVAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQKgNEKQADNLMKKGQTLMEKMGIAGLEQRDITQ----VSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:TIGR00957 715 LRENILFGKAL-NEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 175 KSAQEI-------MTLLseinqQGTAICLVTHDAKVAAQTQRVLFMSDGQIvSEMQFFPE 227
Cdd:TIGR00957 794 HVGKHIfehvigpEGVL-----KNKTRILVTHGISYLPQVDVIIVMSGGKI-SEMGSYQE 847
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-200 |
1.20e-13 |
|
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: 65.93 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelatlsenaladlrrkqm 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 85 gfvfqqptllknlnvldnivlpaqkgnekqadnlmkkgqtlmEKMGIagleqrdITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:cd03221 63 ------------------------------------------VKIGY-------FEQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*.
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSeiNQQGTAIcLVTHD 200
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALK--EYPGTVI-LVSHD 126
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-219 |
1.52e-13 |
|
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: 67.56 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENAladlrrkqmGFvfqQPtllkNLN 98
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG---------GF---NP----ELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLpaqkgnekqadNLMKKG--QTLMEKM-----GIAGLEQRDITQV---SGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03220 101 GRENIYL-----------NGRLLGlsRKEIDEKideiiEFSELGDFIDLPVktySSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLcDRALVLEKGKIR 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-218 |
1.75e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.72 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSF-GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLsENALADLrrk 82
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EPADRDI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 83 QMgfVFQQPTLLKNLNVLDNIV--LPAQKGNEKQADNLMKKGQTLMEkmgIAGLEQRDITQVSGGQLQRAGICRALMGDP 160
Cdd:PRK11650 79 AM--VFQNYALYPHMSVRENMAygLKIRGMPKAEIEERVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 161 QIIFGDEPTGALNSK-SAQ---EIMTLLSEINQqgTAIcLVTHDaKVAAQT--QRVLFMSDGQI 218
Cdd:PRK11650 154 AVFLFDEPLSNLDAKlRVQmrlEIQRLHRRLKT--TSL-YVTHD-QVEAMTlaDRVVVMNGGVA 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-219 |
2.36e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLKNlN 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVL----PAQKGNEKQA------DNLMKKGQTLMEKMGIAGLeqrditQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:PRK10789 405 VANNIALgrpdATQQEIEHVArlasvhDDILRLPQGYDTEVGERGV------MLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVI-ISAHRLSALTEASEILVMQHGHIA 528
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-222 |
2.37e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID--EGSVQFDGKELatlsenALADLR-RKQMG 85
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVC------RFKDIRdSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 86 FVF--QQPTLLKNLNVLDNIVLpaqkGNEKQA------DNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALM 157
Cdd:NF040905 80 IVIihQELALIPYLSIAENIFL----GNERAKrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQG-TAIcLVTHD----AKVAaqtQRVLFMSDGQIVSEM 222
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSI-IISHKlneiRRVA---DSITVLRDGRTIETL 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-235 |
2.52e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 13 SFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDgKEL--ATLSEnalaDLRRKQMGFVF-- 88
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLivARLQQ----DPPRNVEGTVYdf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 ------QQPTLLKNLNVLDNIVLpaqkgnEKQADNLMKKGQTLMEKMGIAGLEQRD--ITQV---------------SGG 145
Cdd:PRK11147 87 vaegieEQAEYLKRYHDISHLVE------TDPSEKNLNELAKLQEQLDHHNLWQLEnrINEVlaqlgldpdaalsslSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 146 QLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEInqQGtAICLVTHD-AKVAAQTQRVLFMSDGQIVSemqf 224
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDrSFIRNMATRIVDLDRGKLVS---- 233
|
250
....*....|..
gi 2519204862 225 FPED-DLNLEEK 235
Cdd:PRK11147 234 YPGNyDQYLLEK 245
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
15-219 |
2.60e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.29 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDE----IDEGSVQFDGKELATLSENALADLRRKQMGFVFQQ 90
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 91 PTLLKN------LNVLDNIVLPAQKGNEKQADNLMK-KGQTLMEKMGIAglEQRDIT-----QVSGGQLQRAGICRALMG 158
Cdd:PRK15093 98 PQSCLDpservgRQLMQNIPGWTYKGRWWQRFGWRKrRAIELLHRVGIK--DHKDAMrsfpyELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 159 DPQIIFGDEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVTHDAKVAAQ-TQRVLFMSDGQIV 219
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQwADKINVLYCGQTV 238
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-219 |
2.68e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 2 KKMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMD--EIDEGSVQFDGKELATLSenalADL 79
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLE----PEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 RRKQMGFV-FQQPTLLKNLNVLDNIVL---PAQKGNEKQADNLMKKGQTLMEKMGIAGLEQ----RDITQ-VSGGQLQRA 150
Cdd:CHL00131 81 RAHLGIFLaFQYPIEIPGVSNADFLRLaynSKRKFQGLPELDPLEFLEIINEKLKLVGMDPsflsRNVNEgFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 151 GICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHdakvaaqTQRVL---------FMSDGQIV 219
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-------YQRLLdyikpdyvhVMQNGKII 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
9-220 |
2.72e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.36 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKIlrNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATlSENA--LADLRRKqMGF 86
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD-AEKGicLPPEKRR-IGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 VFQQPTLLKNLNVLDNIVLPAQKGNEKQADNLMkkgqtlmEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIV-------ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHD----AKVAaqtQRVLFMSDGQIVS 220
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREiNIPILYVSHSldeiLRLA---DRVVVLEQGKVKA 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-200 |
4.97e-13 |
|
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: 68.04 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEidegsvQFDGKelATLSENAladlrrkQMGFVFQQPTLL 94
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------DFNGE--ARPQPGI-------KVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIVLPAQKGNEKQA----------------DNLMKKGQTLMEKMGIAG---LEQR---------------DIT 140
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDrfneisakyaepdadfDKLAAEQAELQEIIDAADawdLDSQleiamdalrcppwdaDVT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 141 QVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEInqQGTAIClVTHD 200
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVA-VTHD 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-224 |
1.41e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGmdeidegsvqfdgkELATLSENALADLRRKQMGfvf 88
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCVDVPDNQFG--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 qqptllKNLNVLDNIvlpAQKGNEKQAdnlmkkgqtlMEKMGIAGLEQ-----RDITQVSGGQLQRAGICRALMGDPQII 163
Cdd:COG2401 98 ------REASLIDAI---GRKGDFKDA----------VELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 164 FGDEPTGALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAA--QTQRVLFMSDGQIVSEMQF 224
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDdlQPDLLIFVGYGGVPEEKRR 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-224 |
2.05e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGmdeidegsvqfdgkELATlSENALADLRrKQMGFVFQQPTLLkNLNV 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSH-AETSSVVIR-GSVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDNIVLpaqkGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQV-------SGGQLQRAGICRALMGDPQIIFGDEPTGAL 172
Cdd:PLN03232 696 RENILF----GSDFESERYWRAIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 173 NSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQIVSEMQF 224
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTF 823
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-199 |
3.17e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDG----KELATLsenaladl 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTY-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 80 rRKQMGFVFQQPTLLKNLNVLDNIV--LPAQKGNEKQAD--NLMKKGQTLMEKMGIagleqrditqVSGGQLQRAGICRA 155
Cdd:PRK13540 73 -QKQLCFVGHRSGINPYLTLRENCLydIHFSPGAVGITElcRLFSLEHLIDYPCGL----------LSSGQKRQVALLRL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2519204862 156 LMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTH 199
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-218 |
5.03e-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: 65.42 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 31 EFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLsenalADLRRKQMGFVFQQPTLLKNLNVLDNIVLPAQ-K 109
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN-----LDAVRQSLGMCPQHNILFHHLTVAEHILFYAQlK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 110 GNEKQADNLmkKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQ 189
Cdd:TIGR01257 1032 GRSWEEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS 1109
|
170 180
....*....|....*....|....*....
gi 2519204862 190 QGTAICLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-236 |
7.12e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 21 RNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELatlseNALADLRRKQMGFVF-----QQPTLLK 95
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI-----NALSTAQRLARGLVYlpedrQSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 NLNVLDNIVlpAQKGNEKQADNLMKKGQTLMEK----MGI--AGLEQrDITQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:PRK15439 355 DAPLAWNVC--ALTHNRRGFWIKPARENAVLERyrraLNIkfNHAEQ-AARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 170 GALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSEMqffPEDDLNLEEKM 236
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEISGAL---TGAAINVDTIM 496
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-200 |
7.31e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGsvqfdgkELATLSENALADLRRKQMGFVFQQPTLLKNLNV 99
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-------KISILGQPTRQALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 L-DNIVLPAQKGNEKQADNLMKKGQTL----MEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNS 174
Cdd:PRK15056 96 LvEDVVMMGRYGHMGWLRRAKKRDRQIvtaaLARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*.
gi 2519204862 175 KSAQEIMTLLSEINQQGTAICLVTHD 200
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-219 |
8.09e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 2 KKM----IVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFdgkelatlSENAla 77
Cdd:PRK15064 313 KKLhrnaLEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW--------SENA-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 78 dlrrkQMGFVFQQPT--LLKNLNVLDNIvlpAQKGNEKQADNLMKkgqtlmekmGIAG---LEQRDITQ----VSGGQLQ 148
Cdd:PRK15064 383 -----NIGYYAQDHAydFENDLTLFDWM---SQWRQEGDDEQAVR---------GTLGrllFSQDDIKKsvkvLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 149 RAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSeiNQQGTAIcLVTHDAK-VAAQTQRVLFMSDGQIV 219
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLI-FVSHDREfVSSLATRIIEITPDGVV 514
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-204 |
8.64e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 8.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 17 EKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelatlsENALADlRRKQMGFVFQQPTLLKN 96
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGD-RSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 97 LNVLDNI-VLPAQKGNEKQadnlmKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSK 175
Cdd:PRK13543 97 LSTLENLhFLCGLHGRRAK-----QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
170 180
....*....|....*....|....*....
gi 2519204862 176 SAQEIMTLLSEINQQGTAICLVTHDAKVA 204
Cdd:PRK13543 172 GITLVNRMISAHLRGGGAALVTTHGAYAA 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-219 |
1.99e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVqfdgkelatLSENALAdlrrkqmgFVFQQPTLLkNL 97
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERSIA--------YVPQQAWIM-NA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 98 NVLDNIVLPAQKGNEKQAD---------NLMKKGQTLMEKMGIAGLeqrditQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:PTZ00243 736 TVRGNILFFDEEDAARLADavrvsqleaDLAQLGGGLETEIGEKGV------NLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:PTZ00243 810 LSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-232 |
2.54e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 23 VSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEN-------ALADLRRKQMGFVfqqPTLlk 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagiMLCPEDRKAEGII---PVH-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 nlNVLDNIVLPAQK---------GNEKQADNlmkkGQTLMEKMGI--AGLEQrDITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:PRK11288 347 --SVADNINISARRhhlragcliNNRWEAEN----ADRFIRSLNIktPSREQ-LIMNLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSEM---QFFPEDDLNL 232
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRIAGELareQATERQALSL 491
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-199 |
2.76e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKElATLSENALadlrrkQ 83
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAE------A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQPTLLKNLNVLDNIVLPAQ--KGNEKQADnlmkkgqTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQ 161
Cdd:PRK13539 75 CHYLGHRNAMKPALTVAENLEFWAAflGGEELDIA-------AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2519204862 162 IIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTH 199
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
5.04e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.87 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 1 MKKMIVGTNIEKSF---------------------GQEK-ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDE 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrREEFwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 59 GSVQFDGKelatLSenALADLrrkQMGFvfqQPtllkNLNVLDNIVLPAQkgnekqadnlmkkgqtlmekmgIAGLEQRD 138
Cdd:COG1134 81 GRVEVNGR----VS--ALLEL---GAGF---HP----ELTGRENIYLNGR----------------------LLGLSRKE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 139 ITQV---------------------SGGQLQRAGICRALMGDPQIIFGDEPTG----ALNSKSAQEIMtllsEINQQGTA 193
Cdd:COG1134 123 IDEKfdeivefaelgdfidqpvktySSGMRARLAFAVATAVDPDILLVDEVLAvgdaAFQKKCLARIR----ELRESGRT 198
|
250 260
....*....|....*....|....*..
gi 2519204862 194 ICLVTHDAKVAAQT-QRVLFMSDGQIV 219
Cdd:COG1134 199 VIFVSHSMGAVRRLcDRAIWLEKGRLV 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-216 |
5.16e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSG---MDEIDEGSVQFDGKELATLSEnaladlRRkqMGFVFQQPTLLK 95
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLDSSFQ------RS--IGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 NLNVLDNIVLPA-----QKGNEKQADNLMKKGQTL--MEK-----MGIAG----LEQRditqvsggqlQRAGICRALMGD 159
Cdd:TIGR00956 850 TSTVRESLRFSAylrqpKSVSKSEKMEYVEEVIKLleMESyadavVGVPGeglnVEQR----------KRLTIGVELVAK 919
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 160 PQ-IIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTH--DAKVAAQTQRVLFMSDG 216
Cdd:TIGR00956 920 PKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpSAILFEEFDRLLLLQKG 979
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-197 |
5.22e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGmdeidegsvqfdgkELATLSENaladlRRKQmgfvFQQPTLLk 95
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG--------------ELPLLSGE-----RQSQ----FSHITRL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 NLNVLDNIVlpaqkGNEKQADN--LMKKG----------------------QTLMEKMGIAGLEQRDITQVSGGQLQRAG 151
Cdd:PRK10938 71 SFEQLQKLV-----SDEWQRNNtdMLSPGeddtgrttaeiiqdevkdparcEQLAQQFGITALLDRRFKYLSTGETRKTL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2519204862 152 ICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLV 197
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-206 |
5.25e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALAdlrrKQMGFVFQQPTLLKNLN 98
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLpaqkGNEKQADNLMKKGQTLMEKM-------GIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGA 171
Cdd:PRK10575 102 VRELVAI----GRYPWHGALGRFGAADREKVeeaislvGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 2519204862 172 LNSKSAQEIMTLLSEINQQ-GTAICLVTHDAKVAAQ 206
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAAR 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-247 |
6.15e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 13 SFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGmdeidegsvqfdgkELATLSeNALADLRRK-----QMGFV 87
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG--------------ELPPRS-DASVVIRGTvayvpQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FqqptllkNLNVLDNIVLpaqkGNEKQADNLMKKGQTLMEKMGIAGLEQRDITQV-------SGGQLQRAGICRALMGDP 160
Cdd:PLN03130 691 F-------NATVRDNILF----GSPFDPERYERAIDVTALQHDLDLLPGGDLTEIgergvniSGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIM-TLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQIVSEMQFfpeDDLN----LEEK 235
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRV-LVTNQLHFLSQVDRIILVHEGMIKEEGTY---EELSnngpLFQK 835
|
250
....*....|..
gi 2519204862 236 MVQVTEKMREIE 247
Cdd:PLN03130 836 LMENAGKMEEYV 847
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-230 |
7.91e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATlsenalADLR--RKQMGFVFQQPT 92
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK------ENIRevRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 -LLKNLNVLDNIVL-PAQKGNEKQAdnLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTG 170
Cdd:PRK13652 89 dQIFSPTVEQDIAFgPINLGLDEET--VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 171 ALNSKSAQEIMTLLSEINQQ-GTAICLVTHDAK-VAAQTQRVLFMSDGQIVSE---MQFFPEDDL 230
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYgtvEEIFLQPDL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-219 |
8.30e-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: 59.58 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEID---EGSVQFDGKELATLSENAladlrRKQMG 85
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY-----PGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 86 FVFQQPTLLKNLNVLDNIVLPAQ-KGNEkqadnlMKKGqtlmekmgiagleqrditqVSGGQLQRAGICRALMGDPQIIF 164
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFALRcKGNE------FVRG-------------------ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 165 GDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDA---KVAAQTQRVLFMSDGQIV 219
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQasdEIYDLFDKVLVLYEGRQI 199
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-219 |
1.41e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.80 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELAtlsenaLAD--LRRKQMGFVFQQPTllKNL 97
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH------FGDysYRSQRIRMIFQDPS--TSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 98 N-------VLDnivLPAQKGNEKQADNLMKKGQTLMEKMGIagleQRDIT-----QVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:PRK15112 101 NprqrisqILD---FPLRLNTDLEPEQREKQIIETLRQVGL----LPDHAsyyphMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 166 DEPTGALNSKSAQEIMTLLSEINQ-QGTAICLVT-HDAKVAAQTQRVLFMSDGQIV 219
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEkQGISYIYVTqHLGMMKHISDQVLVMHQGEVV 229
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-72 |
1.06e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.06e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMD--EIDEGSVQFDGKELATLS 72
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELS 71
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-218 |
1.32e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSEN-------ALADLRRKQMGfvfqqpt 92
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfALVTEERRSTG------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 93 LLKNLNVLDNIVLPAQKGNEKQ----ADNLMKKG-QTLMEKMGIAGLEQR-DITQVSGGQLQRAGICRALMGDPQIIFGD 166
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKvgllDNSRMKSDtQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 167 EPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQI 218
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEmPELLGITDRILVMSNGLV 469
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-200 |
3.91e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 28 EAGEFVSIMGPSGSGKTTLMFALSGM--------------DEIDEgsvQFDGKELatlsENALADLRRKQMGFVfqqptl 93
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswDEVLK---RFRGTEL----QDYFKKLANGEIKVA------ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNLNVlDNIvlPAQ-KGNEKQ----ADNLMKKGQtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:COG1245 164 HKPQYV-DLI--PKVfKGTVREllekVDERGKLDE-LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 2519204862 169 TGALNSKSAQEIMTLLSEINQQGTAICLVTHD 200
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-197 |
4.20e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDE--IDEGSVQFDG--KELATLSenaladlrrKQMGFVFQ---- 89
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpKKQETFA---------RISGYCEQndih 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 90 --QPTLLKNLNVLDNIVLPAQKGNEKQ---ADNLMKKGQTLMEKMGIAGLEqrDITQVSGGQLQRAGICRALMGDPQIIF 164
Cdd:PLN03140 965 spQVTVRESLIYSAFLRLPKEVSKEEKmmfVDEVMELVELDNLKDAIVGLP--GVTGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190
....*....|....*....|....*....|....
gi 2519204862 165 GDEPTGALNSKSAQEIM-TLLSEINQQGTAICLV 197
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMrTVRNTVDTGRTVVCTI 1076
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-181 |
1.23e-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: 53.95 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 24 SVEIEAGEF-----VSIMGPSGSGKTTLMFALSGMDEIDEGSVqfdGKELATLSENAlADLRRKQMGFVFQqptLLKNln 98
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKP-QYIKADYEGTVRD---LLSS-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQKGNEkqadnlmkkgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKsaQ 178
Cdd:cd03237 85 ITKDFYTHPYFKTE------------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--Q 150
|
...
gi 2519204862 179 EIM 181
Cdd:cd03237 151 RLM 153
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-200 |
1.25e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 12 KSFGQEK-ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEidegsvQFDGKelATLSENAladlrrkQMGFVFQQ 90
Cdd:PRK11819 14 KVVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGE--ARPAPGI-------KVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 91 PTLLKNLNVLDNIVLPAQKGNEKQA----------------DNLMKKGQTLMEKMGIAG-------LEQ-----R----- 137
Cdd:PRK11819 79 PQLDPEKTVRENVEEGVAEVKAALDrfneiyaayaepdadfDALAAEQGELQEIIDAADawdldsqLEIamdalRcppwd 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 138 -DITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEInqQGTAIClVTHD 200
Cdd:PRK11819 159 aKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PGTVVA-VTHD 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-216 |
2.09e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGK----------ELATLSENALADLRRKQmgfvF 88
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspqtswiMPGTIKDNIIFGLSYDE----Y 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQKGNEKqadnLMKKGQTLmekmgiagleqrditqvSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:TIGR01271 517 RYTSVIKACQLEEDIALFPEKDKTV----LGEGGITL-----------------SGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2519204862 169 TGALNSKSAQEIM-TLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDG 216
Cdd:TIGR01271 576 FTHLDVVTEKEIFeSCLCKLMSNKTRI-LVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-169 |
2.62e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 30 GEFVSIMGPSGSGKTTLMFALSG--------------MDEIDEgsvQFDGKELAT----LSENALADLRRKQMgfVFQQP 91
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepsWDEVLK---RFRGTELQNyfkkLYNGEIKVVHKPQY--VDLIP 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 92 TLLKNlNVLDniVLpaqkgneKQADNLMKKGQtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPT 169
Cdd:PRK13409 174 KVFKG-KVRE--LL-------KKVDERGKLDE-VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-219 |
2.94e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALS----GMDEIDEGSVQFDGkelatLSENALADLRRKQMGFVFQQPTLL 94
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG-----ITPEEIKKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 95 KNLNVLDNIVLPAQ-KGNEKQADNLMKkgQTLMEK-----MGIAGLEQ-RD-------ITQVSGGQLQRAGICRALMGDP 160
Cdd:TIGR00956 151 PHLTVGETLDFAARcKTPQNRPDGVSR--EEYAKHiadvyMATYGLSHtRNtkvgndfVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519204862 161 QIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVThdAKVAAQT-----QRVLFMSDGQIV 219
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA--IYQCSQDayelfDKVIVLYEGYQI 290
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-220 |
5.99e-08 |
|
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: 52.88 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 23 VSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKElatLSENALADLRRkQMGFVFQQPTLLKNLNVLDN 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREAYRQ-LFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 103 IVLPAQkgnekqadnlmkkGQTLMEKMGIAgleqrDITQVSGGQL--------QR---AGICrALMGDPQIIFGDE---- 167
Cdd:COG4615 427 EADPAR-------------ARELLERLELD-----HKVSVEDGRFsttdlsqgQRkrlALLV-ALLEDRPILVFDEwaad 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 168 --P-------TgalnsksaqeimTLLSEINQQG-TAIClVTHDAKVAAQTQRVLFMSDGQIVS 220
Cdd:COG4615 488 qdPefrrvfyT------------ELLPELKARGkTVIA-ISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-230 |
8.13e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 25 VEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATlsenALADLRrKQMGFVFQQPTLLKNLNVLDNIV 104
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVH-QNMGYCPQFDAIDDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 105 LPAQ-KGneKQADNLMKKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTL 183
Cdd:TIGR01257 2035 LYARlRG--VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 184 LSEINQQGTAICLVTHD-AKVAAQTQRVLFM------------------SDGQIVSEMQFFPEDDL 230
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSHSmEECEALCTRLAIMvkgafqclgtiqhlkskfGDGYIVTMKIKSPKDDL 2178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-222 |
1.91e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLsenALADLRRkQMGFVFQQPTLLKN-- 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY---GLRELRR-QFSMIPQDPVLFDGtv 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 97 -LNVldNIVLPAQKGNEKQADNLMK-KGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMG-DPQIIFGDEPTG--- 170
Cdd:PTZ00243 1401 rQNV--DPFLEASSAEVWAALELVGlRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATAnid 1478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2519204862 171 -ALNSKSAQEIMTLLSEInqqgTAIClVTHDAKVAAQTQRVLFMSDGqIVSEM 222
Cdd:PTZ00243 1479 pALDRQIQATVMSAFSAY----TVIT-IAHRLHTVAQYDKIIVMDHG-AVAEM 1525
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-218 |
2.06e-07 |
|
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: 50.62 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 15 GQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIdEGSVQFDGKELATLSENALadlrRKQMGFVFQQ---- 90
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKW----RKAFGVIPQKvfif 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 91 -PTLLKNLNvldnivlPAQKGNEKQadnLMKKGQTLMEKMGIAGL-EQRDITQVSGGQLQRAG----IC--RALMGDPQI 162
Cdd:cd03289 90 sGTFRKNLD-------PYGKWSDEE---IWKVAEEVGLKSVIEQFpGQLDFVLVDGGCVLSHGhkqlMClaRSVLSKAKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519204862 163 IFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVI-LSEHRIEAMLECQRFLVIEENKV 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-218 |
3.18e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLsenALADLrRKQMGFVFQQPTLLKNlN 98
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDL-RFKITIIPQDPVLFSG-S 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQKGNEK-----QADNLMKKGQTLMEKMGIAGLEQRDitQVSGGQLQRAGICRALMGDPQIIFGDEPTGALN 173
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEvwwalELAHLKTFVSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2519204862 174 SKSAQEIMtllSEINQQ--GTAICLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:TIGR00957 1454 LETDNLIQ---STIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-169 |
1.62e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.63 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKiLRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelatlsenaLA----DLRRKQ 83
Cdd:COG1245 345 PDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK---------ISykpqYISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQqptllknlnVLDNIVLPAQKGNEKQADnlmkkgqtLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQII 163
Cdd:COG1245 415 DGTVEE---------FLRSANTDDFGSSYYKTE--------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
....*.
gi 2519204862 164 FGDEPT 169
Cdd:COG1245 478 LLDEPS 483
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-216 |
1.64e-06 |
|
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: 47.64 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFalsgmDEI-DEGSVQFdgkeLATLSenALADLRRKQMGfvfqQPTllknln 98
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAF-----DTIyAEGQRRY----VESLS--AYARQFLGQMD----KPD------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 vLDNI--VLPA----QKGNEKQADN-------LMKKGQTLMEKMGI---------AGLE----QRDITQVSGGQLQRAGI 152
Cdd:cd03270 70 -VDSIegLSPAiaidQKTTSRNPRStvgtvteIYDYLRLLFARVGIrerlgflvdVGLGyltlSRSAPTLSGGEAQRIRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519204862 153 CR----ALMGDPQIIfgDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDG 216
Cdd:cd03270 149 ATqigsGLTGVLYVL--DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPG 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-169 |
1.74e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGqekilrNVSVEIEAG-----EFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelatlsenaLA----D 78
Cdd:PRK13409 344 PDLTKKLG------DFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK---------ISykpqY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 79 LRRKQMGFVFQqptllknlnVLDNIvlpaqkgNEKQADNLMKkgQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMG 158
Cdd:PRK13409 409 IKPDYDGTVED---------LLRSI-------TDDLGSSYYK--SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSR 470
|
170
....*....|.
gi 2519204862 159 DPQIIFGDEPT 169
Cdd:PRK13409 471 DADLYLLDEPS 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-63 |
2.36e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.01 E-value: 2.36e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 3 KMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQF 63
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-217 |
2.46e-06 |
|
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: 47.54 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGK----------ELATLSENALADLRRKQmgfvF 88
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfssqfswiMPGTIKENIIFGVSYDE----Y 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 QQPTLLKNLNVLDNIVLPAQKGNekqadnlmkkgqTLMEKMGIAgleqrditqVSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03291 128 RYKSVVKACQLEEDITKFPEKDN------------TVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2519204862 169 TGALNSKSAQEIM-TLLSEINQQGTAIcLVTHDAKVAAQTQRVLFMSDGQ 217
Cdd:cd03291 187 FGYLDVFTEKEIFeSCVCKLMANKTRI-LVTSKMEHLKKADKILILHEGS 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-212 |
3.53e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 8 TNIEKSFGQEKilRNVSVEiEAGEFvSIMGPSGSGKTTLMFAlsgmdeiDEGSVQFDGKELATLSenaLADLRrKQMGFV 87
Cdd:PTZ00265 1237 TNEQDYQGDEE--QNVGMK-NVNEF-SLTKEGGSGEDSTVFK-------NSGKILLDGVDICDYN---LKDLR-NLFSIV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLLkNLNVLDNIVLpaqkGNEKQADNLMKKGQTLME-KMGIAGLEQRDITQV-------SGGQLQRAGICRALMGD 159
Cdd:PTZ00265 1302 SQEPMLF-NMSIYENIKF----GKEDATREDVKRACKFAAiDEFIESLPNKYDTNVgpygkslSGGQKQRIAIARALLRE 1376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 160 PQIIFGDEPTGALNSKSAQEIMTLLSEINQQG--TAICLVTHDAKVAAQTQRVLF 212
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVF 1431
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
5-219 |
8.73e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 5 IVGTNIEKSfGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGmdEID-----EGSVQFDGKEL---------AT 70
Cdd:PLN03140 167 MLGINLAKK-TKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAG--KLDpslkvSGEITYNGYRLnefvprktsAY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 71 LSENAL----------ADLRRKQMGfVFQQPTLLKNL--NVLDNIVLPaqkgnEKQADNLMKKgqTLME----------K 128
Cdd:PLN03140 244 ISQNDVhvgvmtvketLDFSARCQG-VGTRYDLLSELarREKDAGIFP-----EAEVDLFMKA--TAMEgvksslitdyT 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 129 MGIAGLeqrDITQ-----------VSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLV 197
Cdd:PLN03140 316 LKILGL---DICKdtivgdemirgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM 392
|
250 260
....*....|....*....|....*.
gi 2519204862 198 THdAKVAAQT----QRVLFMSDGQIV 219
Cdd:PLN03140 393 SL-LQPAPETfdlfDDIILLSEGQIV 417
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-169 |
1.07e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQ-FDGkelatlsenALADLR-RKQMG----FVFQqpTL 93
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGG---------DMADARhRRAVCpriaYMPQ--GL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 LKNL----NVLDNIV----LPAQKGNEKQAdnlmkKGQTLMEKMGIAGLEQRDITQVSGGQLQRAGICRALMGDPQIIFG 165
Cdd:NF033858 86 GKNLyptlSVFENLDffgrLFGQDAAERRR-----RIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
....
gi 2519204862 166 DEPT 169
Cdd:NF033858 161 DEPT 164
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
12-221 |
1.09e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 12 KSFGQEKILRNVSVEIEAGEFVSIMGPSGSG--KTTLMFALSGMDEidegsvqfdGKE---LATLSENALAdlRRKQMGF 86
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDA---------GRRpwrF*TWCANRRA--LRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 87 vfQQPTLL---------KNLNVLDNIVLPAQKGNEKQADNLMKKGqTLMEKMGiagleqRDITQVSGGQLQRAGICRALM 157
Cdd:NF000106 90 --HRPVR*grresfsgrENLYMIGR*LDLSRKDARARADELLERF-SLTEAAG------RAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 158 GDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSD-GQIVSE 221
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDrGRVIAD 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-222 |
1.35e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 16 QEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMD---EIdEGSVQFDGKELATLS-----ENALA----DlrRKQ 83
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygrNI-SGTVFKDGKEVDVSTvsdaiDAGLAyvteD--RKG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 84 MGFVFQQptllknlNVLDNIVLPAQKG-------NEKQAdnlMKKGQTLMEKMGI--AGLEQRdITQVSGGQLQRAGICR 154
Cdd:NF040905 349 YGLNLID-------DIKRNITLANLGKvsrrgviDENEE---IKVAEEYRKKMNIktPSVFQK-VGNLSGGNQQKVVLSK 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 155 ALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHD-AKVAAQTQRVLFMSDGQIVSEM 222
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSElPELLGMCDRIYVMNEGRITGEL 486
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-219 |
1.79e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 44.90 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLK--- 95
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQDPILFSgsi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 96 --NLNvldnivlPAQKGNEKQADNLMKKGQ-TLMEKMGIAGLEQRdITQ----VSGGQLQRAGICRALMGDPQIIFGDEP 168
Cdd:cd03288 112 rfNLD-------PECKCTDDRLWEALEIAQlKNMVKSLPGGLDAV-VTEggenFSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 169 TGALNSKS----AQEIMTLLSEinqqgTAICLVTHDAKVAAQTQRVLFMSDGQIV 219
Cdd:cd03288 184 TASIDMATenilQKVVMTAFAD-----RTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-61 |
1.79e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 1.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2519204862 3 KMIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSV 61
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-47 |
2.86e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.68 E-value: 2.86e-05
10 20
....*....|....*....|....*...
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLM 47
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-218 |
3.91e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 23 VSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKELATLSENALadlrRKQMGFVFQQPTLLKNLnvLDN 102
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY----RKLFSAVFTDFHLFDQL--LGP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 103 IVLPAqkgNEKQADNLMKKGQtLMEKMGIAGLEQRDItQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKSAQEIMT 182
Cdd:PRK10522 416 EGKPA---NPALVEKWLERLK-MAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*..
gi 2519204862 183 -LLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQI 218
Cdd:PRK10522 491 vLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-211 |
3.99e-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: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIdEGSVQFDGkelatLSENALA-DLRRK 82
Cdd:TIGR01271 1219 DVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDG-----VSWNSVTlQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 83 QMGFVFQQ-----PTLLKNLNvldnivlpaqkGNEKQADNLMKKgqtLMEKMGIAG-LEQ----RDITQVSGGQLQRAG- 151
Cdd:TIGR01271 1293 AFGVIPQKvfifsGTFRKNLD-----------PYEQWSDEEIWK---VAEEVGLKSvIEQfpdkLDFVLVDGGYVLSNGh 1358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 152 -----ICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSEINQQGTAIcLVTHDAKVAAQTQRVL 211
Cdd:TIGR01271 1359 kqlmcLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI-LSEHRVEALLECQQFL 1422
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-47 |
6.54e-05 |
|
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: 42.99 E-value: 6.54e-05
10 20
....*....|....*....|....*...
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLM 47
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI 38
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-217 |
6.94e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.31 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALsgmdeidegsvqfdgkeLATLSENALADLRRKqmgfVFQQPTLlknlnV 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLPK----FSRNKLI-----F 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 100 LDnivlpaqkgnekQADNLMKKGqtlmekMGIAGLEQRDITqVSGGQLQRAGICRALMGDPQ---IIFgDEPTGALNSKS 176
Cdd:cd03238 65 ID------------QLQFLIDVG------LGYLTLGQKLST-LSGGELQRVKLASELFSEPPgtlFIL-DEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2519204862 177 AQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVLFMSDGQ 217
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-176 |
1.02e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 18 KILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVqfdgkeLATLSENaLADLR----RKQMGFVFQQPTL 93
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI------IINDSHN-LKDINlkwwRSKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 94 ---------------LKNLNVLDNIVlpAQKGNEKQAD---------------NLM------------KKGQTLMEKMGI 131
Cdd:PTZ00265 472 fsnsiknnikyslysLKDLEALSNYY--NEDGNDSQENknkrnscrakcagdlNDMsnttdsneliemRKNYQTIKDSEV 549
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 132 AGLEQR--------------------DITQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSKS 176
Cdd:PTZ00265 550 VDVSKKvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-47 |
1.14e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 1.14e-04
10 20
....*....|....*....|....*...
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLM 47
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLV 648
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
1.19e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 1.19e-04
10 20
....*....|....*....|....*..
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTL 46
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-48 |
1.34e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.34e-04
10 20
....*....|....*....|....*....
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMF 48
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSLAF 44
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-48 |
2.23e-04 |
|
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: 42.31 E-value: 2.23e-04
10 20
....*....|....*....|....*....
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMF 48
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSLAF 40
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-77 |
2.45e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFD-GKELATLSENALA 77
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQFA 75
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
19-217 |
2.92e-04 |
|
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: 40.42 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 19 ILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSgmdeidegsvqfdgkelatlsenaladlrrkqMGFVFQQPTLLKNLN 98
Cdd:cd03227 10 YFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG--------------------------------LALGGAQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 99 VLDNIVLPAQKgnekqadnlmkkgqtlmekMGIAGLeqrdITQVSGGQLQRAGIC-----RALMGDPQIIFgDEPTGALN 173
Cdd:cd03227 58 VKAGCIVAAVS-------------------AELIFT----RLQLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2519204862 174 SKSAQEIMTLLSEINQQGTAICLVTHDAKV---AAQTQRVLFMSDGQ 217
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHLPELaelADKLIHIKKVITGV 160
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-200 |
5.68e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 4 MIVGTNIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDG--------KELATLSENA 75
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 76 L-----ADLRRKQMGFVFQQPTLLKNLNVldnIVLPAQKGNEKQADNLMKKGQTLMEKMGIAGLE-QRDITQVSGGQLQR 149
Cdd:PRK10636 81 LeyvidGDREYRQLEAQLHDANERNDGHA---IATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2519204862 150 AGICRALMGDPQIIFGDEPTGALNSKSAQEIMTLLSeiNQQGTAIcLVTHD 200
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK--SYQGTLI-LISHD 205
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
88-211 |
5.92e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTLlKNLNVLDNIVLPAQKGNEKQADNLMKKGQTLMEkMGIAGLE-QRDITQVSGGQLQRAGICR----ALMGDPQI 162
Cdd:PRK00635 424 FQQMSL-QELFIFLSQLPSKSLSIEEVLQGLKSRLSILID-LGLPYLTpERALATLSGGEQERTALAKhlgaELIGITYI 501
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2519204862 163 IfgDEPTGALNSKSAQEIMTLLSEINQQGTAICLVTHDAKVAAQTQRVL 211
Cdd:PRK00635 502 L--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-65 |
2.20e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 2.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDG 65
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-200 |
3.32e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.39 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 9 NIEKSFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQfdgkeLATLSENALADLRRKqmgfvf 88
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-----CGTKLEVAYFDQHRA------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 89 qqpTLLKNLNVLDNIvlpaqkGNEKQadNLMKKGQtlmeKMGIAGLEQ-------RDITQV---SGGQLQRAGICRALMG 158
Cdd:PRK11147 393 ---ELDPEKTVMDNL------AEGKQ--EVMVNGR----PRHVLGYLQdflfhpkRAMTPVkalSGGERNRLLLARLFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2519204862 159 DPQIIFGDEPTGALNSksaqEIMTLLSEI--NQQGTAIcLVTHD 200
Cdd:PRK11147 458 PSNLLILDEPTNDLDV----ETLELLEELldSYQGTVL-LVSHD 496
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-48 |
4.06e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 4.06e-03
10 20
....*....|....*....|....*....
gi 2519204862 20 LRNVSVEIEAGEFVSIMGPSGSGKTTLMF 48
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSLAF 44
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-217 |
4.08e-03 |
|
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: 37.17 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 26 EIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKelatlsenaladlrrkqmgfvfqqptllknlnvldNIVL 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI-----------------------------------TPVY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 106 PAQKgnekqadnlmkkgqtlmekmgiagleqrdiTQVSGGQLQRAGICRALMGDPQIIFGDEPTGALNSK---SAQEIMT 182
Cdd:cd03222 66 KPQY------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIR 115
|
170 180 190
....*....|....*....|....*....|....*
gi 2519204862 183 LLSEINQQgTAIcLVTHDAKVAAQTQRVLFMSDGQ 217
Cdd:cd03222 116 RLSEEGKK-TAL-VVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-218 |
4.99e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.69 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 13 SFGQEKILRNVSVEIEAGEFVSIMGPSGSGKTTLMFALSGmdeiDE-----GSVQFDGKELAtlSENALADLRRKqMGFV 87
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHpqgysNDLTLFGRRRG--SGETIWDIKKH-IGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 88 FQQPTL-----LKNLNVL-----DNIVLpaqkgneKQA--DNLMKKGQTLMEKMGIAG-LEQRDITQVSGGQLQRAGICR 154
Cdd:PRK10938 342 SSSLHLdyrvsTSVRNVIlsgffDSIGI-------YQAvsDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVR 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519204862 155 ALMGDPQIIFGDEPTGALNSKSAQ------EIMtllseINQQGTAICLVTHDAKVAAQ--TQRVLFMSDGQI 218
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQlvrrfvDVL-----ISEGETQLLFVSHHAEDAPAciTHRLEFVPDGDI 481
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
15-46 |
9.27e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 36.99 E-value: 9.27e-03
10 20 30
....*....|....*....|....*....|....
gi 2519204862 15 GQEKILRNVsveIEAGEFVSIM--GPSGSGKTTL 46
Cdd:PRK13342 22 GPGKPLRRM---IEAGRLSSMIlwGPPGTGKTTL 52
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-108 |
9.67e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.03 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519204862 22 NVSVEIEAGEFVSIMGPSGSGKTTLMFALSGMDEIDEGSVQFDGKE-----LATlsenaladlrRKQMGFVFQQPTLLKN 96
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdagdIAT----------RRRVGYMSQAFSLYGE 353
|
90
....*....|..
gi 2519204862 97 LNVLDNIVLPAQ 108
Cdd:NF033858 354 LTVRQNLELHAR 365
|
|
| |
