|
Name |
Accession |
Description |
Interval |
E-value |
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-202 |
8.38e-69 |
|
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: 210.27 E-value: 8.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKI-GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVGY 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLD 163
Cdd:COG1122 80 VFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489043565 164 EPTTALDADMQRRIAAILKSLD---VTQIIVSHDKEFISDVA 202
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAELA 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-208 |
1.38e-60 |
|
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: 188.44 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 6 SLKNVCAKI--GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVGY 83
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS-LKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLD 163
Cdd:cd03225 80 VFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 164 EPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVASAMYRL 208
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLkaeGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-213 |
1.02e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 155.74 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHKisNLDEYKP--FRRDVG 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-YLDGK--PLSAMPPpeWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQESndCFICPSVLDDVIFSLLSRGKDKDGSRAKA--EKILRELEIwhLKDEIVfNLSGGEKKLVALAGILVAEPKIL 160
Cdd:COG4619 78 YVPQEP--ALWGGTVRDNLPFPFQLRERKFDRERALEllERLGLPPDI--LDKPVE-RLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489043565 161 LLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFISDVASAMYRLTKSGL 213
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-194 |
4.71e-46 |
|
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: 152.89 E-value: 4.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGYL 84
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR-RELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNDCFicP-SVLDDVIF------SLLSRGKDKDgsRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEP 157
Cdd:COG1120 81 PQEPPAPF--GlTVRELVALgryphlGLFGRPSAED--REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489043565 158 KILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHD 194
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLarerGRTVVMVLHD 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-202 |
5.03e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.55 E-value: 5.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdeykpfRRD 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQ--ESNDCFicP-SVLDdVI-------FSLLSRGKDKDgsRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALA 150
Cdd:COG1121 77 IGYVPQraEVDWDF--PiTVRD-VVlmgrygrRGLFRRPSRAD--REAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVA 202
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTHDLGAVREYF 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-200 |
2.80e-44 |
|
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: 146.90 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPFRRDVGYL 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP---PERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQesNDC-FICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLD 163
Cdd:cd03259 78 FQ--DYAlFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 164 EPTTALDA----DMQRRIAAILKSLDVTQIIVSHDKE---FISD 200
Cdd:cd03259 156 EPLSALDAklreELREELKELQRELGITTIYVTHDQEealALAD 199
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-203 |
4.60e-44 |
|
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: 146.25 E-value: 4.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 6 SLKNVCAKIGERT-LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHKISNldeYKPFRRDVGYL 84
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-LLNGKPIK---AKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNDCFICPSVLDDVIFSLlsrgKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:cd03226 77 MQDVDYQLFTDSVREELLLGL----KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489043565 165 PTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVAS 203
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELaaqGKAVIVITHDYEFLAKVCD 194
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-199 |
1.74e-43 |
|
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: 145.33 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCA--KIGERTLF--ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK--PFR 78
Cdd:cd03255 1 IELKNLSKtyGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 RD-VGYLFQESNdcfICP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVA 155
Cdd:cd03255 81 RRhIGFVFQSFN---LLPdlTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 156 EPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFIS 199
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELnkeaGTTIVVVTHDPELAE 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-196 |
1.84e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 148.71 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdeyKPFRRDVGYL 84
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL---PPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQeSNDCFicP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:COG3842 83 FQ-DYALF--PhlTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 163 DEPTTALDA----DMQRRIAAILKSLDVTQIIVSHDKE 196
Cdd:COG3842 160 DEPLSALDAklreEMREELRRLQRELGITFIYVTHDQE 197
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-196 |
2.75e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.98 E-value: 2.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSctISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHK--ISNLDeykPFR 78
Cdd:COG1118 1 MS--IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLNGRdlFTNLP---PRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 RDVGYLFQEsNDCFicP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAE 156
Cdd:COG1118 75 RRVGFVFQH-YALF--PhmTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 157 PKILLLDEPTTALDA----DMQRRIAAILKSLDVTQIIVSHDKE 196
Cdd:COG1118 152 PEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVTHDQE 195
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-202 |
8.90e-41 |
|
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: 136.93 E-value: 8.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNL-DEYKPFRRDVGY 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLeDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdcficpsvlddvIFSLLSRgkdkdgsrakaekilreleiwhlKDEIVFNLSGGEKKLVALAGILVAEPKILLLD 163
Cdd:cd03229 81 VFQDFA------------LFPHLTV-----------------------LENIALGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489043565 164 EPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFISDVA 202
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqaqlGITVVLVTHDLDEAARLA 168
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-194 |
1.90e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 136.03 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 6 SLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVGYLF 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS-PKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 86 QesndcficpsvlddvifsllsrgkdkdgsrakaekILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEP 165
Cdd:cd03214 80 Q-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 166 TTALDADMQRRIAAILKSL----DVTQIIVSHD 194
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLarerGKTVVMVLHD 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-194 |
2.86e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 138.30 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVC----AKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykpfrRD 80
Cdd:COG1116 8 LELRGVSkrfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG------PD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQEsndcficP------SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILV 154
Cdd:COG1116 82 RGVVFQE-------PallpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 155 AEPKILLLDEPTTALDA----DMQRRIAAILKSLDVTQIIVSHD 194
Cdd:COG1116 155 NDPEVLLMDEPFGALDAltreRLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-206 |
7.48e-40 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 136.48 E-value: 7.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNL--DEYKPFRRDVG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQeSNDCFICPSVLDDVIFSLLSRGKDKDGS-RAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:cd03261 81 MLFQ-SGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489043565 162 LDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHDKEFISDVASAMY 206
Cdd:cd03261 160 YDEPTAGLDpiasGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-210 |
8.13e-40 |
|
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: 133.91 E-value: 8.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 6 SLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVGYLF 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-LEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 86 QesndcficpsvlddvifsllsrgkdkdgsrakaekilreleiwhlkdeivfnLSGGEKKLVALAGILVAEPKILLLDEP 165
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 166 TTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVASAMYRLTK 210
Cdd:cd00267 108 TSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-194 |
2.18e-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: 2.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEykPFRRDVGYL 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE--DYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQEsNDCFICPSVLDDVIFslLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:COG4133 81 GHA-DGLKPELTVRENLRF--WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 489043565 165 PTTALDADMQRRIAAILKSLdVTQ----IIVSHD 194
Cdd:COG4133 158 PFTALDAAGVALLAELIAAH-LARggavLLTTHQ 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-207 |
2.29e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.79 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCaKI-----GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK 75
Cdd:COG1136 1 MSPLLELRNLT-KSygtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 76 --PFRRD-VGYLFQESN--DCFicpSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALA 150
Cdd:COG1136 80 laRLRRRhIGFVFQFFNllPEL---TALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDkefiSDVASAMYR 207
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrelGTTIVMVTHD----PELAARADR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-202 |
7.19e-39 |
|
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: 140.04 E-value: 7.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKN--VCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCG---GHIELFHHKISNLDEyK 75
Cdd:COG1123 1 MTPLLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 76 PFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVA 155
Cdd:COG1123 80 LRGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489043565 156 EPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFISDVA 202
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELqrerGTTVLLITHDLGVVAEIA 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-167 |
1.88e-38 |
|
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: 130.08 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 20 FENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNlDEYKPFRRDVGYLFQESNDcFICPSVLD 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQL-FPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489043565 100 DVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIV----FNLSGGEKKLVALAGILVAEPKILLLDEPTT 167
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-196 |
3.71e-38 |
|
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: 131.98 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPFRRDVGYL 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---PHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQeSNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:cd03300 78 FQ-NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 489043565 165 PTTALDA----DMQRRIAAILKSLDVTQIIVSHDKE 196
Cdd:cd03300 157 PLGALDLklrkDMQLELKRLQKELGITFVFVTHDQE 192
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-194 |
4.95e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 131.72 E-value: 4.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISnlDEYKPFRRDVGYL 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNdcfICP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:COG1131 79 PQEPA---LYPdlTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 489043565 163 DEPTTALDADMQRRIAAILKSL---DVTQIIVSHD 194
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELaaeGKTVLLSTHY 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-194 |
1.11e-37 |
|
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: 130.28 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVC----AKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdeykpfRRD 80
Cdd:cd03293 1 LEVRNVSktygGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP------GPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQESNdcfICP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPK 158
Cdd:cd03293 75 RGYVFQQDA---LLPwlTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489043565 159 ILLLDEPTTALDA----DMQRRIAAILKSLDVTQIIVSHD 194
Cdd:cd03293 152 VLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTHD 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-206 |
4.81e-37 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 134.81 E-value: 4.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhkisnldeykpfRRD--VGYL 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------------PKGlrIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQE--SNDCFicpSVLDDVIFSLLSRGK---------------DKDGSR-----------------AKAEKILRELEIWH 130
Cdd:COG0488 67 PQEppLDDDL---TVLDTVLDGDAELRAleaeleeleaklaepDEDLERlaelqeefealggweaeARAEEILSGLGFPE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489043565 131 LK-DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVASAMY 206
Cdd:COG0488 144 EDlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRIL 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-198 |
5.32e-37 |
|
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: 127.54 E-value: 5.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 23 LNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIEL----FHHKISNLDEYkpfRRDVGYLFQESNDCFICPSVL 98
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIdgepLDYSRKGLLER---RQRVGLVFQDPDDQLFAADVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 99 DDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIA 178
Cdd:TIGR01166 88 QDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQML 167
|
170 180
....*....|....*....|...
gi 489043565 179 AILKSLD---VTQIIVSHDKEFI 198
Cdd:TIGR01166 168 AILRRLRaegMTVVISTHDVDLA 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-203 |
6.99e-37 |
|
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: 128.03 E-value: 6.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISN-LDEYKPFRRDVGY 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdCFICPSVLDDVIFSLLS-RGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03262 81 VFQQFN-LFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 163 DEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVAS 203
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVAD 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-194 |
1.71e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.58 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MScTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPFRRD 80
Cdd:COG3839 1 MA-SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP---PKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQEsndcficP------SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILV 154
Cdd:COG3839 77 IAMVFQS-------YalyphmTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 155 AEPKILLLDEPTTALDA----DMQRRIAAILKSLDVTQIIVSHD 194
Cdd:COG3839 150 REPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
33-207 |
2.89e-36 |
|
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: 132.72 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD--EYKPFRRDVGYLFQESNDCFIC-PSVLDDVIFSLLSRG 109
Cdd:COG1123 294 LGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrSLRELRRRVQMVFQDPYSSLNPrMTVGDIIAEPLRLHG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 110 KdkdGSRAKAEKILRE-LEIWHLKDEIV----FNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:COG1123 374 L---LSRAERRERVAElLERVGLPPDLAdrypHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDL 450
|
170 180 190
....*....|....*....|....*....|
gi 489043565 185 ----DVTQIIVSHD---KEFISDVASAMYR 207
Cdd:COG1123 451 qrelGLTYLFISHDlavVRYIADRVAVMYD 480
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-194 |
5.50e-36 |
|
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: 125.72 E-value: 5.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 6 SLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNldeykpFRRDVGYLF 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK------ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 86 QESN-DCFICPSVLDDVIFSLLSR----GKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKIL 160
Cdd:cd03235 75 QRRSiDRDFPISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 489043565 161 LLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHD 194
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELrreGMTILVVTHD 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-194 |
7.96e-36 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 126.25 E-value: 7.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNAtHKDKI-ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD--EYKPFRRDV 81
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDV-PRGEIlAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQES---NDCficpSVLDDVIFSLLSRGKDkdgSRAKAEKILRE-LEIWHLKD-------EivfnLSGGEKKLVALA 150
Cdd:COG1127 85 GMLFQGGalfDSL----TVFENVAFPLREHTDL---SEAEIRELVLEkLELVGLPGaadkmpsE----LSGGMRKRVALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAA-IL---KSLDVTQIIVSHD 194
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDElIRelrDELGLTSVVVTHD 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-194 |
1.09e-35 |
|
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: 125.31 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNV----CAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEY--KPFR 78
Cdd:cd03257 2 LEVKNLsvsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 RDVGYLFQESNDCFiCP--SVLDDVIFSLLSRGKDKDgsRAKAEKILRELEIWHLKDEIVFN-----LSGGEKKLVALAG 151
Cdd:cd03257 82 KEIQMVFQDPMSSL-NPrmTIGEQIAEPLRIHGKLSK--KEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 152 ILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHD 194
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeelGLTLLFITHD 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-194 |
1.89e-35 |
|
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: 124.29 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPFRRDVGYL 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---PKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQesnDCFICP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03301 78 FQ---NYALYPhmTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 489043565 163 DEPTTALDA----DMQRRIAAILKSLDVTQIIVSHD 194
Cdd:cd03301 155 DEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-203 |
2.51e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 124.74 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSctISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS-----NLDEYK 75
Cdd:COG4161 1 MS--IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 76 PFRRDVGYLFQESNdcfICP--SVLDDVI---FSLLsrGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALA 150
Cdd:COG4161 79 LLRQKVGMVFQQYN---LWPhlTVMENLIeapCKVL--GLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSLD---VTQIIVSHDKEFISDVAS 203
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqtgITQVIVTHEVEFARKVAS 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-202 |
5.16e-35 |
|
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: 122.12 E-value: 5.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISnlDEYKPFRRDVGYL 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQEsndcficpsvlddviFSLlsrgkdkdgsrakaekilreleIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:cd03230 79 PEE---------------PSL----------------------YENLTVRENLKLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489043565 165 PTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVA 202
Cdd:cd03230 122 PTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLC 162
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-198 |
7.44e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.24 E-value: 7.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCaKI--GERTLFENLNLnathkdKIA------LIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK- 75
Cdd:COG2884 2 IRFENVS-KRypGGREALSDVSL------EIEkgefvfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 76 PF-RRDVGYLFQesnDCFICP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGI 152
Cdd:COG2884 75 PYlRRRIGVVFQ---DFRLLPdrTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489043565 153 LVAEPKILLLDEPTTALDADMQRRIAAILKSLD---VTQIIVSHDKEFI 198
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINrrgTTVLIATHDLELV 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
34-202 |
2.12e-34 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 122.16 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYLFQESNdcfICP--SVLDDVI--------- 102
Cdd:cd03219 30 GLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPR---LFPelTVLENVMvaaqartgs 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 103 -FSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAIL 181
Cdd:cd03219 107 gLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELI 186
|
170 180
....*....|....*....|....
gi 489043565 182 KSL---DVTQIIVSHDKEFISDVA 202
Cdd:cd03219 187 RELrerGITVLLVEHDMDVVMSLA 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-210 |
3.24e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 122.99 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS--NLDEykpFRRDVGYLFQESNDCF 92
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIRE---VRKFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 93 ICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALD-- 170
Cdd:PRK13652 92 FSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpq 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489043565 171 --ADMQRRIAAILKSLDVTQIIVSHDKEFISDVASAMYRLTK 210
Cdd:PRK13652 172 gvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-202 |
3.68e-34 |
|
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: 121.68 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPFRRDVGY 83
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdCFICPSVLDDVIFSL----LSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKI 159
Cdd:cd03296 79 VFQHYA-LFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 160 LLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFISDVA 202
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLhdelHVTTVFVTHDQEEALEVA 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-193 |
5.64e-34 |
|
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: 119.41 E-value: 5.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERT--LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVG 82
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDL-ESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQESndcficpsvlddVIFSllsrgkdkdGSrakaekilreleiwhLKDEIvfnLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03228 80 YVPQDP------------FLFS---------GT---------------IRENI---LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 163 DEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:cd03228 121 DEATSALDPETEALILEALRALakGKTVIVIAH 153
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-209 |
8.28e-34 |
|
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: 8.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 9 NVCAKIGERTLFENLNLNATHK-DKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFH------HKISNLdeyKPFRRDV 81
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLNeEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINL---PPQQRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQEsNDCFICPSVLDDVIFSL--LSRGKDKDgsraKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKI 159
Cdd:cd03297 78 GLVFQQ-YALFPHLNVRENLAFGLkrKRNREDRI----SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489043565 160 LLLDEPTTALDADM----QRRIAAILKSLDVTQIIVSHDkefisdvASAMYRLT 209
Cdd:cd03297 153 LLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD-------LSEAEYLA 199
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-202 |
5.35e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 118.56 E-value: 5.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHI----ELFHHKISNLDEYkpfRRD 80
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgEDLTDSKKDINKL---RRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQESNdCFicP--SVLDDVIFSLL-SRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEP 157
Cdd:COG1126 79 VGMVFQQFN-LF--PhlTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 158 KILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVA 202
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVA 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-202 |
6.43e-33 |
|
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: 115.62 E-value: 6.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfHHKISnldeykpfrrdVGYL 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK-----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQesndcficpsvlddvifsllsrgkdkdgsrakaekilreleiwhlkdeivfnLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:cd03221 69 EQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 165 PTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVA 202
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVA 134
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
34-202 |
2.68e-32 |
|
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: 117.45 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYLFQESNdcfICP--SVLDDV---------- 101
Cdd:COG0411 34 GLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIARTFQNPR---LFPelTVLENVlvaaharlgr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 102 -----IFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRR 176
Cdd:COG0411 111 gllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEE 190
|
170 180 190
....*....|....*....|....*....|
gi 489043565 177 IAAILKSL----DVTQIIVSHDKEFISDVA 202
Cdd:COG0411 191 LAELIRRLrderGITILLIEHDMDLVMGLA 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-199 |
4.04e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 116.83 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGE----RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRD 80
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR-RKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQEsndcficP--SV-----LDDVIFSLLsRGKDKDGSRAKAEKILRELEiwhLKDEIVFN----LSGGEKKLVAL 149
Cdd:COG1124 81 VQMVFQD-------PyaSLhprhtVDRILAEPL-RIHGLPDREERIAELLEQVG---LPPSFLDRyphqLSGGQRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489043565 150 AGILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFIS 199
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLreerGLTYLFVSHDLAVVA 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-203 |
1.12e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.50 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKI-----SNLDEYKPFR 78
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 RDVGYLFQESNdcfICP--SVLDDVIFSLLS-RGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVA 155
Cdd:PRK11124 82 RNVGMVFQQYN---LWPhlTVQQNLIEAPCRvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489043565 156 EPKILLLDEPTTALDADMQRRIAAILKSLD---VTQIIVSHDKEFISDVAS 203
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAetgITQVIVTHEVEVARKTAS 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-196 |
1.17e-31 |
|
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: 115.13 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLfENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdeyKPFRRDVGYL 84
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL---PPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQesnDCFICP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03299 77 PQ---NYALFPhmTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 163 DEPTTALDADMQRRIAAILK----SLDVTQIIVSHDKE 196
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHDFE 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-196 |
1.35e-31 |
|
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: 115.18 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPC-GGHIELFHHK-----ISNLdeykpfR 78
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERrggedVWEL------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 RDVGYL-------FQESNdcficpSVLDDVI---FSLLSRGKD-KDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLV 147
Cdd:COG1119 78 KRIGLVspalqlrFPRDE------TVLDVVLsgfFDSIGLYREpTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489043565 148 ALAGILVAEPKILLLDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHDKE 196
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDlgarELLLALLDKLAAEGAPTLVLVTHHVE 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-202 |
1.40e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.88 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISlkNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpfrRD 80
Cdd:PRK10851 1 MSIEIA--NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQESNdCFICPSVLDDVIFSL--LSRGKDKDGS--RAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAE 156
Cdd:PRK10851 76 VGFVFQHYA-LFRHMTVFDNIAFGLtvLPRRERPNAAaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489043565 157 PKILLLDEPTTALDA----DMQRRIAAILKSLDVTQIIVSHDKEFISDVA 202
Cdd:PRK10851 155 PQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVA 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-203 |
1.50e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.99 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNV--CAKIGERTLfENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFR 78
Cdd:PRK13647 1 MDNIIEVEDLhfRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 RDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPK 158
Cdd:PRK13647 79 SKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 159 ILLLDEPTTALDADMQRRIAAILKSLD---VTQIIVSHDKEFISDVAS 203
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHnqgKTVIVATHDVDLAAEWAD 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-202 |
3.42e-31 |
|
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: 114.18 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYkpFRRDVGYL 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQEsndcFICP---SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:COG4555 80 PDE----RGLYdrlTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 162 LDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVA 202
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALC 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-194 |
3.77e-31 |
|
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: 113.43 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLnATHKDKI-ALIGPNGCGKSTLLEIMAGL-----KSPCGGHIELFHHKISNLDEY-KPF 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISL-DIPKGEItALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 78 RRDVGYLFQESNdcficP---SVLDDVIFSLLSRG-KDKDGSRAKAEKILRELEIW-HLKDEI-VFNLSGGEKKLVALAG 151
Cdd:cd03260 80 RRRVGMVFQKPN-----PfpgSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWdEVKDRLhALGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 152 ILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSHD 194
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-201 |
1.02e-30 |
|
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: 118.40 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERT--LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVG 82
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS-LRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQES---NDcficpSVLDDVIFSllsrgkDKDGSRAKAEKILRELEIWhlkDEIV--------------FNLSGGEKK 145
Cdd:COG2274 553 VVLQDVflfSG-----TIRENITLG------DPDATDEEIIEAARLAGLH---DFIEalpmgydtvvgeggSNLSGGQRQ 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489043565 146 LVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSHDKEFISDV 201
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLA 676
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-215 |
1.29e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfHHKISnldeykpfrrdVGYL 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNDcficpsvLDD--VIFSLLSRGKDKDG-------------SRAKAEKILReleiwhlkdeivfNLSGGEKKLVAL 149
Cdd:COG0488 384 DQHQEE-------LDPdkTVLDELRDGAPGGTeqevrgylgrflfSGDDAFKPVG-------------VLSGGEKARLAL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 150 AGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVASAMYRLTKSGLEP 215
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-195 |
1.66e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHI-----ELFHHKISNldeykpfrRDV 81
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgeDVTHRSIQQ--------RDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQeSNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:PRK11432 81 CMVFQ-SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 162 LDEPTTALDADMQR----RIAAILKSLDVTQIIVSHDK 195
Cdd:PRK11432 160 FDEPLSNLDANLRRsmreKIRELQQQFNITSLYVTHDQ 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-196 |
5.79e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.89 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 2 SCTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPFRRDV 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP---AENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQeSNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:PRK09452 89 NTVFQ-SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 489043565 162 LDEPTTALDA----DMQRRIAAILKSLDVTQIIVSHDKE 196
Cdd:PRK09452 168 LDESLSALDYklrkQMQNELKALQRKLGITFVFVTHDQE 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-193 |
6.27e-30 |
|
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: 110.71 E-value: 6.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYL 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNdCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:cd03218 81 PQEAS-IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 165 PTTALD----ADMQrRIAAILKSLDVTQIIVSH 193
Cdd:cd03218 160 PFAGVDpiavQDIQ-KIIKILKDRGIGVLITDH 191
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-194 |
2.03e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.71 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERT-LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHKisNLDEYKP----FRR 79
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGK--PIDYSRKglmkLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 80 DVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKI 159
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 489043565 160 LLLDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHD 194
Cdd:PRK13636 163 LVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-212 |
2.62e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFE-----NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD---EYKP 76
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 FRRDVGYLFQESNDCFICPSVLDDVIFsllsrGKDKDG-SRAKAEKILRE-LEIWHLKDEIV----FNLSGGEKKLVALA 150
Cdd:PRK13649 83 IRKKVGLVFQFPESQLFEETVLKDVAF-----GPQNFGvSQEEAEALAREkLALVGISESLFeknpFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSLD---VTQIIVSHDKEFISDVASAMY-----RLTKSG 212
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHqsgMTIVLVTHLMDDVANYADFVYvlekgKLVLSG 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-194 |
3.72e-29 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 108.68 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCT----ISLKNVCAKIGER----TLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD 72
Cdd:COG4181 1 MSSSsapiIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 73 E--YKPFRRD-VGYLFQEsndcF-ICPS--VLDDVIFSLLSRGkDKDgSRAKAEKILRELEIWHLKDEIVFNLSGGEKKL 146
Cdd:COG4181 81 EdaRARLRARhVGFVFQS----FqLLPTltALENVMLPLELAG-RRD-ARARARALLERVGLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489043565 147 VALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLD----VTQIIVSHD 194
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrergTTLVLVTHD 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-194 |
5.61e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 108.71 E-value: 5.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHkisNLDEYKPF----RR 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR---PLADWSPAelarRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 80 DVgyLFQESNDCFicP-SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILV---- 154
Cdd:PRK13548 79 AV--LPQHSSLSF--PfTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489043565 155 --AEPKILLLDEPTTALDADMQRRIAAILKSLDVTQ----IIVSHD 194
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglavIVVLHD 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-195 |
6.31e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.89 E-value: 6.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGhiELFhhkISN--LDEYKPFRRDVG 82
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG--DLF---IGEkrMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQeSNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:PRK11000 79 MVFQ-SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 489043565 163 DEPTTALDA----DMQRRIAAILKSLDVTQIIVSHDK 195
Cdd:PRK11000 158 DEPLSNLDAalrvQMRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-194 |
1.81e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 111.77 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAK-IGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVG 82
Cdd:COG4988 336 SIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-ASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQESndcficpsvlddVIFS-------LLSRgkdKDGSRAKAEKILRELEIWHLK-------DEIV----FNLSGGEK 144
Cdd:COG4988 415 WVPQNP------------YLFAgtirenlRLGR---PDASDEELEAALEAAGLDEFVaalpdglDTPLgeggRGLSGGQA 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489043565 145 KLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSHD 194
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHR 531
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-205 |
4.97e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 104.97 E-value: 4.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNAThKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYkpFRRDVGYL 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK--LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQEsNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:cd03264 78 PQE-FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489043565 165 PTTALDADMQRRIAAILKSL--DVTQIIVSHDKEFISDVASAM 205
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQV 199
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-210 |
8.38e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 8.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 22 NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS-NLDEYKPFRRDVGYLFQESNDCFICPSVLDD 100
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQNPDDQLFAPTVEED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 101 VIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAI 180
Cdd:PRK13639 100 VAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKL 179
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 181 LKSLD---VTQIIVSHDKEFISDVASAMYRLTK 210
Cdd:PRK13639 180 LYDLNkegITIIISTHDVDLVPVYADKVYVMSD 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-193 |
9.45e-28 |
|
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: 104.59 E-value: 9.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 21 ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPF--RRDVGYLFQES---------N 89
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PAdlRRNIGYVPQDVtlfygtlrdN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 90 DCFICPSVLDDVIFSLLSRG-------KDKDGSrakaekilrELEIwhlkDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03245 98 ITLGAPLADDERILRAAELAgvtdfvnKHPNGL---------DLQI----GERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 163 DEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLlgDKTLIIITH 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-196 |
1.71e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.09 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK--PFR-RDVGYLFQESndcFICPSV--LDDVIFSLLS 107
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraKLRaKHVGFVFQSF---MLIPTLnaLENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 108 RGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLD-- 185
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNre 195
|
170
....*....|...
gi 489043565 186 --VTQIIVSHDKE 196
Cdd:PRK10584 196 hgTTLILVTHDLQ 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-203 |
1.94e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.40 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGhiELFHHKISNLD---EYKPFRRDV 81
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG--DLIVDGLKVNDpkvDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQESNdCFICPSVLDDVIFS-LLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKIL 160
Cdd:PRK09493 80 GMVFQQFY-LFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489043565 161 LLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVAS 203
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVAS 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-199 |
2.61e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 102.29 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIG--ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVG 82
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQesndcficpsvlDDVIFSllsrgkdkdGSraKAEKIlreleiwhlkdeivfnLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03246 80 YLPQ------------DDELFS---------GS--IAENI----------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489043565 163 DEPTTALDADMQRRIAAILKSLD---VTQIIVSHDKEFIS 199
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKaagATRIVIAHRPETLA 160
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-194 |
3.00e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.04 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHkisNLDEYKP----FRRD 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR---PLAAWSPwelaRRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VgyLFQESNDCFicP-SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILV----- 154
Cdd:COG4559 79 V--LPQHSSLAF--PfTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 155 --AEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHD 194
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHD 199
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-196 |
3.58e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 104.30 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAK--IGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS--NLDEykpFRRD 80
Cdd:PRK13632 8 IKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKE---IRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQESNDCFICPSVLDDVIFSLlsrgKDKDGSRAKAEKILRELE-----IWHLKDEiVFNLSGGEKKLVALAGILVA 155
Cdd:PRK13632 85 IGIIFQNPDNQFIGATVEDDIAFGL----ENKKVPPKKMKDIIDDLAkkvgmEDYLDKE-PQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 156 EPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKE 196
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHDMD 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-204 |
4.19e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.56 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 6 SLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSP---CGGHIELFHHKISNLdeyKPFRRDVG 82
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL---PAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQesndcficpsvlDDVIFSLLS----------RGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGI 152
Cdd:COG4136 80 ILFQ------------DDLLFPHLSvgenlafalpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 153 LVAEPKILLLDEPTTALDADM-------------QRRIAAILksldvtqiiVSHDKEfisDVASA 204
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAALraqfrefvfeqirQRGIPALL---------VTHDEE---DAPAA 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-203 |
4.65e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.91 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLfeNLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHKisNLDEYKPFRRDVGYL 84
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI-LWNGQ--DLTALPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNdCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:COG3840 77 FQENN-LFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489043565 165 PTTALD----ADMQRRIAAILKSLDVTQIIVSHDKEFISDVAS 203
Cdd:COG3840 156 PFSALDpalrQEMLDLVDELCRERGLTVLMVTHDPEDAARIAD 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-194 |
9.62e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 101.81 E-value: 9.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCaKIGERTLF---ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIsnLDEYKPFRRDV 81
Cdd:cd03263 1 LQIRNLT-KTYKKGTKpavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYlfqesndcfiCPSvlDDVIFSLLS-----------RGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALA 150
Cdd:cd03263 78 GY----------CPQ--FDALFDELTvrehlrfyarlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSHD 194
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVrkGRSIILTTHS 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-203 |
1.04e-26 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 102.27 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGER----TLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK--PFR 78
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 RDVGYLFQESNdCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPK 158
Cdd:cd03258 82 RRIGMIFQHFN-LLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489043565 159 ILLLDEPTTALDADMQRRIAAILK----SLDVTQIIVSHDKEFISDVAS 203
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICD 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-210 |
2.19e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.89 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFEnLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHI---ELFHHKISNLDEYKPFRRDVGYLFQESNDC 91
Cdd:PRK13643 18 ASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 92 FICPSVLDDVIFSLLSRGKDKDgsraKAEKILRE-LEIWHLKDEI----VFNLSGGEKKLVALAGILVAEPKILLLDEPT 166
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKE----KAEKIAAEkLEMVGLADEFweksPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 167 TALDADMQRRIAAILKSLDVTQ---IIVSHDKEFISDVASAMYRLTK 210
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGqtvVLVTHLMDDVADYADYVYLLEK 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-200 |
5.91e-26 |
|
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: 99.79 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 22 NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK-PF-RRDVGYLFQESNdcfICP--SV 97
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAiPYlRRKIGVVFQDFR---LLPdrNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 98 LDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRI 177
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180
....*....|....*....|....*.
gi 489043565 178 AAILKSLD---VTQIIVSHDKEFISD 200
Cdd:cd03292 176 MNLLKKINkagTTVVVATHAKELVDT 201
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-194 |
7.62e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.52 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdeykpfRRDVGYL 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA------REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNdcfICP--SVLDDVIFSLlsRGKdkdgSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:PRK11247 87 FQDAR---LLPwkKVIDNVGLGL--KGQ----WRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 489043565 163 DEPTTALDA----DMQRRIAAILKSLDVTQIIVSHD 194
Cdd:PRK11247 158 DEPLGALDAltriEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-194 |
7.97e-26 |
|
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: 102.49 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIE-----LFH-HKISNLdeyKPFRRDVGYLFQESNdCFicP--SVLDDVIFSL 105
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLQDsARGIFL---PPHRRRIGYVFQEAR-LF--PhlSVRGNLLYGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 106 lsRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALdaDMQRRiAAIL---- 181
Cdd:COG4148 103 --KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL--DLARK-AEILpyle 177
|
170
....*....|....*.
gi 489043565 182 ---KSLDVTQIIVSHD 194
Cdd:COG4148 178 rlrDELDIPILYVSHS 193
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-199 |
8.17e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.79 E-value: 8.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISnldEYKP--FRRDVGYL 84
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS---TLKPeiYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQesNDCFICPSVLDDVIFSLLSRGKDKDgsrakAEKILRELEIWHLKDEI----VFNLSGGEKKLVALAGILVAEPKIL 160
Cdd:PRK10247 87 AQ--TPTLFGDTVYDNLIFPWQIRNQQPD-----PAIFLDDLERFALPDTIltknIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489043565 161 LLDEPTTALDADMQRRIAAILKSLDVTQII----VSHDKEFIS 199
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIavlwVTHDKDEIN 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-196 |
1.14e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 21 ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdeyKPFRRDVGYLFQeSNDCFICPSVLDD 100
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV---PPYQRPINMMFQ-SYALFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 101 VIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDAD----MQRR 176
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLE 191
|
170 180
....*....|....*....|
gi 489043565 177 IAAILKSLDVTQIIVSHDKE 196
Cdd:PRK11607 192 VVDILERVGVTCVMVTHDQE 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-213 |
1.82e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFE-----NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS------NLd 72
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEkkgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 73 eyKPFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELeiwHLKDEIV----FNLSGGEKKLVA 148
Cdd:PRK13641 81 --KKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV---GLSEDLIskspFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489043565 149 LAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDV---TQIIVSHDKEFISDVASAMYRLTKSGL 213
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-171 |
2.10e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.55 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MScTISLKNVCA----KIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEykp 76
Cdd:COG4525 1 MS-MLTVRHVSVrypgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 frrDVGYLFQesNDCFIcP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILV 154
Cdd:COG4525 77 ---DRGVVFQ--KDALL-PwlNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170
....*....|....*..
gi 489043565 155 AEPKILLLDEPTTALDA 171
Cdd:COG4525 151 ADPRFLLMDEPFGALDA 167
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-178 |
2.24e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.95 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGY 83
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQEsndcficPSvlddvIFSLLS-----------RGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGI 152
Cdd:COG1137 83 LPQE-------AS-----IFRKLTvednilavlelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190
....*....|....*....|....*....|
gi 489043565 153 LVAEPKILLLDEPTTALD----ADMQRRIA 178
Cdd:COG1137 151 LATNPKFILLDEPFAGVDpiavADIQKIIR 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-204 |
2.95e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.32 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDK 112
Cdd:PRK13635 36 VAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 113 DGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQ 188
Cdd:PRK13635 115 EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeqkGITV 194
|
170
....*....|....*.
gi 489043565 189 IIVSHDkefISDVASA 204
Cdd:PRK13635 195 LSITHD---LDEAAQA 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-193 |
3.30e-25 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 98.50 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGY 83
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdCFICPSVLDDVIFSLLSRGK-DKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:TIGR04406 81 LPQEAS-IFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 489043565 163 DEPTTALD----ADMQRRIaAILKSLDVTQIIVSH 193
Cdd:TIGR04406 160 DEPFAGVDpiavGDIKKII-KHLKERGIGVLITDH 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-193 |
4.32e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEI---MAGLKSPCG--GHIELFHHKIsnldeYKP--- 76
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPEVTitGSIVYNGHNI-----YSPrtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 ---FRRDVGYLFQESNdcficP---SVLDDVIFSLLSRG-KDKDGSRAKAEKILRELEIW-HLKDEI---VFNLSGGEKK 145
Cdd:PRK14239 81 tvdLRKEIGMVFQQPN-----PfpmSIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIWdEVKDRLhdsALGLSGGQQQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489043565 146 LVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTR 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-196 |
5.84e-25 |
|
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: 97.44 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIsnLDEYKPFRRDVGYL 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQEsndcficPSVLDD-------VIFSLLSrGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEP 157
Cdd:cd03265 79 FQD-------LSVDDEltgwenlYIHARLY-GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489043565 158 KILLLDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHDKE 196
Cdd:cd03265 151 EVLFLDEPTIGLDpqtrAHVWEYIEKLKEEFGMTILLTTHYME 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-202 |
7.53e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.90 E-value: 7.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MScTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIsnlDEYKPF--- 77
Cdd:PRK11264 1 MS-AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI---DTARSLsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 78 -------RRDVGYLFQESNdCFICPSVLDDVIFS-LLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVAL 149
Cdd:PRK11264 77 kglirqlRQHVGFVFQNFN-LFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 150 AGILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVA 202
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVA 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
34-194 |
8.77e-25 |
|
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: 99.42 E-value: 8.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELfHHKISNLDEYK----PFRRDVGYLFQESNdCFICPSVLDDVIFSL-LSR 108
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVL-NGRTLFDSRKGiflpPEKRRIGYVFQEAR-LFPHLSVRGNLRYGMkRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 109 GKDKdgsRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL---- 184
Cdd:TIGR02142 105 PSER---RISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLhaef 181
|
170
....*....|
gi 489043565 185 DVTQIIVSHD 194
Cdd:TIGR02142 182 GIPILYVSHS 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-208 |
2.17e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.00 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 19 LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHKisNLDEYK----PFRRDVGYLFQESNDCFIC 94
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGK--PLDYSKrgllALRQQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 95 PSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQ 174
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 175 RRIAAILKSLdVTQ----IIVSHDKEFISDVASAMYRL 208
Cdd:PRK13638 173 TQMIAIIRRI-VAQgnhvIISSHDIDLIYEISDAVYVL 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-202 |
2.48e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.40 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNL---NATHKDK--IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS---NLDEYKP 76
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALydvNVSIPSGsyVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 FRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELeiwHLKDEIV----FNLSGGEKKLVALAGI 152
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELV---GLPEELLarspFELSGGQMRRVAIAGV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489043565 153 LVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEfisDVA 202
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkekGLTTVLVTHSME---DAA 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
33-194 |
2.67e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFH------HKISNLDEY-----------------KPFRRDVGYLFQESN 89
Cdd:PRK13651 36 IAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFkdeknkKKTKEKEKVleklviqktrfkkikkiKEIRRRVGVVFQFAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 90 DCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILrelEIWHLKDEIV----FNLSGGEKKLVALAGILVAEPKILLLDEP 165
Cdd:PRK13651 116 YQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYI---ELVGLDESYLqrspFELSGGQKRRVALAGILAMEPDFLVFDEP 192
|
170 180 190
....*....|....*....|....*....|..
gi 489043565 166 TTALDADMQRRIAAILKSLDV---TQIIVSHD 194
Cdd:PRK13651 193 TAGLDPQGVKEILEIFDNLNKqgkTIILVTHD 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-193 |
3.10e-24 |
|
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: 93.76 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGE-RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLkSPCG-GHIElfhhkisnldeyKPFRRDVG 82
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL-WPWGsGRIG------------MPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQesndcficpsvlddvifsllsRGKDKDGSrakaekiLRELEIWHLKDEivfnLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03223 68 FLPQ---------------------RPYLPLGT-------LREQLIYPWDDV----LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|.
gi 489043565 163 DEPTTALDADMQRRIAAILKSLDVTQIIVSH 193
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-198 |
3.34e-24 |
|
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: 95.71 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNL--DEYKPFRRDVGYLFQESNdcf 92
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgKALRQLRRQIGMIFQQFN--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 93 ICP--SVLDDVIF----------SLLSRGKDKDgsRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKIL 160
Cdd:cd03256 89 LIErlSVLENVLSgrlgrrstwrSLFGLFPKEE--KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489043565 161 LLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFI 198
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRInreeGITVIVSLHQVDLA 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-194 |
5.80e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 98.68 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKI--GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDV 81
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE-DDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQESndcficpsvlddVIFS-------LLSRGkdkDGSRAKAEKILRELEIWHLKDEIV-----------FNLSGGE 143
Cdd:COG4987 412 AVVPQRP------------HLFDttlrenlRLARP---DATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489043565 144 KKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSHD 194
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHR 529
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-196 |
1.56e-23 |
|
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: 93.33 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 23 LNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPFRRDVGYLFQEsNDCFICPSVLDDVI 102
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQE-NNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 103 FSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALD----ADMQRRIA 178
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVL 172
|
170
....*....|....*...
gi 489043565 179 AILKSLDVTQIIVSHDKE 196
Cdd:cd03298 173 DLHAETKMTVLMVTHQPE 190
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
34-209 |
2.06e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHkisnldeykpfrRDVGYLFQES--NDCFICpSVLDDVIFSL-----L 106
Cdd:NF040873 22 AVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG------------ARVAYVPQRSevPDSLPL-TVRDLVAMGRwarrgL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 107 SRGKDKDgSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL-- 184
Cdd:NF040873 89 WRRLTRD-DRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEha 167
|
170 180
....*....|....*....|....*.
gi 489043565 185 -DVTQIIVSHDKEfisDVASAMYRLT 209
Cdd:NF040873 168 rGATVVVVTHDLE---LVRRADPCVL 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
33-209 |
2.11e-23 |
|
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: 93.27 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHKISNLD--EYKPF------RRDVGYLFQesndcF--ICPSV--LDD 100
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGNYLPDSGSI-LVRHDGGWVDlaQASPReilalrRRTIGYVSQ-----FlrVIPRVsaLDV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 101 VIFSLLSRGKDKDGSRAKAEKILRELEI----WHLKdEIVFnlSGGEKKLVALAGILVAEPKILLLDEPTTALDAdmQRR 176
Cdd:COG4778 114 VAEPLLERGVDREEARARARELLARLNLperlWDLP-PATF--SGGEQQRVNIARGFIADPPLLLLDEPTASLDA--ANR 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 177 IAAI-----LKSLDVTQIIVSHDKEFISDVASAMYRLT 209
Cdd:COG4778 189 AVVVelieeAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-194 |
5.68e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 9 NVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD--EYKPFRRDVGYLFQ 86
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 87 ES----NDCFICPSVLDDVIFSLLSRgkDKDGSRAKAEKILRELEiwhLKDEIV----FNLSGGEKKLVALAGILVAEPK 158
Cdd:PRK10419 97 DSisavNPRKTVREIIREPLRHLLSL--DKAERLARASEMLRAVD---LDDSVLdkrpPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489043565 159 ILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHD 194
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLqqqfGTACLFITHD 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-188 |
9.66e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 92.74 E-value: 9.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRdVGYLFQESNdcfiC 94
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNAT----T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 95 PSvlDDVIFSLLSRG------------KDKDGSRAKAekiLRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:PRK10253 93 PG--DITVQELVARGryphqplftrwrKEDEEAVTKA---MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180
....*....|....*....|....*.
gi 489043565 163 DEPTTALDADMQRRIAAILKSLDVTQ 188
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREK 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-193 |
9.78e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 95.23 E-value: 9.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVC-AKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVG 82
Cdd:COG1132 339 EIEFENVSfSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT-LESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQES---NDcficpSVLDDVIFSllsrgkDKDGSRAKAEKILRELEIWH----LK---DEIV----FNLSGGEKKLVA 148
Cdd:COG1132 418 VVPQDTflfSG-----TIRENIRYG------RPDATDEEVEEAAKAAQAHEfieaLPdgyDTVVgergVNLSGGQRQRIA 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 149 LAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAH 533
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-202 |
9.78e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 9.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 16 ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS----NLDEykpFRRDVGYLFQESNDC 91
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSD---IRKKVGLVFQYPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 92 FICPSVLDDVIFSLLSRGKDKD--GSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTAL 169
Cdd:PRK13637 96 LFEETIEKDIAFGPINLGLSEEeiENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 489043565 170 DA----DMQRRIAAILKSLDVTQIIVSHDKEFISDVA 202
Cdd:PRK13637 176 DPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLA 212
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-183 |
1.07e-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: 90.88 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNL-DEYKpfrRDVGY 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPH---ENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdcfICP--SVLDDVIF-SLLSRGKDKDGSRAKAEKILRELEiwhlkDEIVFNLSGGEKKLVALAGILVAEPKIL 160
Cdd:TIGR01189 78 LGHLPG---LKPelSALENLHFwAAIHGGAQRTIEDALAAVGLTGFE-----DLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180
....*....|....*....|...
gi 489043565 161 LLDEPTTALDADMQRRIAAILKS 183
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRA 172
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
34-194 |
1.56e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.12 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHKISNLDEYKPFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKD 113
Cdd:PRK13648 39 SIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 114 GSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQI 189
Cdd:PRK13648 118 EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITII 197
|
....*
gi 489043565 190 IVSHD 194
Cdd:PRK13648 198 SITHD 202
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-206 |
1.63e-22 |
|
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: 90.96 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNAtHKDKI-ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGY 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTV-PEGEIvALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdcficpsvlddvIFSLLS---------RGKDKDGSRAKAEKIL----RELEIWHLKdeiVFNLSGGEKKLVALA 150
Cdd:cd03224 80 VPEGRR------------IFPELTveenlllgaYARRRAKRKARLERVYelfpRLKERRKQL---AGTLSGGEQQMLAIA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVASAMY 206
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELrdeGVTILLVEQNARFALEIADRAY 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-194 |
1.89e-22 |
|
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: 91.21 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGE-RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVGY 83
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE-LRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdCFICPSVLDDV--IFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:cd03295 80 VIQQIG-LFPHMTVEENIalVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 489043565 162 LDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHD 194
Cdd:cd03295 159 MDEPFGALDpitrDQLQEEFKRLQQELGKTIVFVTHD 195
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-213 |
3.01e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.72 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGY 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdCFICPSVLDDVIFSLLSRgKD--KDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:PRK10895 83 LPQEAS-IFRRLSVYDNLMAVLQIR-DDlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 162 LDEPTTALDA----DMqRRIAAILKSLDVTQIIVSHDKEFISDVASAMYRLTKSGL 213
Cdd:PRK10895 161 LDEPFAGVDPisviDI-KRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-196 |
4.46e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.53 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpfrrdvGYL 84
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQesNDCFIcP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:PRK11248 76 FQ--NEGLL-PwrNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 163 DEPTTALDA----DMQRRIAAILKSLDVTQIIVSHDKE 196
Cdd:PRK11248 153 DEPFGALDAftreQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-194 |
4.68e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.46 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGY 83
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-RQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQEsndcFICP---SVLDDVIF------SLLSRGKDKDgsRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILV 154
Cdd:PRK11231 81 LPQH----HLTPegiTVRELVAYgrspwlSLWGRLSAED--NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489043565 155 AEPKILLLDEPTTALDADMQRRIAAILKSLDV---TQIIVSHD 194
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD 197
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-194 |
9.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.18 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKIG---ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNlDEYKPF 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE-ENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 78 RRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEP 157
Cdd:PRK13650 80 RHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489043565 158 KILLLDEPTTALDA----DMQRRIAAILKSLDVTQIIVSHD 194
Cdd:PRK13650 160 KIIILDEATSMLDPegrlELIKTIKGIRDDYQMTVISITHD 200
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-193 |
1.08e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.33 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNAtHKDKI-ALIGPNGCGKSTLL-------EIMAGLKspCGGHIELFhhkisNLDEYKP 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDI-PENKVtALIGPSGCGKSTLLrclnrmnDLIPGAR--VEGEILLD-----GEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 ------FRRDVGYLFQESNdcficP---SVLDDVIFSLLSRG-KDKDGSRAKAEKILRELEIW-HLKD---EIVFNLSGG 142
Cdd:COG1117 84 dvdvveLRRRVGMVFQKPN-----PfpkSIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALWdEVKDrlkKSALGLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489043565 143 EKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELkkDYTIVIVTH 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
19-196 |
1.33e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 19 LFENL----NLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELF---HHKISnldeykPFRRDVGYLFQESNdc 91
Cdd:PRK10771 10 LYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdHTTTP------PSRRPVSMLFQENN-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 92 ficpsvlddvIFSLLSRG-----------KDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKIL 160
Cdd:PRK10771 82 ----------LFSHLTVAqniglglnpglKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489043565 161 LLDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHDKE 196
Cdd:PRK10771 152 LLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLE 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-181 |
2.35e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.62 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIsnldEYKPFRRDVGY 83
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----DDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LfQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKI-LRELEiwHLKdeivF-NLSGGEKKLVALAGILVAEPKILL 161
Cdd:PRK13539 78 L-GHRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAVgLAPLA--HLP----FgYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180
....*....|....*....|
gi 489043565 162 LDEPTTALDADMQRRIAAIL 181
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELI 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-203 |
2.66e-21 |
|
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: 91.15 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhkisnLDEYKpfrrdVGYLFQE-----SN 89
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-------QPGIK-----VGYLPQEpqldpTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 90 DCFicPSVLDDV--IFSLLSR-----------GKDKDG---SRAKAEKILRELEIWHL---------------KDEIVFN 138
Cdd:TIGR03719 84 TVR--ENVEEGVaeIKDALDRfneisakyaepDADFDKlaaEQAELQEIIDAADAWDLdsqleiamdalrcppWDADVTK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 139 LSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVAS 203
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-208 |
3.56e-21 |
|
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: 87.77 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 22 NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIelfhhKISNLDEYK---PFRRDVGYLFQESNDCFICPSVL 98
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGLVPWKrrkKFLRRIGVVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 99 DDviFSLLSRGKDKDGSRAKA--EKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRR 176
Cdd:cd03267 114 DS--FYLLAAIYDLPPARFKKrlDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 489043565 177 IAAILKSL----DVTQIIVSHDkefISDVASAMYRL 208
Cdd:cd03267 192 IRNFLKEYnrerGTTVLLTSHY---MKDIEALARRV 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-199 |
4.23e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 12 AKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK-PF-RRDVGYLFQESN 89
Cdd:PRK10908 10 AYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvPFlRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 90 dCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTAL 169
Cdd:PRK10908 90 -LLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 170 DADMQRRIAAILKSLD---VTQIIVSHDKEFIS 199
Cdd:PRK10908 169 DDALSEGILRLFEEFNrvgVTVLMATHDIGLIS 201
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-193 |
4.27e-21 |
|
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: 87.28 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 22 NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGYLFQESndcFICP-SVLDD 100
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR-KSLRSMIGVVLQDT---FLFSgTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 101 VIFSllsrgkdkdGSRAKAEKILRELEIWHLKDEIVF--------------NLSGGEKKLVALAGILVAEPKILLLDEPT 166
Cdd:cd03254 97 IRLG---------RPNATDEEVIEAAKEAGAHDFIMKlpngydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180
....*....|....*....|....*....
gi 489043565 167 TALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:cd03254 168 SNIDTETEKLIQEALEKLmkGRTSIIIAH 196
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-193 |
5.97e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 90.18 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 17 RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVGYLFQESndcFI-CP 95
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT-LRQFINYLPQEP---YIfSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 SVLDDVIFsllsrgkdkdGSRAKA--EKILRELEIWHLKDEI--------------VFNLSGGEKKLVALAGILVAEPKI 159
Cdd:TIGR01193 563 SILENLLL----------GAKENVsqDEIWAACEIAEIKDDIenmplgyqtelseeGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190
....*....|....*....|....*....|....*
gi 489043565 160 LLLDEPTTALDADMQRRIAA-ILKSLDVTQIIVSH 193
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNnLLNLQDKTIIFVAH 667
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-212 |
1.09e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.46 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 9 NVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGH-----IELFHHKISNLDEYKPFRRDVGY 83
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNDCFIcpSVLDDVIFSLLS-RGKDKDGSRAKAEKILRELEIWH-LKDEIV---FNLSGGEKKLVALAGILVAEPK 158
Cdd:PRK14271 106 LFQRPNPFPM--SIMDNVLAGVRAhKLVPRKEFRGVAQARLTEVGLWDaVKDRLSdspFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489043565 159 ILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSHD---KEFISDVASAMY--RLTKSG 212
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHNlaqAARISDRAALFFdgRLVEEG 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-193 |
1.54e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYLFQESNdcfICP--SVLDDvIF--SLLSRG 109
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQELN---LVPnlSVAEN-IFlgREPRRG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 110 K--DKDGSRAKAEKILRELEIwHLK-DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTAL-DADMQR--RIAAILKS 183
Cdd:COG1129 110 GliDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLtEREVERlfRIIRRLKA 188
|
170
....*....|
gi 489043565 184 LDVTQIIVSH 193
Cdd:COG1129 189 QGVAIIYISH 198
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-194 |
1.89e-20 |
|
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: 86.40 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 13 KIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD--EYKPFRRDVGYLFQESND 90
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkQRRAFRRDVQLVFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 91 CFICPSVLDDVIFSLLSRGKDKDGSRAKAeKILRELEIWHLKDEIV----FNLSGGEKKLVALAGILVAEPKILLLDEPT 166
Cdd:TIGR02769 100 AVNPRMTVRQIIGEPLRHLTSLDESEQKA-RIAELLDMVGLRSEDAdklpRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190
....*....|....*....|....*....|..
gi 489043565 167 TALDADMQRRIAAILKSLD----VTQIIVSHD 194
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQqafgTAYLFITHD 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-202 |
2.16e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 88.64 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhkisnLDEYKpfrrdVGYLFQEsndcfic 94
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------APGIK-----VGYLPQE------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 95 P------SVLDDV------IFSLLSR--------GKDKDGSRAKAEK------ILRELEIWHL---------------KD 133
Cdd:PRK11819 79 PqldpekTVRENVeegvaeVKAALDRfneiyaayAEPDADFDALAAEqgelqeIIDAADAWDLdsqleiamdalrcppWD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489043565 134 EIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDAD----MQRRiaaiLKSLDVTQIIVSHDKEFISDVA 202
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLEQF----LHDYPGTVVAVTHDRYFLDNVA 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
34-202 |
2.25e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.37 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIEL----FHHKISNlDEYKPFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRG 109
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVTVdditITHKTKD-KYIRPVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 110 KDKDGSRAKAEKILREL----EIWHLKDeivFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLD 185
Cdd:PRK13646 116 MNLDEVKNYAHRLLMDLgfsrDVMSQSP---FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQ 192
|
170 180
....*....|....*....|.
gi 489043565 186 VTQ----IIVSHDkefISDVA 202
Cdd:PRK13646 193 TDEnktiILVSHD---MNEVA 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-202 |
2.58e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 14 IGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGL------KSPCGGHIELFHHKISNLDEYKpFRRDVGYLFQE 87
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIK-LRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 88 SNDcFICPSVLDDVIFSLLSRG-KDKDGSRAKAEKILRELEIW-HLKDEI---VFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:PRK14246 99 PNP-FPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLWkEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489043565 163 DEPTTALDADMQRRIAAILKSL--DVTQIIVSHDKEFISDVA 202
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVA 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
34-194 |
2.70e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPcgghIELFHHKIS------NLDEYKPFRRDVGYLFQESNDCFICPSVLDDVIFSLLS 107
Cdd:PRK13640 37 ALIGHNGSGKSTISKLINGLLLP----DDNPNSKITvdgitlTAKTVWDIREKVGIVFQNPDNQFVGATVGDDVAFGLEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 108 RGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--- 184
Cdd:PRK13640 113 RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkk 192
|
170
....*....|.
gi 489043565 185 -DVTQIIVSHD 194
Cdd:PRK13640 193 nNLTVISITHD 203
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-200 |
2.75e-20 |
|
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: 85.21 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 21 ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIsnlDEYKPFRRDVgylFQESNdcfICP--SVL 98
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRMVV---FQNYS---LLPwlTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 99 DDVifSLLSRGKDKDGSRAKAEKILRE----LEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDA--- 171
Cdd:TIGR01184 73 ENI--ALAVDRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltr 150
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 172 -DMQRRIAAILKSLDVTQIIVSHDKE---FISD 200
Cdd:TIGR01184 151 gNLQEELMQIWEEHRVTVLMVTHDVDealLLSD 183
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-184 |
3.09e-20 |
|
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: 85.03 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 6 SLKNVCAKIGERTLFENLNLNAtHKDKI-ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYL 84
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEV-EEGEIvALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNdcficpsvlddvIFSLLS----------RGKDKDGSRAKAEKI------LRELeiwhlKDEIVFNLSGGEKKLVA 148
Cdd:COG0410 84 PEGRR------------IFPSLTveenlllgayARRDRAEVRADLERVyelfprLKER-----RRQRAGTLSGGEQQMLA 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 489043565 149 LAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-171 |
3.45e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.02 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAK----IGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGL---KSPCGGHIeLFHHKISNLDEykp 76
Cdd:cd03234 3 VLPWWDVGLKaknwNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQI-LFNGQPRKPDQ--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 FRRDVGYLFQesNDCFI-CPSVLDDVIFSLLSRG--KDKDGSRAK--AEKILRELEIWHLKDEIVFNLSGGEKKLVALAG 151
Cdd:cd03234 79 FQKCVAYVRQ--DDILLpGLTVRETLTYTAILRLprKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAV 156
|
170 180
....*....|....*....|
gi 489043565 152 ILVAEPKILLLDEPTTALDA 171
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDS 176
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-194 |
3.90e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 87.80 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 20 FENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGYLFQESNdcFICPSVLD 99
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ-DEVRRRVSVCAQDAH--LFDTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 100 DVifsLLSRGkdkDGSRAKAEKILRE--LEIW--HLKD-------EIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTA 168
Cdd:TIGR02868 428 NL---RLARP---DATDEELWAALERvgLADWlrALPDgldtvlgEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180
....*....|....*....|....*...
gi 489043565 169 LDADMQRR-IAAILKSLD-VTQIIVSHD 194
Cdd:TIGR02868 502 LDAETADElLEDLLAALSgRTVVLITHH 529
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-215 |
4.06e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFE-----NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKI----SNLDEYK 75
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 76 PFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEiwhLKDEIV----FNLSGGEKKLVALAG 151
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ---LPEDYVkrspFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 152 ILVAEPKILLLDEPTTALD---------------ADMQRRIAAILKSLD-----VTQIIVSHDKEFIS-----DVASAMY 206
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDpkgeedfinlferlnKEYKKRIIMVTHNMDqvlriADEVIVMHEGKVISigspfEIFSNQE 243
|
....*....
gi 489043565 207 RLTKSGLEP 215
Cdd:PRK13645 244 LLTKIEIDP 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-202 |
4.44e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKS----------------------------- 55
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 56 ---PCGGHIELFHHKISNLDE--YKPFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWH 130
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDFWNLSDklRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 131 LKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALD---ADM-QRRIAAILKSLDVTQIIVSHDKEFISDVA 202
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLvHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
35-194 |
4.55e-20 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 85.39 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 35 LIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD--EYKPFRR-DVGYLFQeSNDCFICPSVLDDVIFSLLSRGKD 111
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkELRELRRkKISMVFQ-SFALLPHRTVLENVAFGLEVQGVP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 112 KDGSRAKAEKILRE--LEIW--HLKDEivfnLSGGEKKLVALAGILVAEPKILLLDEPTTALD----ADMQRRIAAILKS 183
Cdd:cd03294 134 RAEREERAAEALELvgLEGWehKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAE 209
|
170
....*....|.
gi 489043565 184 LDVTQIIVSHD 194
Cdd:cd03294 210 LQKTIVFITHD 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-214 |
7.04e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.64 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHH------------KISNLDEYKPFRRDVG 82
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlKVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQESNdCFICPSVLDDVIFSLLS-RGKDKDGSRAKAEKILRELEI-WHLKDEIVFNLSGGEKKLVALAGILVAEPKIL 160
Cdd:PRK10619 96 MVFQHFN-LWSHMTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489043565 161 LLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVASAMYRLTKSGLE 214
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-198 |
8.53e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 86.93 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSP------CGGHIEL--FHHKISNLDEYKpfr 78
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQAdsgrihCGTKLEVayFDQHRAELDPEK--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 rdvgylfqesndcficpSVLDDvifslLSRGKDKDGSRAKAEKILRELE--IWHLKDEI--VFNLSGGEKKLVALAGILV 154
Cdd:PRK11147 399 -----------------TVMDN-----LAEGKQEVMVNGRPRHVLGYLQdfLFHPKRAMtpVKALSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 155 AEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFI 198
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-193 |
1.08e-19 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 83.82 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVC-AKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGY 83
Cdd:cd03253 1 IEFENVTfAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTL-DSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 ------LFQES---NDCFICPSVLDDVIFSLlsrgkdkdgsrAKAEKILRELEIWHLK-DEIV----FNLSGGEKKLVAL 149
Cdd:cd03253 80 vpqdtvLFNDTigyNIRYGRPDATDEEVIEA-----------AKAAQIHDKIMRFPDGyDTIVgergLKLSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489043565 150 AGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-196 |
1.57e-19 |
|
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: 86.19 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGYLFQESndcFIC 94
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWRDQIAWVPQHP---FLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 95 P-SVLDDVIFSllsrgkDKDGSRAKAEKILRELEIWHLKDEIVFN-----------LSGGEKKLVALAGILVAEPKILLL 162
Cdd:TIGR02857 409 AgTIAENIRLA------RPDASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190
....*....|....*....|....*....|....*.
gi 489043565 163 DEPTTALDADMQRRIAAILKSL--DVTQIIVSHDKE 196
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLA 518
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-212 |
2.32e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.19 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKS--PCGGHIELFHHKISNLDEYKPFRRDVG 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQEsndcficPSVLDDVifsllsrgkdkdgsraKAEKILRELeiwhlkDEivfNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03217 81 LAFQY-------PPEIPGV----------------KNADFLRYV------NE---GFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 163 DEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFI----SDVASAMY--RLTKSG 212
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLreeGKSVLIITHYQRLLdyikPDRVHVLYdgRIVKSG 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-194 |
4.39e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKIGERTLFENLN---LNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpF 77
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 78 RRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEP 157
Cdd:PRK13642 80 RRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489043565 158 KILLLDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHD 194
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-193 |
4.69e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.86 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 17 RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLkSPCG-GHIELfhhkisnldeykPFRRDVGYLFQESndcFICP 95
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL-WPYGsGRIAR------------PAGARVLFLPQRP---YLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 SVLDDVifsLLSRGKDKDGSRAKAEKILRELEIWHLKD--EIVFN----LSGGEKKLVALAGILVAEPKILLLDEPTTAL 169
Cdd:COG4178 440 GTLREA---LLYPATAEAFSDAELREALEAVGLGHLAErlDEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180
....*....|....*....|....*.
gi 489043565 170 DADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:COG4178 517 DEENEAALYQLLREElpGTTVISVGH 542
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-201 |
5.30e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.47 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 21 ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhKISN--LDEYKP-------FRRDVGYLFQESnDC 91
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDewVDMTKPgpdgrgrAKRYIGILHQEY-DL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 92 FICPSVLDDV-----------------IFSLLSRGKDKDgsraKAEKILRELeiwhlKDEivfnLSGGEKKLVALAGILV 154
Cdd:TIGR03269 377 YPHRTVLDNLteaiglelpdelarmkaVITLKMVGFDEE----KAEEILDKY-----PDE----LSEGERHRVALAQVLI 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489043565 155 AEPKILLLDEPTTALDADMQRRIA-AILKS---LDVTQIIVSHDKEFISDV 201
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVThSILKAreeMEQTFIIVSHDMDFVLDV 494
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-202 |
6.16e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.20 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVC----AKIGERTLFENLNLNAtHKDKI-ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK--PF 77
Cdd:COG1135 2 IELENLSktfpTKGGPVTALDDVSLTI-EKGEIfGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 78 RRDVGYLFQESNdcfICPS--VLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVA 155
Cdd:COG1135 81 RRKIGMIFQHFN---LLSSrtVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489043565 156 EPKILLLDEPTTALDADMQRRIAAILKS----LDVTQIIVSHDKEFISDVA 202
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDinreLGLTIVLITHEMDVVRRIC 208
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-193 |
6.58e-19 |
|
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: 81.82 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 16 ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVGYLFQESNdCFICp 95
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW-LRSQIGLVSQEPV-LFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 SVLDDVIFSllsrgkDKDGSRAKAEKILRELEIwHlkDEIV--------------FNLSGGEKKLVALAGILVAEPKILL 161
Cdd:cd03249 92 TIAENIRYG------KPDATDEEVEEAAKKANI-H--DFIMslpdgydtlvgergSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190
....*....|....*....|....*....|....
gi 489043565 162 LDEPTTALDADMQRRIAAILK--SLDVTQIIVSH 193
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDraMKGRTTIVIAH 196
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
34-194 |
7.06e-19 |
|
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: 82.79 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCG---GHIELFHHKISNLD--EYKPFR-RDVGYLFQES----NDCFicpSVLDDVIF 103
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSekELRKIRgREIQMIFQDPmtslNPVM---TVGDQIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 104 SLLS-RGKDKDGSRAKAEKILRELEIwHLKDEIV----FNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIA 178
Cdd:COG0444 112 PLRIhGGLSKAEARERAIELLERVGL-PDPERRLdrypHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQIL 190
|
170 180
....*....|....*....|
gi 489043565 179 AILKSL----DVTQIIVSHD 194
Cdd:COG0444 191 NLLKDLqrelGLAILFITHD 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-205 |
8.79e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 83.79 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhkisnldeyKPFRRdVGYL 84
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-----------DPNER-LGKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQesnDCFICP--SVLD----------------DVIFSLLSRgKDKDGSR-----------------AKAEKILRELEI- 128
Cdd:PRK15064 70 RQ---DQFAFEefTVLDtvimghtelwevkqerDRIYALPEM-SEEDGMKvadlevkfaemdgytaeARAGELLLGVGIp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 129 --WH--LKDEIvfnlSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVASA 204
Cdd:PRK15064 146 eeQHygLMSEV----APGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTH 221
|
.
gi 489043565 205 M 205
Cdd:PRK15064 222 M 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
33-194 |
1.19e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.58 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykPFRRDVGYLFQesnDCFICP--SVLDDVIFSLLSRGK 110
Cdd:PRK11650 33 IVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE---PADRDIAMVFQ---NYALYPhmSVRENMAYGLKIRGM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 111 DKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDA-----------DMQRRiaa 179
Cdd:PRK11650 107 PKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvqmrleiqRLHRR--- 183
|
170
....*....|....*
gi 489043565 180 ilksLDVTQIIVSHD 194
Cdd:PRK11650 184 ----LKTTSLYVTHD 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-193 |
1.37e-18 |
|
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: 80.74 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIG--ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdEYKPFRRDVG 82
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQesnDCFIcpsvLDDVIFSLLSRGKDkdgsRAKAEKILRELEIWHLKDEIV--------------FNLSGGEKKLVA 148
Cdd:cd03251 80 LVSQ---DVFL----FNDTVAENIAYGRP----GATREEVEEAARAANAHEFIMelpegydtvigergVKLSGGQRQRIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 149 LAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-211 |
1.44e-18 |
|
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: 80.02 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNaTHKDKI-ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykpfRRDVGY 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFS-VEKGEIfGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNdCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLD 163
Cdd:cd03269 75 LPEERG-LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489043565 164 EPTTALD---ADMQRRIAAILKSLDVTQIIVSHDKEFISDVASAMYRLTKS 211
Cdd:cd03269 154 EPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-202 |
1.49e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.21 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLN----ATHKDKI-ALIGPNGCGKSTLLEIMAGLKSPCGGHI---------------ELF 64
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVALNnisyTFEKNKIyFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnheLIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 65 HHKISNLDEYKPFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELeiwHLKDEIV----FNLS 140
Cdd:PRK13631 102 NPYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKM---GLDDSYLerspFGLS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 141 GGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAIL---KSLDVTQIIVSHDKEFISDVA 202
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIldaKANNKTVFVITHTMEHVLEVA 243
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-213 |
1.50e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 83.40 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIelfhhKISNldeykpfRRDVGYLFQ 86
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSE-------NANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 87 ESNDCFICPSVLDDVIfSLLSRGKDKDGS-RAKAEKILREleiwhlKDEI---VFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:PRK15064 390 DHAYDFENDLTLFDWM-SQWRQEGDDEQAvRGTLGRLLFS------QDDIkksVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489043565 163 DEPTTALDadMQRrIAAI---LKSLDVTQIIVSHDKEFISDVASAMYRLTKSGL 213
Cdd:PRK15064 463 DEPTNHMD--MES-IESLnmaLEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-204 |
1.86e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.29 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKI-----GERTL-FENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEY 74
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneeSTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 75 KPFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILV 154
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489043565 155 AEPKILLLDEPTTALDADMQRRIAAILKSLD----VTQIIVSHdkeFISDVASA 204
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNkkygITIILITH---YMEEAVEA 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-194 |
2.14e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 9 NVCAKIGERTL----FENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFH----HKISNLDEYKPFRRD 80
Cdd:PRK11629 10 NLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNgqpmSKLSSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQESNdcfICP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPK 158
Cdd:PRK11629 89 LGFIYQFHH---LLPdfTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489043565 159 ILLLDEPTTALDADMQRRIAAILKSLDVTQ----IIVSHD 194
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQgtafLVVTHD 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-193 |
3.02e-18 |
|
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: 78.51 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGE--RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeyKPFRRDVG 82
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE--KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQEsndcficPSVLDDVIFSLLSRgkdkdgsrakaekilreleiwhlkdeivfNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:cd03247 79 VLNQR-------PYLFDTTLRNNLGR-----------------------------RFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 163 DEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVlkDKTLIWITH 155
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-194 |
3.21e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIElfhhkisnldeyKPFRRD 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQESNdcficpsvLDDVI------FSLLSRG-KDKDGSRAkaekiLRELEIWHLKDEIVFNLSGGEKKLVALAGIL 153
Cdd:PRK09544 69 IGYVPQKLY--------LDTTLpltvnrFLRLRPGtKKEDILPA-----LKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 154 VAEPKILLLDEPTTALDADMQRR----IAAILKSLDVTQIIVSHD 194
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVAlydlIDQLRRELDCAVLMVSHD 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-194 |
3.76e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGY 83
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS-KAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQEsndcfiCPSVLDDVIFSLLSRGK-------DKDGS--RAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILV 154
Cdd:PRK10575 90 LPQQ------LPAAEGMTVRELVAIGRypwhgalGRFGAadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 155 AEPKILLLDEPTTALDADMQRRIAAILKSLD----VTQIIVSHD 194
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSqergLTVIAVLHD 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-195 |
4.98e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVC-----AKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpfR- 78
Cdd:COG1101 2 LELKNLSktfnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--Ra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 RDVGYLFQesnDCFI--CPS--VLDDviFSL---------LSRGKDKDgSRAKAEKILRELEIW---HLKDEiVFNLSGG 142
Cdd:COG1101 80 KYIGRVFQ---DPMMgtAPSmtIEEN--LALayrrgkrrgLRRGLTKK-RRELFRELLATLGLGlenRLDTK-VGLLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489043565 143 EKKLVALAGILVAEPKILLLDEPTTALDAdmqrRIAAILksLDVTQIIVSHDK 195
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDP----KTAALV--LELTEKIVEENN 199
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-197 |
5.69e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGL----KSPcGGHIELFHHKISN----LD 72
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSA-GSHIELLGRTVQRegrlAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 73 EYKPFRRDVGYLFQESNdCFICPSVLDDVIFSLLS-----RGKDKDGSRAKAEKILRELE---IWHLKDEIVFNLSGGEK 144
Cdd:PRK09984 80 DIRKSRANTGYIFQQFN-LVNRLSVLENVLIGALGstpfwRTCFSWFTREQKQRALQALTrvgMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489043565 145 KLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLD----VTQIIVSHDKEF 197
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndgITVVVTLHQVDY 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-215 |
7.74e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 81.37 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhkisnldeYKPFRrdVGYL 84
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------AKGIK--LGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNDcFICPsvlDDVIFSLLSRGKDKDgsrakAEKILRE-LEIWHLK----DEIVFNLSGGEKKLVALAGILVAEPKI 159
Cdd:PRK10636 381 AQHQLE-FLRA---DESPLQHLARLAPQE-----LEQKLRDyLGGFGFQgdkvTEETRRFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 160 LLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVASAMYRLTKSGLEP 215
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEP 507
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
33-194 |
8.95e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 8.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLkSPCGGHIELFHHkisNLDEYKPFR--RDVGYLFQESNDCFICPsvlddvIFSLLSRGK 110
Cdd:COG4138 25 IHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGR---PLSDWSAAElaRHRAYLSQQQSPPFAMP------VFQYLALHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 111 DKDGSRAKAEKILREL-EIWHLKDEI---VFNLSGGEKKLVALAGILV-------AEPKILLLDEPTTALDADMQrriAA 179
Cdd:COG4138 95 PAGASSEAVEQLLAQLaEALGLEDKLsrpLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQ---AA 171
|
170 180
....*....|....*....|.
gi 489043565 180 ILKSLD------VTQIIVSHD 194
Cdd:COG4138 172 LDRLLRelcqqgITVVMSSHD 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
7-184 |
1.45e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLfenlnlnathkdkIALIGPNGCGKSTLLEIMAGLKSP---CGGHIELFHHKIsnldEYKPFRRDVGY 83
Cdd:TIGR00955 41 LKNVSGVAKPGEL-------------LAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI----DAKEMRAISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQEsnDCFIcPS--VLDDVIFSL---LSRGKDKDGSRAKAEKILRELEIWHLKDEI------VFNLSGGEKKLVALAGI 152
Cdd:TIGR00955 104 VQQD--DLFI-PTltVREHLMFQAhlrMPRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASE 180
|
170 180 190
....*....|....*....|....*....|..
gi 489043565 153 LVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-202 |
1.96e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.15 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEI---MAGLKSPCG--GHIELFHHKI----SNLDEyk 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKClnrMNELESEVRveGRVEFFNQNIyerrVNLNR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 76 pFRRDVGYLFQESNdcfICP-SVLDDVIFsllsrGKDKDGSRAK------AEKILRELEIW-HLKDEI---VFNLSGGEK 144
Cdd:PRK14258 86 -LRRQVSMVHPKPN---LFPmSVYDNVAY-----GVKIVGWRPKleiddiVESALKDADLWdEIKHKIhksALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489043565 145 KLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFISDVA 202
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLS 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-194 |
1.97e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGY 83
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA-RAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNDCFIcpsvlddviFSL-----------LSR--GKDKDGSRAkAEKILRELEIWHLKDEIVFNLSGGEKKLVALA 150
Cdd:PRK09536 82 VPQDTSLSFE---------FDVrqvvemgrtphRSRfdTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHD 194
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLvddGKTAVAAIHD 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-183 |
2.17e-17 |
|
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: 76.76 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhKISNLDEYKP-FRRDVGYLfQESNDCFI 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL---NGGPLDFQRDsIARGLLYL-GHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 94 CPSVLDDVIFSllsrgkDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADM 173
Cdd:cd03231 87 TLSVLENLRFW------HADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170
....*....|
gi 489043565 174 QRRIAAILKS 183
Cdd:cd03231 161 VARFAEAMAG 170
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-202 |
2.26e-17 |
|
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: 77.83 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISnldeYKPFRRDVGYlfqesndcficPSVLDDVIFSllsrgKDK 112
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS----YKPQYIKADY-----------EGTVRDLLSS-----ITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 113 D---GSRAKAEkILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL----D 185
Cdd:cd03237 88 DfytHPYFKTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennE 166
|
170
....*....|....*..
gi 489043565 186 VTQIIVSHDKEFISDVA 202
Cdd:cd03237 167 KTAFVVEHDIIMIDYLA 183
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-193 |
2.42e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGL-----KSPCGGHIELFHHKISNLD-EY 74
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDvDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 75 KPFRRDVGYLFQESNDcFICPSVLDDVIFSLLSRG--KDKDGSRAKAEKILRELEIW-HLKDEI---VFNLSGGEKKLVA 148
Cdd:PRK14267 81 IEVRREVGMVFQYPNP-FPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWdEVKDRLndyPSNLSGGQRQRLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 149 LAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-193 |
2.79e-17 |
|
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: 76.87 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFhhkISNLDEYKPFRRDVGYL 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD---GKSYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FqESNDCFICPSVLDDVIFSLLSRGKDKdgsrAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:cd03268 78 I-EAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190
....*....|....*....|....*....|..
gi 489043565 165 PTTALDADMQRRIAAILKSL---DVTQIIVSH 193
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLrdqGITVLISSH 184
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-179 |
3.46e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.38 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEykPFRRDVGY----------L 84
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD--EYHQDLLYlghqpgikteL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNDCFICPsvlddvifslLSRGKDKDGSRAKAEKI-LRELEiwhlkDEIVFNLSGGEKKLVALAGILVAEPKILLLD 163
Cdd:PRK13538 90 TALENLRFYQR----------LHGPGDDEALWEALAQVgLAGFE-----DVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180
....*....|....*....|
gi 489043565 164 EPTTALD----ADMQRRIAA 179
Cdd:PRK13538 155 EPFTAIDkqgvARLEALLAQ 174
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-200 |
3.47e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.72 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERT-LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGY 83
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLD 163
Cdd:PRK13644 82 VFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489043565 164 EPTTALDADMQRRIAAILKSLD---VTQIIVSHDKEFISD 200
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHekgKTIVYITHNLEELHD 201
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-193 |
5.80e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.61 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVC-AKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdEYKPFRR 79
Cdd:PRK10790 337 QSGRIDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 80 DVGYLFQEsndcficPSVLDDVIFSLLSRGKDKDgsrakAEKILRELEIWHLKD--------------EIVFNLSGGEKK 145
Cdd:PRK10790 416 GVAMVQQD-------PVVLADTFLANVTLGRDIS-----EEQVWQALETVQLAElarslpdglytplgEQGNNLSVGQKQ 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489043565 146 LVALAGILVAEPKILLLDEPTTALDAD----MQRRIAAILKSldVTQIIVSH 193
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGteqaIQQALAAVREH--TTLVVIAH 533
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-193 |
1.21e-16 |
|
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: 74.00 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIelfhhkisnldeykpfrrdvgylfqesndcficpsVLDDVIFSLLSRgkdkd 113
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPDSGEI-----------------------------------LVDGKEVSFASP----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 114 gSRAKAEKIlreleiwhlkdEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQII 190
Cdd:cd03216 70 -RDARRAGI-----------AMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIF 137
|
...
gi 489043565 191 VSH 193
Cdd:cd03216 138 ISH 140
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-193 |
1.78e-16 |
|
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: 74.12 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCG--GHIelfhhKISNLDEYKP-FRRDVGYLFQesndc 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEV-----LINGRPLDKRsFRKIIGYVPQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 92 ficpsvlDDVIFSLLSrgkdkdgsrakaekiLRE-LEI-WHLKdeivfNLSGGEKKLVALAGILVAEPKILLLDEPTTAL 169
Cdd:cd03213 90 -------DDILHPTLT---------------VREtLMFaAKLR-----GLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180
....*....|....*....|....*..
gi 489043565 170 DADMQRRIAAILKSL---DVTQIIVSH 193
Cdd:cd03213 143 DSSSALQVMSLLRRLadtGRTIICSIH 169
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
30-202 |
2.01e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 30 KDKI-ALIGPNGCGKSTLLEIMAGLKSPC-GGHIE---LFHHKISNLDEYKP--FRRDVGYLFQESNDcfICPSVLDDVI 102
Cdd:PRK14243 35 KNQItAFIGPSGCGKSTILRCFNRLNDLIpGFRVEgkvTFHGKNLYAPDVDPveVRRRIGMVFQKPNP--FPKSIYDNIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 103 FSLLSRGKDKDGSRAkAEKILRELEIW-HLKDEIVFN---LSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIA 178
Cdd:PRK14243 113 YGARINGYKGDMDEL-VERSLRQAALWdEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIE 191
|
170 180
....*....|....*....|....*.
gi 489043565 179 AILKSL--DVTQIIVSHDKEFISDVA 202
Cdd:PRK14243 192 ELMHELkeQYTIIIVTHNMQQAARVS 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
34-177 |
3.95e-16 |
|
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: 74.04 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVGYLFQESndCFICPSVLDDVIFSLLSRGKDK- 112
Cdd:cd03248 44 ALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEP--VLFARSLQDNIAYGLQSCSFECv 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 113 --DGSRAKAEKILRELE--IWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRI 177
Cdd:cd03248 121 keAAQKAHAHSFISELAsgYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-194 |
4.53e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.76 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNAtHKDKI-ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeykpfRRDVG 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTV-PKGEIfGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-----RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLfqesndcficP---------SVLDDVIF--SLlsRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAG 151
Cdd:COG4152 75 YL----------PeerglypkmKVGEQLVYlaRL--KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489043565 152 ILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHD 194
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELaakGTTVIFSSHQ 188
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-198 |
4.63e-16 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 75.94 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 19 LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIelfhhkisnldeYKPFRRDVGYLFQES-------NDC 91
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL------------TKPAKGKLFYVPQRPymtlgtlRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 92 FICPSVLDDVifsllsrgKDKDGSRAKAEKILRELEIWH-LKDEIVFN--------LSGGEKKLVALAGILVAEPKILLL 162
Cdd:TIGR00954 535 IIYPDSSEDM--------KRRGLSDKDLEQILDNVQLTHiLEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*.
gi 489043565 163 DEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFI 198
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLW 642
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
34-184 |
1.12e-15 |
|
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: 72.79 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIElfhhkISNLDEYK-PF--RRDVGYLFqESNDCFICPSVLDDVIFSLLSRGK 110
Cdd:cd03266 35 GLLGPNGAGKTTTLRMLAGLLEPDAGFAT-----VDGFDVVKePAeaRRRLGFVS-DSTGLYDRLTARENLEYFAGLYGL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489043565 111 DKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:cd03266 109 KGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-215 |
1.23e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 74.90 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGG--------HIELF-HHKISNLD-EYKPFRrdvgYL 84
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGtvfrsakvRMAVFsQHHVDGLDlSSNPLL----YM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQesndCFicPSVLDDVIFSLLsrgkdkdGSRAKAEkilreleiwHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDE 164
Cdd:PLN03073 596 MR----CF--PGVPEQKLRAHL-------GSFGVTG---------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489043565 165 PTTALDADMqrrIAAILKSLDVTQ---IIVSHDKEFISDVASAMYRLTKSGLEP 215
Cdd:PLN03073 654 PSNHLDLDA---VEALIQGLVLFQggvLMVSHDEHLISGSVDELWVVSEGKVTP 704
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-184 |
1.25e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpfRRDVGYL 84
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA--RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNdcficpsvLD---DVIFSLLSRGKDKDGSRAKAEKILREL-EIWHLK---DEIVFNLSGGEKKLVALAGILVAEP 157
Cdd:PRK13537 86 PQFDN--------LDpdfTVRENLLVFGRYFGLSAAAARALVPPLlEFAKLEnkaDAKVGELSGGMKRRLTLARALVNDP 157
|
170 180
....*....|....*....|....*..
gi 489043565 158 KILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSL 184
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
35-202 |
1.32e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.07 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 35 LIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD--EYKPFRRDVGYLFQESNdcfICPS--VLDDVIFSLLSRGK 110
Cdd:PRK11153 36 VIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekELRKARRQIGMIFQHFN---LLSSrtVFDNVALPLELAGT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 111 DKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKS----LDV 186
Cdd:PRK11153 113 PKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDinreLGL 192
|
170
....*....|....*.
gi 489043565 187 TQIIVSHDKEFISDVA 202
Cdd:PRK11153 193 TIVLITHEMDVVKRIC 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
33-201 |
1.89e-15 |
|
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: 74.40 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGYLFQEsndcficPSVLDDVIFSLLSRGKDK 112
Cdd:COG4618 361 LGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR-EELGRHIGYLPQD-------VELFDGTIAENIARFGDA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 113 DGSR----AKA----EKILR-----ELEIwhlkDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDAD-MQRRIA 178
Cdd:COG4618 433 DPEKvvaaAKLagvhEMILRlpdgyDTRI----GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEgEAALAA 508
|
170 180
....*....|....*....|....*
gi 489043565 179 AI--LKSLDVTQIIVSHDKEFISDV 201
Cdd:COG4618 509 AIraLKARGATVVVITHRPSLLAAV 533
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-198 |
2.09e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 71.79 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfHHKISNLDEykpfrrdVGY 83
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVSSLLG-------LGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQESndcficPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLD 163
Cdd:cd03220 94 GFNPE------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 164 EPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFI 198
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSI 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
33-194 |
3.49e-15 |
|
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: 73.57 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTL-LEIMaGLkSPCGGHIELFHHKISNLD--EYKPFRRDVGYLFQesnDCFicpSVLD------DVI- 102
Cdd:COG4172 315 LGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDGLSrrALRPLRRRMQVVFQ---DPF---GSLSprmtvgQIIa 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 103 --FSLLSRGKDKDGSRAKAEKILRELEIwhlkDEIVFN-----LSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQR 175
Cdd:COG4172 387 egLRVHGPGLSAAERRARVAEALEEVGL----DPAARHrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQA 462
|
170 180
....*....|....*....|...
gi 489043565 176 RIAAILKSL----DVTQIIVSHD 194
Cdd:COG4172 463 QILDLLRDLqrehGLAYLFISHD 485
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-181 |
5.60e-15 |
|
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: 73.12 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVcAKIGE---RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKI-SNLDeykPFRRD 80
Cdd:TIGR01257 929 VCVKNL-VKIFEpsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLD---AVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQEsNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKIL 160
Cdd:TIGR01257 1005 LGMCPQH-NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180
....*....|....*....|.
gi 489043565 161 LLDEPTTALDADMQRRIAAIL 181
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLL 1104
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-193 |
5.97e-15 |
|
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: 70.98 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 16 ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGYLFQESndCFICP 95
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQEN--VLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 SVLDDVifSLLSRGKDKD-----GSRAKAEKILRELEIWHlkDEIV----FNLSGGEKKLVALAGILVAEPKILLLDEPT 166
Cdd:cd03252 91 SIRDNI--ALADPGMSMErvieaAKLAGAHDFISELPEGY--DTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180
....*....|....*....|....*....
gi 489043565 167 TALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:cd03252 167 SALDYESEHAIMRNMHDIcaGRTVIIIAH 195
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-194 |
1.02e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 31 DKIALIGPNGCGKSTLLEIMAGLkSPCGGHIELFHHKISNLDEYKPFRRDvGYLFQESNDCFICPsvlddvIFSLLSRGK 110
Cdd:PRK03695 23 EILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTPPFAMP------VFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 111 DKDGSRAKAEKILREL-EIWHLKDEI---VFNLSGGEKKLVALAGILV-------AEPKILLLDEPTTALDADMQRRIAA 179
Cdd:PRK03695 95 PDKTRTEAVASALNEVaEALGLDDKLgrsVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAALDR 174
|
170
....*....|....*...
gi 489043565 180 ILK---SLDVTQIIVSHD 194
Cdd:PRK03695 175 LLSelcQQGIAVVMSSHD 192
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-206 |
1.13e-14 |
|
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: 70.47 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 35 LIGPNGCGKSTLLEIMAGLKSPCGGHIE--------LFHHKISNLDEYkpFRRdvgyLFQESNDCFICPSVLDDV----- 101
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeiLDEFRGSELQNY--FTK----LLEGDVKVIVKPQYVDLIpkavk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 102 --IFSLLSRgKDKdgsRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAA 179
Cdd:cd03236 105 gkVGELLKK-KDE---RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 180 ILKSL---DVTQIIVSHD---KEFISDVASAMY 206
Cdd:cd03236 181 LIRELaedDNYVLVVEHDlavLDYLSDYIHCLY 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-194 |
1.18e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.56 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPF--RRDVGYLFQeSNDCF 92
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvRKRMSMLFQ-SGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 93 ICPSVLDDVIFSLlsrgkdKDGSRAKAE----KILRELEIWHLK---DEIVFNLSGGEKKLVALAGILVAEPKILLLDEP 165
Cdd:PRK11831 97 TDMNVFDNVAYPL------REHTQLPAPllhsTVMMKLEAVGLRgaaKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190
....*....|....*....|....*....|...
gi 489043565 166 TTALD----ADMQRRIAAILKSLDVTQIIVSHD 194
Cdd:PRK11831 171 FVGQDpitmGVLVKLISELNSALGVTCVVVSHD 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-202 |
1.46e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFhhkisnlDEYKpfrrdVGYL 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-------ETVK-----LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESNDcficpsvLDD--VIFSLLSRGKD-------KDGSRAKAEKilreleiwhlkdeivFN------------LSGGE 143
Cdd:TIGR03719 391 DQSRDA-------LDPnkTVWEEISGGLDiiklgkrEIPSRAYVGR---------------FNfkgsdqqkkvgqLSGGE 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 144 KKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVA 202
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIA 507
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-184 |
1.59e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 13 KIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAG-LKSPC-GGHIELFHHKISnldeyKPFRRDVGYLFQesnD 90
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPT-----KQILKRTGFVTQ---D 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 91 CFICP--SVLDDVIF-SLLS--RGKDKDGSRAKAEKILRELEIWHLKDEIVFN-----LSGGEKKLVALAGILVAEPKIL 160
Cdd:PLN03211 149 DILYPhlTVRETLVFcSLLRlpKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLL 228
|
170 180
....*....|....*....|....
gi 489043565 161 LLDEPTTALDADMQRRIAAILKSL 184
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSL 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-193 |
1.78e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTL--FENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVG 82
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 ------YLFQES---NDCFICPSVLDDVIFSLLSR-GKDK-------------DGSRAkaekilreleiwhlkdeivfnL 139
Cdd:PRK11160 418 vvsqrvHLFSATlrdNLLLAAPNASDEALIEVLQQvGLEKlleddkglnawlgEGGRQ---------------------L 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 140 SGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITH 532
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-200 |
1.88e-14 |
|
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: 71.35 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIElFHHKISnldeYKPfrrdvgylfQesndcFICPSVLDDVIFSLLSRGKDK 112
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKIS----YKP---------Q-----YISPDYDGTVEEFLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 113 -DGSRAKAEkILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADmQRRIAA-----ILKSLDV 186
Cdd:COG1245 430 fGSSYYKTE-IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRLAVAkairrFAENRGK 507
|
170
....*....|....*..
gi 489043565 187 TQIIVSHD---KEFISD 200
Cdd:COG1245 508 TAMVVDHDiylIDYISD 524
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
7-193 |
2.00e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 69.60 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKS--PCGGHIELFHHKISNLDEYKPFRRDVGYL 84
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKGQDLLELEPDERARAGLFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQE-------SNDCFicpsvLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFN------LSGGEKKLVALAG 151
Cdd:TIGR01978 83 FQYpeeipgvSNLEF-----LRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNrsvnegFSGGEKKRNEILQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 152 ILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSH 193
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITH 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-193 |
2.21e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.29 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 16 ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVGYLFQESndCFICP 95
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD-HHYLHRQVALVGQEP--VLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 SVLDDVIFSLLSRGKDKDGSRAK---AEKILRELE--IWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALD 170
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKaanAHDFIMEFPngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|...
gi 489043565 171 ADMQRRIAAILKSLDVTQIIVSH 193
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAH 672
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-194 |
2.28e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.73 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNaTHKDKI-ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGY 83
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLT-IPKGGItALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS-RELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 LFQEsNDCFICPSVLDDVIFSLL--SRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:COG4604 80 LRQE-NHINSRLTVRELVAFGRFpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 489043565 162 LDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHD 194
Cdd:COG4604 159 LDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-207 |
2.48e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.56 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLkspcgghIELFHH-KISN---LDEYKPFRRD 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRL-------IELYPEaRVSGevyLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGYLFQESNDCFICP------SVLDDVIFSL-LSR-GKDKDGSRAKAEKILRELEIW-HLKDEI---VFNLSGGEKKLVA 148
Cdd:PRK14247 77 VIELRRRVQMVFQIPnpipnlSIFENVALGLkLNRlVKSKKELQERVRWALEKAQLWdEVKDRLdapAGKLSGGQQQRLC 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489043565 149 LAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH---DKEFISDVASAMYR 207
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHfpqQAARISDYVAFLYK 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-193 |
3.88e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYL 84
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESndcficpSVLDDV-------IFSLLSRG------KDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAG 151
Cdd:PRK09700 86 YQEL-------SVIDELtvlenlyIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 152 ILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQII-VSH 193
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrkEGTAIVyISH 203
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-201 |
4.07e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHhkisnldeYKPFRRDVGYLFQ------------------ESndcfic 94
Cdd:COG4586 51 VGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--------YVPFKRRKEFARRigvvfgqrsqlwwdlpaiDS------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 95 psvlddviFSLLsrGKDKDGSRAKAEKILREL-EIWHLKDEI---VFNLSGGEKKLVALAGILVAEPKILLLDEPTTALD 170
Cdd:COG4586 117 --------FRLL--KAIYRIPDAEYKKRLDELvELLDLGELLdtpVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190
....*....|....*....|....*....|....*
gi 489043565 171 ADMQRRIAAILKSL----DVTQIIVSHDkefISDV 201
Cdd:COG4586 187 VVSKEAIREFLKEYnrerGTTILLTSHD---MDDI 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-194 |
4.30e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.52 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 22 NLNLNAthKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNL--DEYKPFRRD-VGYLFQESNdcfICP--S 96
Cdd:PRK10535 28 SLDIYA--GEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdaDALAQLRREhFGFIFQRYH---LLShlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 97 VLDDVIFSLLSRGKDKDGSRAKAEKILRELeiwHLKDEIVF---NLSGGEKKLVALAGILVAEPKILLLDEPTTALDADM 173
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRL---GLEDRVEYqpsQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180
....*....|....*....|....
gi 489043565 174 QRRIAAILKSLDV---TQIIVSHD 194
Cdd:PRK10535 180 GEEVMAILHQLRDrghTVIIVTHD 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-202 |
4.51e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHH-KISNLDEYKPfrRDV-G 82
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQQDPP--RNVeG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLF-------QESNDCF-----ICPSVLDDVIFSLLSRgkdkdgsRAKAEKILRELEIWHLKDEIVFN------------ 138
Cdd:PRK11147 82 TVYdfvaegiEEQAEYLkryhdISHLVETDPSEKNLNE-------LAKLQEQLDHHNLWQLENRINEVlaqlgldpdaal 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 139 --LSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVA 202
Cdd:PRK11147 155 ssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMA 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-184 |
5.13e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 2 SCTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGhielfhhKISNLDEYKP----- 76
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG-------KITVLGVPVPararl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 FRRDVGYLFQESNdcficpsvLD---DVIFSLLSRGKDKDGSRAKAEKILREL-EIWHLK---DEIVFNLSGGEKKLVAL 149
Cdd:PRK13536 112 ARARIGVVPQFDN--------LDlefTVRENLLVFGRYFGMSTREIEAVIPSLlEFARLEskaDARVSDLSGGMKRRLTL 183
|
170 180 190
....*....|....*....|....*....|....*
gi 489043565 150 AGILVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSL 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-193 |
8.06e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDE---YKPFRRDVGYLFQES----------NDCFICpsvldd 100
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgicLPPEKRRIGYVFQDArlfphykvrgNLRYGM------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 101 vifsllsrgkdKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAI 180
Cdd:PRK11144 102 -----------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170
....*....|....*..
gi 489043565 181 L----KSLDVTQIIVSH 193
Cdd:PRK11144 171 LerlaREINIPILYVSH 187
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-184 |
9.52e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 9.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS-----NLDEYKPFRRDVGYLFqesndcficPSVLDDVIF----- 103
Cdd:PRK15056 37 ALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqalqkNLVAYVPQSEEVDWSF---------PVLVEDVVMmgryg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 104 --SLLSRGKDKDgsRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAIL 181
Cdd:PRK15056 108 hmGWLRRAKKRD--RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
...
gi 489043565 182 KSL 184
Cdd:PRK15056 186 REL 188
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-193 |
9.58e-14 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 69.36 E-value: 9.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIG--ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdEYKPFRRDVG 82
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY-TLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQesnDCFIcpsvLDDVIFSLLSRGKDKDGSRAKaekILRELEIWHLKDEI--------------VFNLSGGEKKLVA 148
Cdd:TIGR02203 410 LVSQ---DVVL----FNDTIANNIAYGRTEQADRAE---IERALAAAYAQDFVdklplgldtpigenGVLLSGGQRQRLA 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 149 LAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAH 526
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-201 |
2.11e-13 |
|
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: 65.95 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 19 LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhkisnldeykpfRRDVGYLFQES---NDcficp 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--------------PGSIAYVSQEPwiqNG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 SVLDDVIFsllsrGKDKDGSR----AKAEKILRELEIWHLKDEIV-----FNLSGGEKKLVALAGILVAEPKILLLDEPT 166
Cdd:cd03250 81 TIRENILF-----GKPFDEERyekvIKACALEPDLEILPDGDLTEigekgINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 489043565 167 TALDADMQRRIA--AILKSL--DVTQIIVSHDKEFISDV 201
Cdd:cd03250 156 SAVDAHVGRHIFenCILGLLlnNKTRILVTHQLQLLPHA 194
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-200 |
2.58e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIElFHHKISnldeYKPfrrdvgylfQesndcFICPSVLDDVIFSLLSRGKDK 112
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-PELKIS----YKP---------Q-----YIKPDYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 113 DGSRAKAEkILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADmQRRIAA-----ILKSLDVT 187
Cdd:PRK13409 429 GSSYYKSE-IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRLAVAkairrIAEEREAT 506
|
170
....*....|....*.
gi 489043565 188 QIIVSHD---KEFISD 200
Cdd:PRK13409 507 ALVVDHDiymIDYISD 522
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-184 |
3.38e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 16 ERTLFENLNLNATHKDKIALIGPNGCGKS-TLLEIMAGLKSP----CGGHIeLFHHKiSNLDEYKPFRRDV-----GYLF 85
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDI-RFHGE-SLLHASEQTLRGVrgnkiAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 86 QEsndcficPSV-------LDDVIFSLLS--RGKDKDGSRAKAEKILRELEIWH----LKDeIVFNLSGGEKKLVALAGI 152
Cdd:PRK15134 99 QE-------PMVslnplhtLEKQLYEVLSlhRGMRREAARGEILNCLDRVGIRQaakrLTD-YPHQLSGGERQRVMIAMA 170
|
170 180 190
....*....|....*....|....*....|..
gi 489043565 153 LVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLREL 202
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-193 |
3.86e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIelfhhKISNLD----EYKPFRRDVGYLFQEsnd 90
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI-----LIDGTDirtvTRASLRRNIAVVFQD--- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 91 cficPSVLDDVIFSLLSRGKDKdgsrAKAEKILRELEIWHLKDEIVFN--------------LSGGEKKLVALAGILVAE 156
Cdd:PRK13657 418 ----AGLFNRSIEDNIRVGRPD----ATDEEMRAAAERAQAHDFIERKpdgydtvvgergrqLSGGERQRLAIARALLKD 489
|
170 180 190
....*....|....*....|....*....|....*....
gi 489043565 157 PKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELmkGRTTFIIAH 528
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-191 |
4.68e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.96 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 3 CTISLKNVCAKI----GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSpcGGHI--ELFhhkISNLDEYKP 76
Cdd:cd03232 2 SVLTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVItgEIL---INGRPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 FRRDVGYLfqESNDCFI-CPSVLDDVIFSLLSRGkdkdgsrakaekilreleiwhlkdeivfnLSGGEKKLVALAGILVA 155
Cdd:cd03232 77 FQRSTGYV--EQQDVHSpNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAA 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 489043565 156 EPKILLLDEPTTALDADMQRRIAAILKSL-DVTQIIV 191
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAIL 162
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-181 |
8.73e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.79 E-value: 8.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSpcGGHIElFHHKISNLDEYK-PFRRDVGYLfqESNDCFiCP--SVLDDVIFSLLSRGK 110
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGRKT--GGYIE-GDIRISGFPKKQeTFARISGYC--EQNDIH-SPqvTVRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 111 DKDGSRAK---AEKILRELEIWHLKDEIV-----FNLSGGEKKLVALAGILVAEPKILLLDEPTTALDAdmqrRIAAIL 181
Cdd:PLN03140 984 KEVSKEEKmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA----RAAAIV 1058
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-193 |
1.70e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 6 SLKNVCAKIGERTLFENLNLNA----THkdkiALIGPNGCGKSTLLEIMAGLKS--PCGGHIELFHHKISNLDEYKPFRR 79
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIkpgeVH----AIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 80 DVGYLFQ---EsndcfIcPSV-LDDVIFSLLSRGKDKDGSRAKAEKILRE-LEIWHLKDEIVF-----NLSGGEKKLVAL 149
Cdd:COG0396 78 GIFLAFQypvE-----I-PGVsVSNFLRTALNARRGEELSAREFLKLLKEkMKELGLDEDFLDryvneGFSGGEKKRNEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 150 AGILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSH 193
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITH 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-193 |
2.14e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVgYLFQESNDCFICPSVLDDVIFSLLSRGKDKd 113
Cdd:PRK15439 41 ALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGI-YLVPQEPLLFPNLSVKENILFGLPKRQASM- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 114 gsrAKAEKILRELEIwHLK-DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQI 189
Cdd:PRK15439 119 ---QKMKQLLAALGC-QLDlDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELlaqGVGIV 194
|
....
gi 489043565 190 IVSH 193
Cdd:PRK15439 195 FISH 198
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
34-206 |
4.29e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.98 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD--EYKPFRRDVGYLFQesnDCFicpSVLD------DVI-FS 104
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgrELRPLRRRMQMVFQ---DPY---ASLNprmtvgDIIaEP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 105 LLSRG-KDKDGSRAKAEKILRE--LEIWHLkdeivfN-----LSGGEKKLVALAGILVAEPKILLLDEPTTALD------ 170
Cdd:COG4608 122 LRIHGlASKAERRERVAELLELvgLRPEHA------DrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqaq 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 171 -----ADMQRRiaailksLDVTQIIVSHD---KEFISD-VAsAMY 206
Cdd:COG4608 196 vlnllEDLQDE-------LGLTYLFISHDlsvVRHISDrVA-VMY 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-207 |
4.65e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 21 ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYK--PFRRDVGYLFQESNDCFICPSVL 98
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqALRRDIQFIFQDPYASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 99 DDVIFSLLSRGKDKDGsRAKAEKILRELEIWHLKDEIVF----NLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQ 174
Cdd:PRK10261 421 GDSIMEPLRVHGLLPG-KAAAARVAWLLERVGLLPEHAWryphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489043565 175 RRIAAIL----KSLDVTQIIVSHDK---EFISDVASAMYR 207
Cdd:PRK10261 500 GQIINLLldlqRDFGIAYLFISHDMavvERISHRVAVMYL 539
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-193 |
4.88e-12 |
|
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: 62.51 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAK--IGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVG 82
Cdd:cd03244 3 IEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD-LRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQEsndcficPSVLDDVI-FSLLSRGKDKDgsrakaEKILRELEIWHLKDEIVF--------------NLSGGEKKLV 147
Cdd:cd03244 82 IIPQD-------PVLFSGTIrSNLDPFGEYSD------EELWQALERVGLKEFVESlpggldtvveeggeNLSVGQRQLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 148 ALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH 196
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-200 |
1.82e-11 |
|
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: 60.89 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGER--TLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVG 82
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED-LRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQEsndcficPSVLDDVIFSLLSR-GKDKDgsrakaEKILRELEIwhlkDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:cd03369 86 IIPQD-------PTLFSGTIRSNLDPfDEYSD------EEIYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489043565 162 LDEPTTALDADMQRRIAAILKSL--DVTQIIVSHDKEFISD 200
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEftNSTILTIAHRLRTIID 189
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-194 |
2.34e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 4 TISLKNVCAKIGERTlFE--NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS--NLDEYKPfrr 79
Cdd:PRK10522 322 TLELRNVTFAYQDNG-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeQPEDYRK--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 80 dvgyLFQesndcficpSVLDDV-IFSLLSRGKDKDGSRAKAEKILRELEIWH---LKDEIVFN--LSGGEKKLVALAGIL 153
Cdd:PRK10522 398 ----LFS---------AVFTDFhLFDQLLGPEGKPANPALVEKWLERLKMAHkleLEDGRISNlkLSKGQKKRLALLLAL 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 154 VAEPKILLLDEptTALDADMQ-RRI-----AAILKSLDVTQIIVSHD 194
Cdd:PRK10522 465 AEERDILLLDE--WAADQDPHfRREfyqvlLPLLQEMGKTIFAISHD 509
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
5-170 |
3.29e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.89 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFenlNLNATHKDK-IALI-GPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeyKPFRRDVG 82
Cdd:PRK13541 2 LSLHQLQFNIEQKNLF---DLSITFLPSaITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLFQESndcficpsvLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:PRK13541 77 HNLGLK---------LEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
....*...
gi 489043565 163 DEPTTALD 170
Cdd:PRK13541 148 DEVETNLS 155
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-184 |
4.63e-11 |
|
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: 61.24 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 32 KIALIGPNGCGKS-TLLEIMAGLKSP---CGGHIELFHHKISNLDEyKPFRR----DVGYLFQEsndcficP-------- 95
Cdd:COG4172 38 TLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSE-RELRRirgnRIAMIFQE-------Pmtslnplh 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 SVLDDVIFSL-LSRGKDKDGSRAKAEKILRELEIwhlKD-EIVFN-----LSGGEKKLVALAGILVAEPKILLLDEPTTA 168
Cdd:COG4172 110 TIGKQIAEVLrLHRGLSGAAARARALELLERVGI---PDpERRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTA 186
|
170
....*....|....*.
gi 489043565 169 LDADMQRRIAAILKSL 184
Cdd:COG4172 187 LDVTVQAQILDLLKDL 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-203 |
4.94e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVC----------------------AKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCG 58
Cdd:COG1134 1 MSSMIEVENVSksyrlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 59 GHIELfHHKISNLDEykpfrrdVGYLFQesndcficP--SVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIV 136
Cdd:COG1134 81 GRVEV-NGRVSALLE-------LGAGFH--------PelTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489043565 137 FNLSGGEKklVALA-GILVA-EPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVAS 203
Cdd:COG1134 145 KTYSSGMR--ARLAfAVATAvDPDILLVDEVLAVGDAAFQKKCLARIRELresGRTVIFVSHSMGAVRRLCD 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-206 |
7.86e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHI----------------ELFHH--KISNLD---EYKPFRRDVgylfqesndc 91
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtELQDYfkKLANGEikvAHKPQYVDL---------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 92 fiCPSVLDDVIFSLLsrgkDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDA 171
Cdd:COG1245 172 --IPKVFKGTVRELL----EKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489043565 172 DMQRRIAAILKSL---DVTQIIVSHD---KEFISDVASAMY 206
Cdd:COG1245 246 YQRLNVARLIRELaeeGKYVLVVEHDlaiLDYLADYVHILY 286
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-214 |
1.02e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 58.77 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEimaGLKSPCGGhiELFHHKISNLDEYKPFRR-----DVGYLFQESND----CFICPSVLDDVIFs 104
Cdd:cd03240 26 LIVGQNGAGKTTIIE---ALKYALTG--ELPPNSKGGAHDPKLIREgevraQVKLAFENANGkkytITRSLAILENVIF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 105 llsrgkdkdgsrakaekiLRELEI-WHLKDEIVFnLSGGEKKLV------ALAGILVAEPKILLLDEPTTALDADMQR-- 175
Cdd:cd03240 100 ------------------CHQGESnWPLLDMRGR-CSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDEENIEes 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489043565 176 --RIAAILKSLDVTQIIV-SHDKEFIsDVASAMYRLTKSGLE 214
Cdd:cd03240 161 laEIIEERKSQKNFQLIViTHDEELV-DAADHIYRVEKDGRQ 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-201 |
1.33e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.24 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 18 TLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLkSPCGGHIELFHHKISNLDEyKPFRRDVGYLFQESNdcFICPSV 97
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDP-ESWRKHLSWVGQNPQ--LPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 98 LDDVifsLLSRGKDKDGS------RAKAEKILRELEIwHLKDEIVFN---LSGGEKKLVALAGILVAEPKILLLDEPTTA 168
Cdd:PRK11174 440 RDNV---LLGNPDASDEQlqqaleNAWVSEFLPLLPQ-GLDTPIGDQaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190
....*....|....*....|....*....|....*
gi 489043565 169 LDADMQRRIAAILK--SLDVTQIIVSHDKEFISDV 201
Cdd:PRK11174 516 LDAHSEQLVMQALNaaSRRQTTLMVTHQLEDLAQW 550
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-200 |
1.45e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 16 ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAG--LKSPCGGHIELfhhkisnldEYKPFRRDVgylfqesndcfi 93
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV---------PDNQFGREA------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 94 cpSVLDDVifsllsrgkDKDGSRAKAEKILrelEIWHLKDEIVF-----NLSGGEKKLVALAGILVAEPKILLLDEPTTA 168
Cdd:COG2401 101 --SLIDAI---------GRKGDFKDAVELL---NAVGLSDAVLWlrrfkELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 489043565 169 LDADMQRRIAAIL----KSLDVTQIIVSHDKEFISD 200
Cdd:COG2401 167 LDRQTAKRVARNLqklaRRAGITLVVATHHYDVIDD 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-194 |
1.59e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 14 IGERTLFENLNLNATHKDKIALIGPNGCGKST----LLEIMAGlkspcGGHIELFHHKISNLDEYK--PFRRDVGYLFQE 87
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQllPVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 88 SNDCfICP--SVLDDVIFSLlsRGKDKDGSRAKAE-KILRELEIWHLKDEIVF----NLSGGEKKLVALAGILVAEPKIL 160
Cdd:PRK15134 371 PNSS-LNPrlNVLQIIEEGL--RVHQPTLSAAQREqQVIAVMEEVGLDPETRHrypaEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190
....*....|....*....|....*....|....*...
gi 489043565 161 LLDEPTTALDADMQRRIAAILKSLDVTQ----IIVSHD 194
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHqlayLFISHD 485
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-206 |
1.90e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.85 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 22 NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYLFQESNdCFICPSVLDDV 101
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVR-LFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 102 IF-------SLLSRG--KDKDGSRAKAEKILRE---LEIWHLKD---EIVFNLSGGEKKLVALAGILVAEPKILLLDEPT 166
Cdd:PRK11300 102 LVaqhqqlkTGLFSGllKTPAFRRAESEALDRAatwLERVGLLEhanRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489043565 167 TALD----ADMQRRIAAILKSLDVTQIIVSHDKEFISDVASAMY 206
Cdd:PRK11300 182 AGLNpketKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIY 225
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-202 |
1.92e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIEL--------------------FHHKISNLDEY 74
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnwqlawvnqetpalpqpaLEYVIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 75 KPFRRDVGYLfQESNDCFICPSV---LDDVifsllsrgkDKDGSRAKAEKILRELEIWHLK-DEIVFNLSGGEKKLVALA 150
Cdd:PRK10636 92 RQLEAQLHDA-NERNDGHAIATIhgkLDAI---------DAWTIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVA 202
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIV 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
36-206 |
2.89e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.56 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 36 IGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDE--YKPFRRDVGYLFQESNDCFICPSVLDDVI-------FSLL 106
Cdd:PRK15079 53 VGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSDIQMIFQDPLASLNPRMTIGEIIaeplrtyHPKL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 107 SRGKDKDGSRAKAEKI-LRELEIWHLKDEivfnLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL- 184
Cdd:PRK15079 133 SRQEVKDRVKAMMLKVgLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLq 208
|
170 180
....*....|....*....|....*...
gi 489043565 185 ---DVTQIIVSHD---KEFISDVASAMY 206
Cdd:PRK15079 209 remGLSLIFIAHDlavVKHISDRVLVMY 236
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-183 |
3.19e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALI--GPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKpFRRDVGYLFQESNDCficpSVLDDVIF--SLLSRG 109
Cdd:PRK13543 39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSR-FMAYLGHLPGLKADL----STLENLHFlcGLHGRR 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489043565 110 KDKDGSRAKAEKILRELEiwhlkDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDAD----MQRRIAAILKS 183
Cdd:PRK13543 114 AKQMPGSALAIVGLAGYE-----DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgitlVNRMISAHLRG 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-207 |
3.53e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 21 ENLNLNATHKDKIALIGPNGCGKS-TLLEIM-----AGLKSPCGGH-IELFHHKISNLDEY--KPFRR----DVGYLFQE 87
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMlLRRRSRQVIELSEQsaAQMRHvrgaDMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 88 S----NDCFicpSVLDDVIFSL-LSRGKDKDGSRAKAEKILRELEIWHLKDEIV---FNLSGGEKKLVALAGILVAEPKI 159
Cdd:PRK10261 113 PmtslNPVF---TVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAQTILSrypHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 160 LLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFISDVAS---AMYR 207
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLqkemSMGVIFITHDMGVVAEIADrvlVMYQ 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-206 |
3.64e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAG-LKSPCGGHIE-------LFHHKISNLDEY-------------KPFRRDvgylfqesndc 91
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGeLIPNLGDYEEepswdevLKRFRGTELQNYfkklyngeikvvhKPQYVD----------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 92 fICPSVLDDVIFSLLSRgKDKdgsRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDA 171
Cdd:PRK13409 171 -LIPKVFKGKVRELLKK-VDE---RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489043565 172 DmQR-RIAAILKSL--DVTQIIVSHD---KEFISDVASAMY 206
Cdd:PRK13409 246 R-QRlNVARLIRELaeGKYVLVVEHDlavLDYLADNVHIAY 285
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-196 |
3.82e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGlKSPCG--GHIELFHHKISNLDEYKPFRRDVG 82
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysNDLTLFGRRRGSGETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 YLfqeSN----DCFICPSVLdDVIFS--LLSRGKDKDGSRAKAEKILRELEIWHLKDEIV---F-NLSGGEKKLVALAGI 152
Cdd:PRK10938 340 YV---SSslhlDYRVSTSVR-NVILSgfFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTAdapFhSLSWGQQRLALIVRA 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 153 LVAEPKILLLDEPTTALDA---DMQRRIAAILKSLDVTQII-VSHDKE 196
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLISEGETQLLfVSHHAE 463
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-202 |
5.09e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHH-KISNLDEYkpfrRDvgy 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvKLAYVDQS----RD--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 lfqesndcficpsVLDD--VIFSLLSRGKD--KDG-----SRAKA----------EKilreleiwhlkdeIVFNLSGGEK 144
Cdd:PRK11819 398 -------------ALDPnkTVWEEISGGLDiiKVGnreipSRAYVgrfnfkggdqQK-------------KVGVLSGGER 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489043565 145 KLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVA 202
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIA 509
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-169 |
6.95e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRD 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 81 VGyLFQESNDCFICPSVLDDvifslLSRGKDKDGSRAKAEKILRELEIW----HLKDEIVFNLSGGEKKLVALAGILVAE 156
Cdd:PRK11614 82 VA-IVPEGRRVFSRMTVEEN-----LAMGGFFAERDQFQERIKWVYELFprlhERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170
....*....|...
gi 489043565 157 PKILLLDEPTTAL 169
Cdd:PRK11614 156 PRLLLLDEPSLGL 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-193 |
1.41e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 19 LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHK--------------------ISNLDEYKPFR 78
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEhtndmtneqdyqgdeeqnvgMKNVNEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 79 R----DVGYLFQES-----NDCFICPSVLDDV--IFSLLSR---------------GKDkDGSRAKAEKILRELEIwhlk 132
Cdd:PTZ00265 1263 EggsgEDSTVFKNSgkillDGVDICDYNLKDLrnLFSIVSQepmlfnmsiyenikfGKE-DATREDVKRACKFAAI---- 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 133 DEIV---------------FNLSGGEKKLVALAGILVAEPKILLLDEPTTALDAD----MQRRIAAILKSLDVTQIIVSH 193
Cdd:PTZ00265 1338 DEFIeslpnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-194 |
1.63e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.58 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFH---HKISNLDEYKPFRRDV 81
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQeSNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILL 161
Cdd:PRK10070 109 AMVFQ-SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 489043565 162 LDEPTTALD----ADMQRRIAAILKSLDVTQIIVSHD 194
Cdd:PRK10070 188 MDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-203 |
1.71e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 20 FENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDE---------YKPFRRDVGYLFQES-- 88
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvYLPEDRQSSGLYLDApl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 89 --NdcfICPSVLDDVIFsLLSRGKDkdgsRAKAEKILRELEI-WHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEP 165
Cdd:PRK15439 359 awN---VCALTHNRRGF-WIKPARE----NAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489043565 166 TTALDADMQRRIAAILKSL---DVTQIIVSHDKEFISDVAS 203
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMAD 471
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-201 |
1.84e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.88 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELfhhkisnldeykpfRRDVGYLFQES---NDcficpSVLDDVIFsllsrG 109
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--------------KGSVAYVPQQAwiqND-----SLRENILF-----G 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 110 KDKDGSRAK----AEKILRELEIWHLKD-----EIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRI--- 177
Cdd:TIGR00957 723 KALNEKYYQqvleACALLPDLEILPSGDrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfeh 802
|
170 180
....*....|....*....|....*...
gi 489043565 178 ----AAILKslDVTQIIVSHDKEFISDV 201
Cdd:TIGR00957 803 vigpEGVLK--NKTRILVTHGISYLPQV 828
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
30-210 |
2.29e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 30 KDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVGYLFQESNDCfICPSVLDDVIFSLLSRG 109
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD-YSYRSQRIRMIFQDPSTS-LNPRQRISQILDFPLRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 110 KDKDGSRAKAEKILREL-EIWHLKDEIVF---NLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLD 185
Cdd:PRK15112 117 NTDLEPEQREKQIIETLrQVGLLPDHASYyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQ 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489043565 186 ---------VTQ-----------IIVSHDKEFI-----SDV-ASAMYRLTK 210
Cdd:PRK15112 197 ekqgisyiyVTQhlgmmkhisdqVLVMHQGEVVergstADVlASPLHELTK 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-185 |
2.45e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 16 ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKI-SNLDEYKPFRRDVGYLFQESNDCFIC 94
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 95 PSVLDDVIFSLLSRGKDkdgsrakaeKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDadmQ 174
Cdd:PRK13540 93 ENCLYDIHFSPGAVGIT---------ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---E 160
|
170
....*....|.
gi 489043565 175 RRIAAILKSLD 185
Cdd:PRK13540 161 LSLLTIITKIQ 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-193 |
2.74e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERT---LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHI-------------------- 61
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkwwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 62 -------ELFHHKISNLDEYKPFR-RDVGYLFQESN-DCFICPSVLDDV---------IFSLLSRGKDKDG--SRAKAEK 121
Cdd:PTZ00265 463 gvvsqdpLLFSNSIKNNIKYSLYSlKDLEALSNYYNeDGNDSQENKNKRnscrakcagDLNDMSNTTDSNEliEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 122 ILRELEIWHLKDEIVFN--------------------LSGGEKKLVALAGILVAEPKILLLDEPTTALDAD----MQRRI 177
Cdd:PTZ00265 543 TIKDSEVVDVSKKVLIHdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseylVQKTI 622
|
250
....*....|....*.
gi 489043565 178 AAILKSLDVTQIIVSH 193
Cdd:PTZ00265 623 NNLKGNENRITIIIAH 638
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-193 |
2.97e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIsnldeykPFR--RD-----VGYLFQESN--DCFicpSVLDDVIfs 104
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-------RIRspRDaialgIGMVHQHFMlvPNL---TVAENIV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 105 lLSRGKDKDG--SRAKAEKILREL-EIWHLK---DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIA 178
Cdd:COG3845 103 -LGLEPTKGGrlDRKAARARIRELsERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELF 181
|
170
....*....|....*...
gi 489043565 179 AILKSL---DVTQIIVSH 193
Cdd:COG3845 182 EILRRLaaeGKSIIFITH 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-208 |
3.15e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMA-----GLKSPCG-GHIE--LFHHKISNLD---- 72
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPKNCQiLHVEqeVVGDDTTALQcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 73 ---EYKPFRRDVGYLFQESNDCFICPSVLDDVIFSllSRGKDKDGSRAKAEKILRELEI--------------------- 128
Cdd:PLN03073 258 tdiERTQLLEEEAQLVAQQRELEFETETGKGKGAN--KDGVDKDAVSQRLEEIYKRLELidaytaearaasilaglsftp 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 129 -WHLKDEIVFnlSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIVSHDKEFISDVASAMYR 207
Cdd:PLN03073 336 eMQVKATKTF--SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILH 413
|
.
gi 489043565 208 L 208
Cdd:PLN03073 414 L 414
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
32-193 |
3.69e-09 |
|
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: 55.98 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 32 KIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEyKPFRRDVGYLFQESndcficpsVL-DDVIFSLLSRGK 110
Cdd:COG5265 386 TVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ-ASLRAAIGIVPQDT--------VLfNDTIAYNIAYGR 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 111 DkDGSRAkaekilrelEIW------HLKDEIV--------------FNLSGGEKKLVALAGILVAEPKILLLDEPTTALD 170
Cdd:COG5265 457 P-DASEE---------EVEaaaraaQIHDFIEslpdgydtrvgergLKLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
170 180
....*....|....*....|....*
gi 489043565 171 ADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:COG5265 527 SRTERAIQAALREVarGRTTLVIAH 551
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-191 |
4.06e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSpcGGHIElFHHKISN---LDEykPFRRDVGYLFQesNDCFICPS-VLDDVIFSLLSRG 109
Cdd:TIGR00956 793 ALMGASGAGKTTLLNVLAERVT--TGVIT-GGDRLVNgrpLDS--SFQRSIGYVQQ--QDLHLPTStVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 110 KDKDGSRAK---AEKILRELEIWHLKDEIV----FNLSGGEKKLVALAGILVAEPKILL-LDEPTTALDADMQRRIAAIL 181
Cdd:TIGR00956 866 PKSVSKSEKmeyVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLM 945
|
170
....*....|.
gi 489043565 182 KSL-DVTQIIV 191
Cdd:TIGR00956 946 RKLaDHGQAIL 956
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-184 |
5.67e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 17 RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAG-LKSPCG-------GHIELFHHKISNLDEYKPFRRDvGYLFQES 88
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLR-AVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 89 NDCFicPSVLDDVIfsLLSRGKDkdgSRAKAEKILRELEI-WH---------LKDEIVFNLSGGEKKLVALAGIL----- 153
Cdd:PRK13547 93 QPAF--AFSAREIV--LLGRYPH---ARRAGALTHRDGEIaWQalalagataLVGRDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190
....*....|....*....|....*....|....*
gi 489043565 154 ----VAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRL 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-206 |
7.25e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLD--EYKPFRRDVGYLFQEsndcficP-----------SVLD 99
Cdd:PRK11308 44 LAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeAQKLLRQKIQIVFQN-------PygslnprkkvgQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 100 D--VIFSLLSRgkdkdgsRAKAEKILRELEIWHLKDEIVFN----LSGGEKKLVALAGILVAEPKILLLDEPTTALDADM 173
Cdd:PRK11308 117 EplLINTSLSA-------AERREKALAMMAKVGLRPEHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489043565 174 QrriAAIL-------KSLDVTQIIVSHD---KEFISDVASAMY 206
Cdd:PRK11308 190 Q---AQVLnlmmdlqQELGLSYVFISHDlsvVEHIADEVMVMY 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
35-194 |
9.01e-09 |
|
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: 54.80 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 35 LIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIS--NLDEYkpfrRDvgyLFqeSndcficpsvlddVIFS---LLSR- 108
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTadNREAY----RQ---LF--S------------AVFSdfhLFDRl 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 109 -GKDKDGSRAKAEKILRELEIWH---LKDEiVF---NLSGGEKKLVALagiLVA--EPK-ILLLDEptTALDADMQ-RRI 177
Cdd:COG4615 422 lGLDGEADPARARELLERLELDHkvsVEDG-RFsttDLSQGQRKRLAL---LVAllEDRpILVFDE--WAADQDPEfRRV 495
|
170 180
....*....|....*....|..
gi 489043565 178 --AAIL---KSLDVTQIIVSHD 194
Cdd:COG4615 496 fyTELLpelKARGKTVIAISHD 517
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-193 |
1.10e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 1 MSCTISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLkSPCG---GHI-----ELFHHKISNLD 72
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIifegeELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 73 eykpfRRDVGYLFQEsndCFICP--SVLDDvIF--SLLSRGK--DKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKL 146
Cdd:PRK13549 81 -----RAGIAIIHQE---LALVKelSVLEN-IFlgNEITPGGimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489043565 147 VALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSH 193
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLkahGIACIYISH 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-184 |
2.31e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 17 RTL-FENLNLNAthKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLdEYKPFRRDVGYLFQESNDcficp 95
Cdd:PRK10938 17 KTLqLPSLTLNA--GDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRL-SFEQLQKLVSDEWQRNNT----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 svlddvifSLLSRGKDkDGSRAKAEKILRELE-------------IWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLL 162
Cdd:PRK10938 89 --------DMLSPGED-DTGRTTAEIIQDEVKdparceqlaqqfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180
....*....|....*....|..
gi 489043565 163 DEPTTALDADMQRRIAAILKSL 184
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASL 181
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-184 |
2.34e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 52.26 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 35 LIGPNGCGKSTLLEIMAGLKSPCG---GHIelfHHK-ISNLDEYKPFRRDVGYLFQEsnDCFICP-SVLDDVIFSLLSRG 109
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEGNVsveGDI---HYNgIPYKEFAEKYPGEIIYVSEE--DVHFPTlTVRETLDFALRCKG 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 110 kdkdgsrakaekilreleiwhlkDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:cd03233 113 -----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTM 164
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-193 |
2.52e-08 |
|
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: 53.29 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLkSPCG---GHI-----ELFHHKISNLDeykp 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIywsgsPLKASNIRDTE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 fRRDVGYLFQEsndCFICP--SVLDDVIF----SLLSRGKDKDGSRAKAEKILRELEIWHLKD-EIVFNLSGGEKKLVAL 149
Cdd:TIGR02633 77 -RAGIVIIHQE---LTLVPelSVAENIFLgneiTLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489043565 150 AGILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSH 193
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLkahGVACVYISH 199
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-193 |
5.75e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 21 ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHkisNLDEYK--PFRRDVGYLFQESNdcficpsVL 98
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTlaSLRNQVALVSQNVH-------LF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 99 DDVIFSLLSRGKDKDGSRA---KAEKILRELE-IWHLK---DEIV----FNLSGGEKKLVALAGILVAEPKILLLDEPTT 167
Cdd:PRK11176 430 NDTIANNIAYARTEQYSREqieEAARMAYAMDfINKMDnglDTVIgengVLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180
....*....|....*....|....*...
gi 489043565 168 ALDADMQRRIAAILKSL--DVTQIIVSH 193
Cdd:PRK11176 510 ALDTESERAIQAALDELqkNRTSLVIAH 537
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
5-201 |
5.95e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 51.54 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAkigertlFENLNLNATHKDKI-ALIGPNGCGKSTLLEIMA--------GLKSPCGGHIELFHHKISN----- 70
Cdd:COG3950 6 LTIENFRG-------FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIAlalsgllsRLDDVKFRKLLIRNGEFGDsakli 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 71 -------------LDEYKPFRRDVGYLFQESNDCFICPSVLDDVIFSLLSRGKD--KDGSRAKAEKI------------- 122
Cdd:COG3950 79 lyygtsrllldgpLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDleNKLSDELDEKLeavrealnkllpd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 123 LRELEIWHLKDEIVF-----------NLSGGEKKLVALAGILV--------------AEPKILLLDEPTTALDADMQRRI 177
Cdd:COG3950 159 FKDIRIDRDPGRLVIldkngeelplnQLSDGERSLLALVGDLArrlaelnpalenplEGEGIVLIDEIDLHLHPKWQRRI 238
|
250 260
....*....|....*....|....*.
gi 489043565 178 AAILKS-LDVTQIIVS-HDKEFISDV 201
Cdd:COG3950 239 LPDLRKiFPNIQFIVTtHSPLILSSL 264
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-170 |
6.57e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNldeyKPFRRDVgylfqesndcfiCP----------------- 95
Cdd:NF033858 30 VGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAV------------CPriaympqglgknlyptl 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489043565 96 SVLDDVIFslLSR--GKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALD 170
Cdd:NF033858 94 SVFENLDF--FGRlfGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
40-166 |
8.62e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 40 GCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGY---------LFQE----SNdcfICPSVLDDVI-FSL 105
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYvpedrkgegLVLDlsirEN---ITLASLDRLSrGGL 364
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 106 LSRGKDkdgsRAKAEKILRELEIwhlK----DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPT 166
Cdd:COG1129 365 LDRRRE----RALAEEYIKRLRI---KtpspEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
140-194 |
2.00e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.49 E-value: 2.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 140 SGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHD 194
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkrefNTAIIMITHD 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
33-194 |
2.34e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHI----------ELFHhkISNLDEYKPFRRDVGYLFQESNDCF-ICPSVLDDV 101
Cdd:PRK11701 35 LGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrDLYA--LSEAERRRLLRTEWGFVHQHPRDGLrMQVSAGGNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 102 IFSLLSRGKDKDGS-RAKAEKILRELEIWHLK-DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAA 179
Cdd:PRK11701 113 GERLMAVGARHYGDiRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLD 192
|
170
....*....|....*....
gi 489043565 180 ILKSL----DVTQIIVSHD 194
Cdd:PRK11701 193 LLRGLvrelGLAVVIVTHD 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-193 |
2.60e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKS--PCGGHIELFHHKISNLDEYKPFRRDVGYL 84
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAHLGIFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 85 FQESndcFICPSVLDDVIFSLLSRGKDKdgSRAKAEK-ILRELEIWHLKDEIV-----F-------NLSGGEKKLVALAG 151
Cdd:CHL00131 90 FQYP---IEIPGVSNADFLRLAYNSKRK--FQGLPELdPLEFLEIINEKLKLVgmdpsFlsrnvneGFSGGEKKRNEILQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 152 ILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQ---IIVSH 193
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEnsiILITH 209
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-194 |
3.07e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.72 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISnldeYKPfrrdvgylfqesndcficpsvlddvifsllsrgkdk 112
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV----YKP------------------------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 113 dgsrakaEKIlreleiwhlkdeivfNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQ 188
Cdd:cd03222 68 -------QYI---------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTA 125
|
....*.
gi 489043565 189 IIVSHD 194
Cdd:cd03222 126 LVVEHD 131
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-200 |
3.62e-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: 49.94 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERT--LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISnldeykpfrrDVG 82
Cdd:TIGR00957 1285 VEFRNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA----------KIG 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 83 yLFQESNDCFICPSvlDDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKD--------------EIVFNLSGGEKKLVA 148
Cdd:TIGR00957 1355 -LHDLRFKITIIPQ--DPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTfvsalpdkldhecaEGGENLSVGQRQLVC 1431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489043565 149 LAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSHDKEFISD 200
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHRLNTIMD 1485
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
135-210 |
4.82e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 135 IVFNLSGGEKKLVALAGIL----VAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQ---IIVSHDKEFISDvASAMYR 207
Cdd:cd03227 74 TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaqvIVITHLPELAEL-ADKLIH 152
|
...
gi 489043565 208 LTK 210
Cdd:cd03227 153 IKK 155
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
139-206 |
8.26e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.58 E-value: 8.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 139 LSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL----DVTQIIVSHDKEFISDVAS---AMY 206
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqkeNMALVLITHDLALVAEAAHkiiVMY 228
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
34-206 |
1.06e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 47.46 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMA---GLKSpcgghielfhhkisnldeYKPFRRDVgylfqesndcficpsvLDDVIFSllsrGK 110
Cdd:cd03278 26 AIVGPNGSGKSNIIDAIRwvlGEQS------------------AKSLRGEK----------------MSDVIFA----GS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 111 DKDGSRAKAEKIL------REL---------EIWHLKDEIVFN---LSGGEKKLVALA---GILVAEPK-ILLLDEPTTA 168
Cdd:cd03278 68 ETRKPANFAEVTLtfdnsdGRYsiisqgdvsEIIEAPGKKVQRlslLSGGEKALTALAllfAIFRVRPSpFCVLDEVDAA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489043565 169 LDADMQRRIAAILKSL-DVTQ-IIVSHDKEFISdVASAMY 206
Cdd:cd03278 148 LDDANVERFARLLKEFsKETQfIVITHRKGTME-AADRLY 186
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-212 |
1.08e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.07 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 20 FENLNLNaTHKDKIALIGPNGCGKSTLLEIMAGLKSPCGG-------------------HIEL-FHHKISNL-------D 72
Cdd:COG3593 14 IKDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeiEIELtFGSLLSRLlrlllkeE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 73 EYKPFRRDVGYLFQESNDCFicpSVLDDVIFSLLSRGKDK-----DGSRAKAEKILRELEIwHLKDEIVFNLSG---GEK 144
Cdd:COG3593 93 DKEELEEALEELNEELKEAL---KALNELLSEYLKELLDGldlelELSLDELEDLLKSLSL-RIEDGKELPLDRlgsGFQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 145 KLV--ALAGILV-----AEPKILLLDEPTTALDADMQRRIAAILKSLDV--TQIIVS-HDKEFISDV-ASAMYRLTKSG 212
Cdd:COG3593 169 RLIllALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEkpNQVIITtHSPHLLSEVpLENIRRLRRDS 247
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
137-194 |
1.59e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 1.59e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489043565 137 FNLSGG--EKKLVALAgiLVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQ----IIVSHD 194
Cdd:PRK10418 139 FEMSGGmlQRMMIALA--LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRalgmLLVTHD 200
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
138-210 |
1.88e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 1.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 138 NLSGGEKKLVALA---GILVAEPK-ILLLDEPTTALDADMQRRIAAILKSL-DVTQIIV-SHDKEFISdVASAMYRLTK 210
Cdd:pfam02463 1077 LLSGGEKTLVALAlifAIQKYKPApFYLLDEIDAALDDQNVSRVANLLKELsKNAQFIViSLREEMLE-KADKLVGVTM 1154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-199 |
2.36e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNV--CAKIGERTLfenlnlnathkdkiaLIGPNGCGKSTLLEIMAGlkspcggHIELFHHKISN--------LDEYKP 76
Cdd:TIGR00956 77 LKPMdgLIKPGELTV---------------VLGRPGSGCSTLLKTIAS-------NTDGFHIGVEGvitydgitPEEIKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 77 -FRRDVGYLFQesNDC-FICPSVLDDVIFSLLSR-------GKDKDGSRAK-AEKILRELEIWHLKDEIVFN-----LSG 141
Cdd:TIGR00956 135 hYRGDVVYNAE--TDVhFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHiADVYMATYGLSHTRNTKVGNdfvrgVSG 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489043565 142 GEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKsldvTQIIVSHDKEFIS 199
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALK----TSANILDTTPLVA 266
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-177 |
2.40e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 16 ERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGlkspcgghiELFHHKISNLDeykpFRRDVGYLFQESndCFICP 95
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG---------ELSHAETSSVV----IRGSVAYVPQVS--WIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 96 SVLDDVIFsllsrGKDKDGSR----AKAEKILRELEIWHLKD-----EIVFNLSGGEKKLVALAGILVAEPKILLLDEPT 166
Cdd:PLN03232 694 TVRENILF-----GSDFESERywraIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170
....*....|.
gi 489043565 167 TALDADMQRRI 177
Cdd:PLN03232 769 SALDAHVAHQV 779
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-198 |
3.73e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 7 LKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIeLFHHKISNLDEYK-PFRRDVGYLF 85
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI-LFQGKEIDFKSSKeALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 86 QESNDCFICpSVLDDVifsLLSRGK------DKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKI 159
Cdd:PRK10982 80 QELNLVLQR-SVMDNM---WLGRYPtkgmfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489043565 160 LLLDEPTTAL---DADMQRRIAAILKSLDVTQIIVSHDKEFI 198
Cdd:PRK10982 156 VIMDEPTSSLtekEVNHLFTIIRKLKERGCGIVYISHKMEEI 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-196 |
5.60e-06 |
|
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: 46.44 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGE--RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGghiELFHHKIS-NLDEYKPFRRDV 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG---EIQIDGVSwNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQEsndCFICPSV----LDDvifslLSRGKDKDGSRAKAEKILRELeIWHLKDEIVFNL-------SGGEKKLVALA 150
Cdd:TIGR01271 1295 GVIPQK---VFIFSGTfrknLDP-----YEQWSDEEIWKVAEEVGLKSV-IEQFPDKLDFVLvdggyvlSNGHKQLMCLA 1365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489043565 151 GILVAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIVSHDKE 196
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEHRVE 1413
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-198 |
7.99e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 32 KIALIGPNGCGKSTLLEIMAglkspcgghielfhhkisnldeykpfrrdvGYLFQESNDCFICpsvlddvifsllsrgkd 111
Cdd:smart00382 4 VILIVGPPGSGKTTLARALA------------------------------RELGPPGGGVIYI----------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 112 kDGSRAKAEKILRELEIwhLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIV 191
Cdd:smart00382 37 -DGEDILEEVLDQLLLI--IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS 113
|
....*..
gi 489043565 192 SHDKEFI 198
Cdd:smart00382 114 EKNLTVI 120
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-212 |
8.60e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.17 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLK--SPCGGHIELfhhKISNLDEYKPFRR--- 79
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEF---KGKDLLELSPEDRage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 80 DVGYLFQE-------SNDCFICPSV-----------LDDVIFSLLSRGKdkdgsrAKAEKILRELeiwhLKDEIVFNLSG 141
Cdd:PRK09580 79 GIFMAFQYpveipgvSNQFFLQTALnavrsyrgqepLDRFDFQDLMEEK------IALLKMPEDL----LTRSVNVGFSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 142 GEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQ---IIVSHDKEFIS----DVASAMY--RLTKSG 212
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKrsfIIVTHYQRILDyikpDYVHVLYqgRIVKSG 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
40-170 |
1.05e-05 |
|
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: 44.35 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 40 GCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYlfqesndcficpsVLDDvifsllsrgkdkdgsRaKA 119
Cdd:cd03215 36 GNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY-------------VPED---------------R-KR 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489043565 120 EKILRELEIWhlkDEIVFN--LSGGEKKLVALAGILVAEPKILLLDEPTTALD 170
Cdd:cd03215 87 EGLVLDLSVA---ENIALSslLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
139-209 |
1.17e-05 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 44.56 E-value: 1.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 139 LSGGEKKLVALAGILV---AEPK-ILLLDEPTTALDADMQRRIAAILKSL-DVTQIIVSHDKEFISDVASAMYRLT 209
Cdd:cd03272 159 LSGGQKSLVALALIFAiqkCDPApFYLFDEIDAALDAQYRTAVANMIKELsDGAQFITTTFRPELLEVADKFYGVK 234
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
139-199 |
1.33e-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: 43.85 E-value: 1.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 139 LSGGEKKLVALAGILVAEPK--ILLLDEPTTALDADMQRRIAAILKSL---DVTQIIVSHDKEFIS 199
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVLS 153
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-177 |
1.49e-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: 45.29 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 19 LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIelfhhkisnldeykpfrRDVGYLFQESNDCFICPSVL 98
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------------KHSGRISFSPQTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 99 DDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVF-----NLSGGEKKLVALAGILVAEPKILLLDEPTTALDADM 173
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
....
gi 489043565 174 QRRI 177
Cdd:TIGR01271 584 EKEI 587
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-196 |
1.59e-05 |
|
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: 45.39 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKIsnLDEYKPFRRDVGYlfqesndcfiCPSVldDVIFSLLS------ 107
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGY----------CPQF--DAIDDLLTgrehly 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 108 -----RGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILK 182
Cdd:TIGR01257 2035 lyarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170
....*....|....*..
gi 489043565 183 SL---DVTQIIVSHDKE 196
Cdd:TIGR01257 2115 SIireGRAVVLTSHSME 2131
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
133-177 |
1.70e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 1.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489043565 133 DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRI 177
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI 434
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
98-199 |
1.72e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.69 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 98 LDDVIFSLLSRGKDKDGSRAKA--EKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVA---EPKILLLDEPTTALDAD 172
Cdd:pfam13304 194 LADLNLSDLGEGIEKSLLVDDRlrERGLILLENGGGGELPAFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPK 273
|
90 100 110
....*....|....*....|....*....|
gi 489043565 173 MQRRIAAILKSLDV--TQIIV-SHDKEFIS 199
Cdd:pfam13304 274 LLRRLLELLKELSRngAQLILtTHSPLLLD 303
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-196 |
2.13e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.07 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGE--RTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSpCGGHIELfhHKIS-NLDEYKPFRRDV 81
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI--DGVSwNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 82 GYLFQEsndCFICPSVLDDvifSLLSRGKDKDGSRAK-AEKILRELEIWHLKDEIVFNL-------SGGEKKLVALAGIL 153
Cdd:cd03289 80 GVIPQK---VFIFSGTFRK---NLDPYGKWSDEEIWKvAEEVGLKSVIEQFPGQLDFVLvdggcvlSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 154 VAEPKILLLDEPTTALDADMQRRIAAILKS--LDVTQIIVSHDKE 196
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEHRIE 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-198 |
2.36e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 34 ALIGPNGCGKSTLLEIMAGLKSPCGGHIEL------FHHKISNLDEykpfrrDVGYLFQESNdcfICP--SVLDDVIFSL 105
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIdgqemrFASTTAALAA------GVAIIYQELH---LVPemTVAENLYLGQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 106 L-SRGKDKDGSRAKAEkILRELEiwHLKDEI-----VFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAA 179
Cdd:PRK11288 105 LpHKGGIVNRRLLNYE-AREQLE--HLGVDIdpdtpLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFR 181
|
170 180
....*....|....*....|..
gi 489043565 180 ILKSL--DVTQII-VSHDKEFI 198
Cdd:PRK11288 182 VIRELraEGRVILyVSHRMEEI 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-198 |
2.88e-05 |
|
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: 43.47 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 22 NLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHI---ELFHHKISNLDEYKPFRRDVGYLFQESndCFICPSVL 98
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKP--WLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 99 DDVIFsllsrGKDKDGSRAKAE----KILRELEIWHLKD-----EIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTAL 169
Cdd:cd03290 97 ENITF-----GSPFNKQRYKAVtdacSLQPDIDLLPFGDqteigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|....
gi 489043565 170 DAD-----MQRRIAAILKSLDVTQIIVSHDKEFI 198
Cdd:cd03290 172 DIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-209 |
4.31e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 112 KDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLDVTQIIV 191
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATV 197
|
90
....*....|....*...
gi 489043565 192 SHDKEFISDVASAMYRLT 209
Cdd:NF000106 198 LLTTQYMEEAEQLAHELT 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
137-203 |
4.69e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 4.69e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489043565 137 FNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSLD----VTQIIVSHDKEFISDVAS 203
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqnnnTTILLISHDLQMLSQWAD 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-195 |
4.79e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 4.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489043565 139 LSGGEKKLVALA---GILVAEPK-ILLLDEPTTALDADMQRRIAAILKSL-DVTQ-IIVSHDK 195
Cdd:TIGR02168 1090 LSGGEKALTALAllfAIFKVKPApFCILDEVDAPLDDANVERFANLLKEFsKNTQfIVITHNK 1152
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-193 |
5.50e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 31 DKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVGYLFQEsndcficPSVLDDVI-FSL--LS 107
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG-LMDLRKVLGIIPQA-------PVLFSGTVrFNLdpFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 108 RGKDKDgsrakaekILRELEIWHLKDEI----------VF----NLSGGEKKLVALAGILVAEPKILLLDEPTTAL---- 169
Cdd:PLN03130 1338 EHNDAD--------LWESLERAHLKDVIrrnslgldaeVSeageNFSVGQRQLLSLARALLRRSKILVLDEATAAVdvrt 1409
|
170 180
....*....|....*....|....
gi 489043565 170 DADMQRRIAAILKSldVTQIIVSH 193
Cdd:PLN03130 1410 DALIQKTIREEFKS--CTMLIIAH 1431
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-212 |
6.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 102 IFSLLSRGKdKDGSRAKAEK-ILRELEIWHLKDEIVFNLSGGEK-------KLvALAGILVAEPKILLLDEPTTALDADM 173
Cdd:PRK03918 752 IFEELTEGK-YSGVRVKAEEnKVKLFVVYQGKERPLTFLSGGERialglafRL-ALSLYLAGNIPLLILDEPTPFLDEER 829
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489043565 174 QRRIAAILKSL--DVTQ-IIVSHDKEfISDVASAMYRLTKSG 212
Cdd:PRK03918 830 RRKLVDIMERYlrKIPQvIIVSHDEE-LKDAADYVIRVSLEG 870
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
23-199 |
8.23e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.72 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 23 LNLNATHKD--KIALI-GPNGCGKSTLLEIMAGLKSPcgghIELFHHKISNLdeYKPFRRDVGY---------------- 83
Cdd:COG1106 19 LSMVASGLRllRVNLIyGANASGKSNLLEALYFLRNL----VLNSSQPGDKL--VEPFLLDSESknepsefeilflldgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 84 ------------------------------LFQESNDCFICPSVLDDVIFSLLSRGKDKDGSRAKAEKILRELEI----- 128
Cdd:COG1106 93 ryeygfeldkeriisewlyflstaaqlnvpLLSPLYDWFDNNISLDTSSDGLTLLLKEDESLKEELLELLKIADPgiedi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 129 -----------------WHLKDEIVFNL---SGGEKKLVALAGILV---AEPKILLLDEPTTALDADMQRRIAAILKSLD 185
Cdd:COG1106 173 eveeeeiedlverklifKHKGGNVPLPLseeSDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKLFLDLA 252
|
250
....*....|....*...
gi 489043565 186 V---TQIIV-SHDKEFIS 199
Cdd:COG1106 253 NknnAQLIFtTHSTELLD 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-201 |
1.11e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 15 GERTLFENLNLNATHKDKIALIGPNGCGKSTLLEIMAG-LKSPCGGHIELfhhkisnldeykpfRRDVGYLFQESndCFI 93
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI--------------RGTVAYVPQVS--WIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 94 CPSVLDDVIFsllsrgkdkdGSRAKAEKILRELEIWHLKDEIVF--------------NLSGGEKKLVALAGILVAEPKI 159
Cdd:PLN03130 692 NATVRDNILF----------GSPFDPERYERAIDVTALQHDLDLlpggdlteigergvNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489043565 160 LLLDEPTTALDADMQRRI--AAILKSL-DVTQIIVSHDKEFISDV 201
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVfdKCIKDELrGKTRVLVTNQLHFLSQV 806
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-184 |
1.12e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 5 ISLKNVCAKIGERTLFENLNLNATHKDKIALI-------------GPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNL 71
Cdd:PRK09700 251 NAMKENVSNLAHETVFEVRNVTSRDRKKVRDIsfsvcrgeilgfaGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 72 DEYKPF----------RRDVGYL--FQESNDCFICPSVLDDVIFSLLSRGKDKDGSR-AKAEKILRELEIWHLKDEIVfN 138
Cdd:PRK09700 331 SPLDAVkkgmayitesRRDNGFFpnFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRtAENQRELLALKCHSVNQNIT-E 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489043565 139 LSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL 455
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
138-170 |
1.23e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 1.23e-04
10 20 30
....*....|....*....|....*....|...
gi 489043565 138 NLSGGEKKLVALAGILVAEPKILLLDEPTTALD 170
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-177 |
1.23e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.77 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 19 LFENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIelfhhkisnldeykpfrRDVGYLFQESNDCFICPSVL 98
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------------KHSGRISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 99 DDVIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVF-----NLSGGEKKLVALAGILVAEPKILLLDEPTTALDADM 173
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
....
gi 489043565 174 QRRI 177
Cdd:cd03291 195 EKEI 198
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
132-212 |
1.26e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 42.42 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 132 KDEIVFNLSGGEKKLVALAGIL--------VAEPKILLLDEPTTALDADMQRRIAAILKSL--DVTQIIV-SHDKEFISD 200
Cdd:COG4694 485 DAKPAKTLSEGEKTAIALAYFLaelegdenDLKKKIVVIDDPVSSLDSNHRFAVASLLKELskKAKQVIVlTHNLYFLKE 564
|
90
....*....|..
gi 489043565 201 VASAMYRLTKSG 212
Cdd:COG4694 565 LRDLADEDNKKK 576
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-200 |
1.39e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.27 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 31 DKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDeYKPFRRDVGYLFQESndcficpsvlddVIFSLLSRGK 110
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRRVLSIIPQSP------------VLFSGTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 111 DKDGSRAKAEKILRELEIWHLKDEI----------VF----NLSGGEKKLVALAGILVAEPKILLLDEPTTAL----DAD 172
Cdd:PLN03232 1330 IDPFSEHNDADLWEALERAHIKDVIdrnpfgldaeVSeggeNFSVGQRQLLSLARALLRRSKILVLDEATASVdvrtDSL 1409
|
170 180
....*....|....*....|....*...
gi 489043565 173 MQRRIAAILKSldVTQIIVSHDKEFISD 200
Cdd:PLN03232 1410 IQRTIREEFKS--CTMLVIAHRLNTIID 1435
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
138-212 |
1.67e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 138 NLSGGEKKLVALA------GILVAEPKILLLDEPTTALDADMQRRIAAILK-----SLDVTQ-IIVSHDKEFISdVASAM 205
Cdd:PRK01156 801 SLSGGEKTAVAFAlrvavaQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEyslkdSSDIPQvIMISHHRELLS-VADVA 879
|
....*..
gi 489043565 206 YRLTKSG 212
Cdd:PRK01156 880 YEVKKSS 886
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
138-177 |
1.80e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489043565 138 NLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRI 177
Cdd:PTZ00243 782 NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-202 |
2.33e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 2.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489043565 133 DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTAL-DADMQRRIAAI--LKSLDVTQIIVSHDKEFISDVA 202
Cdd:NF040905 134 DTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLleLKAQGITSIIISHKLNEIRRVA 206
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-170 |
2.65e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 2.65e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489043565 133 DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALD 170
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-210 |
3.13e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 139 LSGGEKKLVAL---AGI--LVAE---------PkiLLLDEPTTALDADMQRRIAAILKS---LDVTQII-VSHDKEFIsD 200
Cdd:PRK02224 782 LSGGERALFNLslrCAIyrLLAEgiegdaplpP--LILDEPTVFLDSGHVSQLVDLVESmrrLGVEQIVvVSHDDELV-G 858
|
90
....*....|
gi 489043565 201 VASAMYRLTK 210
Cdd:PRK02224 859 AADDLVRVEK 868
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-184 |
3.65e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 35 LIGPNGCGKSTLLEIMAGLKSP---CGGHIELFHHKisnLDEYKPfRRDVGYLFQesNDCFI----CPSVLD-------- 99
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPslkVSGEITYNGYR---LNEFVP-RKTSAYISQ--NDVHVgvmtVKETLDfsarcqgv 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 100 ----DVIFSLLSRGKDKdGSRAKAE-----------------------KILrELEIWH---LKDEIVFNLSGGEKKLVAL 149
Cdd:PLN03140 270 gtryDLLSELARREKDA-GIFPEAEvdlfmkatamegvksslitdytlKIL-GLDICKdtiVGDEMIRGISGGQKKRVTT 347
|
170 180 190
....*....|....*....|....*....|....*
gi 489043565 150 AGILVAEPKILLLDEPTTALDADMQRRIAAILKSL 184
Cdd:PLN03140 348 GEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI 382
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
139-199 |
4.27e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.93 E-value: 4.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489043565 139 LSGGEKKLVALAGILVAEPK--ILLLDEPTTAL-DADMQRRIAAI--LKSLDVTQIIVSHDKEFIS 199
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhPRDNDRLIETLkrLRDLGNTVLVVEHDEDTIR 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
36-170 |
7.00e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 36 IGPNGCGKSTLLEIMAGLKSPCGGHIELFHHKI--SNLDEykpfRRDVGYLFQEsndcficpsvlddviFSL-------- 105
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIAT----RRRVGYMSQA---------------FSLygeltvrq 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489043565 106 -------LSRGKDKDGSRAKAEKILR-ELEiwHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALD 170
Cdd:NF033858 359 nlelharLFHLPAAEIAARVAEMLERfDLA--DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
139-210 |
7.51e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 7.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489043565 139 LSGGEKKLVALAGIL----VAEPKILLLDEPTTALDADMQRRIAAILKSLDV--TQIIVSHDKEFISDVASAMYRLTK 210
Cdd:cd03239 95 LSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKhtSQFIVITLKKEMFENADKLIGVLF 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
117-192 |
9.38e-04 |
|
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: 39.42 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 117 AKAEKILRELEIWHLK----DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADMQRRIAAILKSL---DVTQI 189
Cdd:TIGR02633 378 AELQIIGSAIQRLKVKtaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaqeGVAII 457
|
...
gi 489043565 190 IVS 192
Cdd:TIGR02633 458 VVS 460
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-202 |
1.33e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 21 ENLNLNATHKDKIALIGPNGCGKSTLLEIMAGLKSPCGGHIELfHHKISNLdeykpfRRDVGYLFQESNdcficpsvLDD 100
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDR-NGEVSVI------AISAGLSGQLTG--------IEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 101 VIFSLLSRGKDKDGSRAKAEKILRELEIWHLKDEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADM-QRRIAA 179
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFaQKCLDK 185
|
170 180
....*....|....*....|....*....
gi 489043565 180 I--LKSLDVTQIIVSHD----KEFISDVA 202
Cdd:PRK13546 186 IyeFKEQNKTIFFVSHNlgqvRQFCTKIA 214
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
7-57 |
3.72e-03 |
|
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213253 [Multi-domain] Cd Length: 218 Bit Score: 37.02 E-value: 3.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489043565 7 LKNVCAKIGERTLF--ENLNLNATHKDKIALIGPNGCGKSTLLE------IMAGLKSPC 57
Cdd:cd03286 5 LRHPCLNASTASSFvpNDVDLGATSPRILVLTGPNMGGKSTLLRtvclavIMAQMGMDV 63
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
40-180 |
3.94e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 37.70 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 40 GCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVGYLFQESNDCFICP--SVLDDVIFSLLSRGK------- 110
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPdmSVAENLILGRYRRPPfsrggfl 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489043565 111 DKDGSRAKAEKILRELEIwhlK----DEIVFNLSGG-EKKLVaLAGILVAEPKILLLDEPTTALDadmqrrIAAI 180
Cdd:COG3845 374 DRKAIRAFAEELIEEFDV---RtpgpDTPARSLSGGnQQKVI-LARELSRDPKLLIAAQPTRGLD------VGAI 438
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
40-194 |
4.33e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 37.58 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 40 GCGKSTLLEIMAGLKSPCGGHIELFHHKISNLDEYKPFRRDVgylfqesndcFICP------------SVLDDVIFS--- 104
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGI----------MLCPedrkaegiipvhSVADNINISarr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 105 -------LLSRGKDKDgsraKAEKILRELEIwhlK----DEIVFNLSGGEKKLVALAGILVAEPKILLLDEPTTALDADM 173
Cdd:PRK11288 359 hhlragcLINNRWEAE----NADRFIRSLNI---KtpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180
....*....|....*....|....
gi 489043565 174 QRRIAAILKSL---DVTQIIVSHD 194
Cdd:PRK11288 432 KHEIYNVIYELaaqGVAVLFVSSD 455
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
33-193 |
6.54e-03 |
|
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410891 [Multi-domain] Cd Length: 231 Bit Score: 36.39 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 33 IALIGPNGCGKSTLLEIMAglkspcgghielfHHKISNLDEykpfrrDVGYLFQESNDcficpsvlDDVIFSLLSRGKDK 112
Cdd:cd19483 1 VTIGAGSGIGKSTIVRELA-------------YHLITEHGE------KVGIISLEESV--------EETAKGLAGKHLGK 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043565 113 DGSRAKAEKILRELEIWHLKDE-------IVFNLSGGE---------KKLVALAGIlvaepKILLLD------------E 164
Cdd:cd19483 54 PEPLELPRDDITEEEEDDAFDNelgsgrfFLYDHFGSLdwdnlkekiRYMVKVLGC-----KVIVLDhltilvsgldssD 128
|
170 180
....*....|....*....|....*....
gi 489043565 165 PTTALDADMQRrIAAILKSLDVTQIIVSH 193
Cdd:cd19483 129 ERKELDEIMTE-LAALVKELGVTIILVSH 156
|
|
| |
