|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-180 |
1.41e-41 |
|
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: 141.85 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 1 MDLAIKGksLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING------------QVS 68
Cdd:COG4133 1 MMLEAEN--LSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 69 YAPDHLPKSITLTVQQYLLFVEQLYEVQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEP 148
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 1248686454 149 FSGLDKQSVSVLTSILK-YLKQYATVILTSHDE 180
Cdd:COG4133 159 FTALDAAGVALLAELIAaHLARGGAVLLTTHQP 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-182 |
6.49e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.27 E-value: 6.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING------------QVSYAPDHLP 75
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 76 KSITLTVQQYLLFVEQLYEVQHSCFA--LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:COG1131 84 LYPDLTVRENLRFFARLYGLPRKEARerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190
....*....|....*....|....*....|..
gi 1248686454 154 KQSVSVLTSILKYLKQY-ATVILTSH--DEAQ 182
Cdd:COG1131 164 PEARRELWELLRELAAEgKTVLLSTHylEEAE 195
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-179 |
1.72e-34 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 124.58 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING------------QVSYAPD 72
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 73 --HLPKsiTLTVQQYLLFVEQLYEVQHS--CFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEP 148
Cdd:COG4555 82 erGLYD--RLTVRENIRYFAELYGLFDEelKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190
....*....|....*....|....*....|..
gi 1248686454 149 FSGLDKQSVSVLTSILKYLKQY-ATVILTSHD 179
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEgKTVLFSSHI 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-182 |
3.61e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 121.35 E-value: 3.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ------------VSYAPD 72
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkepeevkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 73 HLPKSITLTVQQYLLFveqlyevqhscfalddliqrfhieaflsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGL 152
Cdd:cd03230 81 EPSLYENLTVRENLKL----------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190
....*....|....*....|....*....|...
gi 1248686454 153 DKQSVSVLTSILK-YLKQYATVILTSH--DEAQ 182
Cdd:cd03230 127 DPESRREFWELLReLKKEGKTILLSSHilEEAE 159
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-178 |
2.01e-30 |
|
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: 113.14 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-QVSYAPDH----LPKSIT 79
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkPLDIAARNrigyLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 80 L----TVQQYLLFVEQLYEVQHSCFA--LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:cd03269 81 LypkmKVIDQLVYLAQLKGLKKEEARrrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180
....*....|....*....|....*.
gi 1248686454 154 KQSVSVLTSILKYLK-QYATVILTSH 178
Cdd:cd03269 161 PVNVELLKDVIRELArAGKTVILSTH 186
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-179 |
2.10e-28 |
|
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: 107.62 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--------VSYAPDH--LPKS 77
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRrsIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 78 ITLTVQQYLL-----FVEQLYEVQHSCFAL-DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSG 151
Cdd:cd03235 83 FPISVRDVVLmglygHKGLFRRLSKADKAKvDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180
....*....|....*....|....*....
gi 1248686454 152 LDKQSVSVLTSILKYLKQY-ATVILTSHD 179
Cdd:cd03235 163 VDPKTQEDIYELLRELRREgMTILVVTHD 191
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-179 |
5.02e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.48 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 1 MDLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--------VSYAP- 71
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 72 -DHLPKSITLTVQQyllFVEQLYEVQHSCF---------ALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQAD 141
Cdd:COG1121 83 rAEVDWDFPITVRD---VVLMGRYGRRGLFrrpsradreAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1248686454 142 IYILDEPFSGLDKQSVSVLTSILKYLKQY-ATVILTSHD 179
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHD 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-181 |
1.10e-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: 106.05 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKV--INGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDHLPKSI------ 78
Cdd:cd03263 4 RNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLgycpqf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 79 -----TLTVQQYLLFVEQL--YEVQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSG 151
Cdd:cd03263 84 dalfdELTVREHLRFYARLkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190
....*....|....*....|....*....|..
gi 1248686454 152 LDKQSVSVLTSILKYLKQYATVILTSH--DEA 181
Cdd:cd03263 164 LDPASRRAIWDLILEVRKGRSIILTTHsmDEA 195
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-179 |
1.21e-26 |
|
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: 101.55 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQvsyapdHLPKSITLTVQQYLL 87
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK------DIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 88 FVEQLyevqhscfalddliqrfhieaflsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSV-SVLTSILKY 166
Cdd:cd00267 77 YVPQL------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASReRLLELLREL 126
|
170
....*....|...
gi 1248686454 167 LKQYATVILTSHD 179
Cdd:cd00267 127 AEEGRTVIIVTHD 139
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-179 |
1.67e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.81 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQvSYAPDHL------------- 74
Cdd:COG4152 5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-PLDPEDRrrigylpeergly 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 75 PKsitLTVQQYLLFVEQLY-----EVQHscfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPF 149
Cdd:COG4152 84 PK---MKVGEQLVYLARLKglskaEAKR---RADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 1248686454 150 SGLDKQSVSVLTSILKYLK-QYATVILTSHD 179
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAaKGTTVIFSSHQ 188
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-181 |
1.78e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING--QVSYAPDH--LPKSITLTVQQYL---L 87
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRseVPDSLPLTVRDLVamgR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 88 FVEQLYEVQHSC---FALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSIL 164
Cdd:NF040873 83 WARRGLWRRLTRddrAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170
....*....|....*...
gi 1248686454 165 KYL-KQYATVILTSHDEA 181
Cdd:NF040873 163 AEEhARGATVVVVTHDLE 180
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-185 |
3.07e-22 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 93.22 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 12 KVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-QVSYAPDHLPKSITLTVQQY----- 85
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGyDVVREPRKVRRSIGIVPQYAsvded 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 86 ------LLFVEQLYEVQHSCFA--LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSV 157
Cdd:TIGR01188 81 ltgrenLEMMGRLYGLPKDEAEerAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190
....*....|....*....|....*....|.
gi 1248686454 158 SVLTSILKYLKQYA-TVILTSH--DEAQHYG 185
Cdd:TIGR01188 161 RAIWDYIRALKEEGvTILLTTHymEEADKLC 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-179 |
4.20e-22 |
|
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: 90.19 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQvsyaPDHLPKSITLTvqQYLLFVEQlye 94
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK----DLASLSPKELA--RKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 95 vqhscfalddLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD-KQSVSVLtSILKYLKQYA-- 171
Cdd:cd03214 81 ----------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiAHQIELL-ELLRRLARERgk 149
|
....*...
gi 1248686454 172 TVILTSHD 179
Cdd:cd03214 150 TVVMVLHD 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
17-179 |
1.18e-21 |
|
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: 89.83 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 17 QVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQV--SYAPDHLPKSI------------TLTV 82
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltKLSLKELRRKVglvfqnpddqffGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 QQYLLF-VEQLY----EVQHscfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSV 157
Cdd:cd03225 94 EEEVAFgLENLGlpeeEIEE---RVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180
....*....|....*....|...
gi 1248686454 158 SVLTSILKYLK-QYATVILTSHD 179
Cdd:cd03225 171 RELLELLKKLKaEGKTIIIVTHD 193
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-179 |
1.96e-21 |
|
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: 89.17 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNqSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ------------VSYAPD 72
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 73 HLPKSITLTVQQYLLFVEQLYEVQHSCF--ALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFS 150
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVkaRVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180
....*....|....*....|....*....
gi 1248686454 151 GLDKQSVSVLTSILKYLKQYATVILTSHD 179
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHI 188
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-179 |
2.15e-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: 89.70 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYA--PDHLpKSIT------------LTVQQYLL 87
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrrKKFL-RRIGvvfgqktqlwwdLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 88 FVEQLYEVQHSCFA--LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDkqsVSVLTSILK 165
Cdd:cd03267 118 LLAAIYDLPPARFKkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD---VVAQENIRN 194
|
170
....*....|....*....
gi 1248686454 166 YLKQY-----ATVILTSHD 179
Cdd:cd03267 195 FLKEYnrergTTVLLTSHY 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-181 |
2.41e-21 |
|
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: 89.12 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 10 LTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDHLpKSITLTVQQYLLF 88
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdVTGVPPER-RNIGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 89 ----VEQlyevqHSCFAL--------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFS 150
Cdd:cd03259 85 phltVAE-----NIAFGLklrgvpkaeirarvRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1248686454 151 GLDKQS-VSVLTSILKYLKQY-ATVILTSHD--EA 181
Cdd:cd03259 160 ALDAKLrEELREELKELQRELgITTIYVTHDqeEA 194
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-179 |
4.26e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.18 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 18 VIFSDMTIEFPNQS------------IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLPKSITLTVQQY 85
Cdd:PRK13409 341 VEYPDLTKKLGDFSleveggeiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 86 LLFVEQLYevqHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD-KQSVSVLTSIL 164
Cdd:PRK13409 421 LRSITDDL---GSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDvEQRLAVAKAIR 497
|
170
....*....|....*.
gi 1248686454 165 KYLKQY-ATVILTSHD 179
Cdd:PRK13409 498 RIAEEReATALVVDHD 513
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-178 |
1.34e-20 |
|
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: 86.89 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ----VSYAPDHLPKSIT- 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkNIEALRRIGALIEa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 80 ------LTVQQYLLFVEQLYEVQHScfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:cd03268 81 pgfypnLTARENLRLLARLLGIRKK--RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180
....*....|....*....|....*.
gi 1248686454 154 KQSVSVLTSILKYLKQY-ATVILTSH 178
Cdd:cd03268 159 PDGIKELRELILSLRDQgITVLISSH 184
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-179 |
1.44e-20 |
|
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: 86.97 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 14 INGQVIFSDMTIEFP-NQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQV---SYAPDHLP---KSITLTVQQYL 86
Cdd:cd03297 6 IEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdSRKKINLPpqqRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 87 LFvEQLYEVQHSCFAL------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDk 154
Cdd:cd03297 86 LF-PHLNVRENLAFGLkrkrnredrisvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD- 163
|
170 180 190
....*....|....*....|....*....|
gi 1248686454 155 qsVSVLTSILKYLKQYAT-----VILTSHD 179
Cdd:cd03297 164 --RALRLQLLPELKQIKKnlnipVIFVTHD 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-179 |
2.10e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.61 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYA--PDHLpKSIT------------LTVQQYLLFVEQLYEVQH 97
Cdd:COG4586 50 IVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKrrKEFA-RRIGvvfgqrsqlwwdLPAIDSFRLLKAIYRIPD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 98 SCFA--LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDkqsVSVLTSILKYLKQY----- 170
Cdd:COG4586 129 AEYKkrLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD---VVSKEAIREFLKEYnrerg 205
|
....*....
gi 1248686454 171 ATVILTSHD 179
Cdd:COG4586 206 TTILLTSHD 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-179 |
2.30e-20 |
|
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: 87.08 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 26 EFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTI-NGQVSYAPDHLPKSITLTVQQYLLFVEQ-LYEvqHSCFAlD 103
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIeLDTVSYKPQYIKADYEGTVRDLLSSITKdFYT--HPYFK-T 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248686454 104 DLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKY--LKQYATVILTSHD 179
Cdd:cd03237 98 EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRfaENNEKTAFVVEHD 175
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
32-182 |
2.76e-20 |
|
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: 86.27 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-QVSYAPDHLPKSI-----------TLTVQQYLLFVEQLYEVQHSC 99
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLgfvsdstglydRLTARENLEYFAGLYGLKGDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 100 F--ALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLK-QYATVILT 176
Cdd:cd03266 113 LtaRLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRaLGKCILFS 192
|
....*...
gi 1248686454 177 SH--DEAQ 182
Cdd:cd03266 193 THimQEVE 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-150 |
3.15e-20 |
|
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: 84.24 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPD--HLPKSITLTVQQYLLF-----VEQLYEVQHSCFA--- 101
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkSLRKEIGYVFQDPQLFprltvRENLRLGLLLKGLskr 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1248686454 102 -----LDDLIQRFHIEAFLSQPI----KQCSKGTQQKLNLIQCLLKQADIYILDEPFS 150
Cdd:pfam00005 93 ekdarAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-179 |
3.36e-20 |
|
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: 89.84 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVI--FSDMTIEFPNQS------------IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDH 73
Cdd:COG1245 330 HAPRREKEEETLveYPDLTKSYGGFSleveggeiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQY 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 LPKSITLTVQQYLLFVeqLYEVQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:COG1245 410 ISPDYDGTVEEFLRSA--NTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180
....*....|....*....|....*...
gi 1248686454 154 -KQSVSVLTSILKYLKQY-ATVILTSHD 179
Cdd:COG1245 488 vEQRLAVAKAIRRFAENRgKTAMVVDHD 515
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-178 |
5.09e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.10 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 7 GKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDHLPKSI------- 78
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTpLAEQRDEPHENIlylghlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 79 ----TLTVQQYLLFVEQLYevQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDK 154
Cdd:TIGR01189 83 glkpELSALENLHFWAAIH--GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*
gi 1248686454 155 QSVSVLTSILK-YLKQYATVILTSH 178
Cdd:TIGR01189 161 AGVALLAGLLRaHLARGGIVLLTTH 185
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-178 |
6.77e-20 |
|
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: 83.97 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQV--SYAPDHLPKSITLTVQQYLLFveql 92
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrDLDLESLRKNIAYVPQDPFLF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 yevqhscfalDDLIqRFHIeafLsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYAT 172
Cdd:cd03228 89 ----------SGTI-RENI---L-------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKT 147
|
....*.
gi 1248686454 173 VILTSH 178
Cdd:cd03228 148 VIVIAH 153
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-179 |
7.29e-20 |
|
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: 84.16 E-value: 7.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLP----KSITL 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 81 TVQQYLLFveqlyevqhscfalddliqrFHIEAF--LSQPIkqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVS 158
Cdd:cd03229 81 VFQDFALF--------------------PHLTVLenIALGL---SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180
....*....|....*....|...
gi 1248686454 159 VLTSILKYLKQYA--TVILTSHD 179
Cdd:cd03229 138 EVRALLKSLQAQLgiTVVLVTHD 160
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-179 |
1.11e-19 |
|
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: 85.48 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 4 AIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-------------VSYA 70
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 71 PDHLPKSITLTVQQ--------YLLFVEQLYEVQHScfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADI 142
Cdd:COG1120 81 PQEPPAPFGLTVRElvalgrypHLGLFGRPSAEDRE--AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1248686454 143 YILDEPFSGLD-KQSVSVLtSILKYLKQYA--TVILTSHD 179
Cdd:COG1120 159 LLLDEPTSHLDlAHQLEVL-ELLRRLARERgrTVVMVLHD 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-181 |
2.37e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 81.73 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYApdhlpksitltvqq 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 85 yllFVEQLyevqhscfalddliqrfhieaflsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSIL 164
Cdd:cd03221 67 ---YFEQL------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170
....*....|....*..
gi 1248686454 165 KYLKQyaTVILTSHDEA 181
Cdd:cd03221 114 KEYPG--TVILVSHDRY 128
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-179 |
3.17e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING--QVSYAPDHLPKSITLTVQQY 85
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 86 LLFV-------------------------EQLYEVQHSCFALD---------DLIQRFHI-EAFLSQPIKQCSKGTQQKL 130
Cdd:COG0488 82 VLDGdaelraleaeleeleaklaepdedlERLAELQEEFEALGgweaearaeEILSGLGFpEEDLDRPVSELSGGWRRRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1248686454 131 NLIQCLLKQADIYILDEPFSGLDKQSVSVLTsilKYLKQYA-TVILTSHD 179
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLE---EFLKNYPgTVLVVSHD 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-178 |
3.81e-19 |
|
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: 82.93 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDHLPKSI-------- 78
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLlylghapg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 79 ---TLTVQQYLLFveqlYEVQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQ 155
Cdd:cd03231 84 iktTLSVLENLRF----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....
gi 1248686454 156 SVSVLTSILK-YLKQYATVILTSH 178
Cdd:cd03231 160 GVARFAEAMAgHCARGGMVVLTTH 183
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-179 |
2.15e-18 |
|
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: 81.61 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQV--SYAPDHLPKSITLTVQ----QylLF 88
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitKKNLRELRRKVGLVFQnpddQ--LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 89 ---VEQlyEVqhsCFAL--------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLiqcllkqA-------DIYI 144
Cdd:COG1122 90 aptVEE--DV---AFGPenlglpreeirervEEALELVGLEHLADRPPHELSGGQKQRVAI-------AgvlamepEVLV 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1248686454 145 LDEPFSGLDKQSVSVLTSILKYL-KQYATVILTSHD 179
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHD 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-183 |
2.39e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.62 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ------VSYAPD-----HLP--KSItLTVQQYLLFVEQLYEVQHS 98
Cdd:PRK13538 29 LVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrDEYHQDllylgHQPgiKTE-LTALENLRFYQRLHGPGDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 99 cFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSIL-KYLKQYATVILTS 177
Cdd:PRK13538 108 -EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaQHAEQGGMVILTT 186
|
....*.
gi 1248686454 178 HDEAQH 183
Cdd:PRK13538 187 HQDLPV 192
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-182 |
9.86e-18 |
|
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: 79.50 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSY--------APDhlpksitLTVQQYLLFVE 90
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSllglgggfNPE-------LTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 91 QLYEVQHSCfaLDDLIQRFH----IEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD----KQSVSVLTS 162
Cdd:cd03220 110 RLLGLSRKE--IDEKIDEIIefseLGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafqEKCQRRLRE 187
|
170 180
....*....|....*....|
gi 1248686454 163 IlkyLKQYATVILTSHDEAQ 182
Cdd:cd03220 188 L---LKQGKTVILVSHDPSS 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-182 |
3.20e-17 |
|
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: 78.18 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-QVSYAPDHLPKSITLTVQ 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 84 -----------QYLLFVEQLYEVQHSCFA--LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFS 150
Cdd:cd03265 81 dlsvddeltgwENLYIHARLYGVPGAERRerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1248686454 151 GLDKQSVSVLTSILKYLK--QYATVILTSH--DEAQ 182
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKeeFGMTILLTTHymEEAE 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-178 |
4.30e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 1 MDLAikGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHlPKSIT- 79
Cdd:PRK13539 1 MMLE--GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-AEACHy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 80 ----------LTVQQYLLFVEQLY-----EVQHS--CFALDDLiqrFHIeaflsqPIKQCSKGTQQKLNLIQCLLKQADI 142
Cdd:PRK13539 78 lghrnamkpaLTVAENLEFWAAFLggeelDIAAAleAVGLAPL---AHL------PFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1248686454 143 YILDEPFSGLDKQSVSVLTS-ILKYLKQYATVILTSH 178
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAElIRAHLAQGGIVIAATH 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-180 |
4.98e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 77.30 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 17 QVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQvsyapdHLPKSITlTVQQYLLFVEQ----- 91
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ------SIKKDLC-TYQKQLCFVGHrsgin 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 92 ---------LYEVQHSCFAL--DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSV-SV 159
Cdd:PRK13540 87 pyltlrencLYDIHFSPGAVgiTELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLlTI 166
|
170 180
....*....|....*....|.
gi 1248686454 160 LTSILKYLKQYATVILTSHDE 180
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHQD 187
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-181 |
6.66e-17 |
|
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: 77.13 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEfPNQsIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHlpkSITLTVQQYLLF--------VEQLY 93
Cdd:cd03293 24 SLSVE-EGE-FVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGYVFQQDALLpwltvldnVALGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 94 EVQHSCFAL-----DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVL-TSILKYL 167
Cdd:cd03293 99 ELQGVPKAEareraEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIW 178
|
170
....*....|....*..
gi 1248686454 168 KQY-ATVILTSHD--EA 181
Cdd:cd03293 179 RETgKTVLLVTHDidEA 195
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-181 |
1.20e-16 |
|
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: 79.42 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLFV--- 89
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlRDLDEDDLRRRIAVVPQRPHLFDttl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 90 -------------EQLYE----VQhscfaLDDLIQRFH--IEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFS 150
Cdd:COG4987 426 renlrlarpdatdEELWAalerVG-----LGDWLAALPdgLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|..
gi 1248686454 151 GLDKQSV-SVLTSILKYLKQyATVILTSHDEA 181
Cdd:COG4987 501 GLDAATEqALLADLLEALAG-RTVLLITHRLA 531
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-181 |
1.91e-16 |
|
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: 75.75 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPdhlPK--SITLTVQQ 84
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdVTDLP---PKdrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 85 YLLFVEQ-LYEvqHSCFAL-------DDLIQRFH-------IEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPF 149
Cdd:cd03301 81 YALYPHMtVYD--NIAFGLklrkvpkDEIDERVRevaellqIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1248686454 150 SGLD-KQSVSVLTSILKYLKQY-ATVILTSHD--EA 181
Cdd:cd03301 159 SNLDaKLRVQMRAELKRLQQRLgTTTIYVTHDqvEA 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-178 |
2.37e-16 |
|
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: 76.04 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 10 LTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDH---------LPK--S 77
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQdITKLPMHkrarlgigyLPQeaS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 78 I--TLTVQQYLLFV----EQLYEVQHScfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSG 151
Cdd:cd03218 86 IfrKLTVEENILAVleirGLSKKEREE--KLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180
....*....|....*....|....*...
gi 1248686454 152 LDKQSVSVLTSILKYLKQYATVIL-TSH 178
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLiTDH 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-179 |
3.55e-16 |
|
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: 77.95 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLF---- 88
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlRQIDPASLRRQIGVVLQDVFLFsgti 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 89 ------------VEQLYEV-QHSCfaLDDLIQRFH--IEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:COG2274 566 renitlgdpdatDEEIIEAaRLAG--LHDFIEALPmgYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180
....*....|....*....|....*.
gi 1248686454 154 KQSVSVLTSILKYLKQYATVILTSHD 179
Cdd:COG2274 644 AETEAIILENLRRLLKGRTVIIIAHR 669
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-182 |
5.52e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 17 QVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYL----LFVE 90
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpiSMLSSRQLARRLALLPQHHLtpegITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 91 QLYEVQHSCF-------------ALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSV 157
Cdd:PRK11231 95 ELVAYGRSPWlslwgrlsaednaRVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180
....*....|....*....|....*.
gi 1248686454 158 SVLTSILKYLKQYA-TVILTSHDEAQ 182
Cdd:PRK11231 175 VELMRLMRELNTQGkTVVTVLHDLNQ 200
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-182 |
7.48e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDHLpKSITLTVQQYL 86
Cdd:PRK11607 23 RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPPYQ-RPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 87 LFVEQLYEvQHSCFAL--------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGL 152
Cdd:PRK11607 102 LFPHMTVE-QNIAFGLkqdklpkaeiasrvNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190
....*....|....*....|....*....|....*
gi 1248686454 153 DKQ-----SVSVLtSILKYLKqyATVILTSHDEAQ 182
Cdd:PRK11607 181 DKKlrdrmQLEVV-DILERVG--VTCVMVTHDQEE 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-179 |
8.57e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.49 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYkPTVGNVTINGQ--VSYAPDHL-----------PKSITLTVQQYL-LFVEQLYEVQH 97
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRplSDWSAAELarhraylsqqqSPPFAMPVFQYLaLHQPAGASSEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 98 SCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLK-------QADIYILDEPFSGLDKQSVSVLTSILKYLK-Q 169
Cdd:COG4138 103 VEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCqQ 182
|
170
....*....|
gi 1248686454 170 YATVILTSHD 179
Cdd:COG4138 183 GITVVMSSHD 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-179 |
2.73e-15 |
|
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: 75.21 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVT------------------------INGQ--VSYAP---DHLPKSITLTV 82
Cdd:COG1245 101 VTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrfrgtelqdyfkklANGEikVAHKPqyvDLIPKVFKGTV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 QQYLLFVEQlyevqhsCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD-KQSVSVLT 161
Cdd:COG1245 181 RELLEKVDE-------RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVAR 253
|
170
....*....|....*...
gi 1248686454 162 SILKYLKQYATVILTSHD 179
Cdd:COG1245 254 LIRELAEEGKYVLVVEHD 271
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-191 |
3.27e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 2 DLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTI--NGQVSYAP---DHLPK 76
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgeTVKIGYFDqhqEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 77 SitLTVQQYLL-FVEQLYEvQHScfalddliqRFHIEAFL------SQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPF 149
Cdd:COG0488 393 D--KTVLDELRdGAPGGTE-QEV---------RGYLGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1248686454 150 SGLDKQSVSVLTSilkYLKQYA-TVILTSHDeaqHY---GLVTHQF 191
Cdd:COG0488 461 NHLDIETLEALEE---ALDDFPgTVLLVSHD---RYfldRVATRIL 500
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-191 |
4.43e-15 |
|
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: 72.14 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLPKSITLTVQQYLLF----VEQ------ 91
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFahltVEQnvglgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 92 -----LYEVQHScfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDkqsvsvltSILKy 166
Cdd:cd03298 96 spglkLTAEDRQ--AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD--------PALR- 164
|
170 180
....*....|....*....|....*.
gi 1248686454 167 lKQYATVILTSHDEAQHYGL-VTHQF 191
Cdd:cd03298 165 -AEMLDLVLDLHAETKMTVLmVTHQP 189
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-181 |
5.92e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVT------------------------INGQ--VSYAP---DHLPKSITLTV 82
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrfrgtelqnyfkklYNGEikVVHKPqyvDLIPKVFKGKV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 QQYLLFVEQlyevqhsCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD-KQSVSVlT 161
Cdd:PRK13409 181 RELLKKVDE-------RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDiRQRLNV-A 252
|
170 180
....*....|....*....|
gi 1248686454 162 SILKYLKQYATVILTSHDEA 181
Cdd:PRK13409 253 RLIRELAEGKYVLVVEHDLA 272
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1-179 |
6.62e-15 |
|
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: 71.52 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 1 MDLAIKGKSLTKVINgqvifsDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLpKSITL 80
Cdd:cd03226 3 ENISFSYKKGTEILD------DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR-KSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 81 TVQ--QYLLFVEQLY-EVQHSCFALDD-------LIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFS 150
Cdd:cd03226 76 VMQdvDYQLFTDSVReELLLGLKELDAgneqaetVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190
....*....|....*....|....*....|
gi 1248686454 151 GLDKQS-VSVLTSILKYLKQYATVILTSHD 179
Cdd:cd03226 156 GLDYKNmERVGELIRELAAQGKAVIVITHD 185
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-182 |
6.95e-15 |
|
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: 70.15 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYA-PDHlpksitltvqqy 85
Cdd:cd03216 4 RGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKeVSFAsPRD------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 86 llfveqlyevqhscfALDDLIQRFHieaflsqpikQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILK 165
Cdd:cd03216 72 ---------------ARRAGIAMVY----------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
170 180
....*....|....*....|
gi 1248686454 166 YLK-QYATVILTSH--DEAQ 182
Cdd:cd03216 127 RLRaQGVAVIFISHrlDEVF 146
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-182 |
9.92e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 9.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 18 VIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVS--------YAPDhlpksitLTVQQYLLFV 89
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPE-------LTGRENIYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 90 EQLY-----EVQHscfALDDlIQRF-HIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFS-G--------LDK 154
Cdd:COG1134 113 GRLLglsrkEIDE---KFDE-IVEFaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAvGdaafqkkcLAR 188
|
170 180
....*....|....*....|....*...
gi 1248686454 155 qsvsvltsILKYLKQYATVILTSHDEAQ 182
Cdd:COG1134 189 --------IRELRESGRTVIFVSHSMGA 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-182 |
1.00e-14 |
|
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: 71.44 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLA-----QIYKPTVGNVTINGQVSYAPDH--------- 73
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndlIPGAPDEGEVLLDGKDIYDLDVdvlelrrrv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 ---------LPKSI------TLTVQQYLLFVEQLYEVQHSC--FALDDliqrfhiEAFLSQPIKQCSKGTQQKLNLIQCL 136
Cdd:cd03260 84 gmvfqkpnpFPGSIydnvayGLRLHGIKLKEELDERVEEALrkAALWD-------EVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1248686454 137 LKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYATVILTSHDEAQ 182
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQ 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-181 |
1.60e-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: 71.24 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVT------------------------INGQVSYA--P---DHLPKSITLTV 82
Cdd:cd03236 28 VLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnyftklLEGDVKVIvkPqyvDLIPKAVKGKV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 qqyllfvEQLYEVQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD-KQSVSVLT 161
Cdd:cd03236 108 -------GELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDiKQRLNAAR 180
|
170 180
....*....|....*....|
gi 1248686454 162 SILKYLKQYATVILTSHDEA 181
Cdd:cd03236 181 LIRELAEDDNYVLVVEHDLA 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-229 |
3.30e-14 |
|
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: 70.02 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVING-QVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLT 81
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 82 VQQYLLF-----------VEQLYEVQHSCFA--LDDLIQRFHIE--AFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILD 146
Cdd:cd03295 81 IQQIGLFphmtveenialVPKLLKWPKEKIRerADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 147 EPFSGLDKQSVSVLTSILKYLKQ--YATVILTSHD--EAqhyglvthqFKLStQR--LMKLTEQAQVSYKiiETQFVSQI 220
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDidEA---------FRLA-DRiaIMKNGEIVQVGTP--DEILRSPA 228
|
....*....
gi 1248686454 221 dlNELVREF 229
Cdd:cd03295 229 --NDFVAEF 235
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-181 |
9.99e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 67.97 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 14 INGQVIFsDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTI-NGQV--------SYAPDHLPKSITLTVQQ 84
Cdd:PRK13541 11 IEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYkNCNInniakpycTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 85 YLLFVEQLYEvqhSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTS-I 163
Cdd:PRK13541 90 NLKFWSEIYN---SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNlI 166
|
170
....*....|....*...
gi 1248686454 164 LKYLKQYATVILTSHDEA 181
Cdd:PRK13541 167 VMKANSGGIVLLSSHLES 184
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-179 |
1.27e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDH---------L 74
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdISLLPLHararrgigyL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 75 PKSIT----LTVQQYLLFV----EQLYEVQHSCFAlDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILD 146
Cdd:PRK10895 84 PQEASifrrLSVYDNLMAVlqirDDLSAEQREDRA-NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 1248686454 147 EPFSGLDKQSVSVLTSILKYLKQYAT-VILTSHD 179
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHN 196
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-179 |
1.88e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.86 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIefPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLtvQQYLLF----VEQ---- 91
Cdd:COG3840 19 DLTI--AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdlTALPPAERPVSMLF--QENNLFphltVAQnigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 92 -------LYEVQHScfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD---KQsvsvlt 161
Cdd:COG3840 95 glrpglkLTAEQRA--QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalRQ------ 166
|
170 180
....*....|....*....|...
gi 1248686454 162 SILKYLKQYA-----TVILTSHD 179
Cdd:COG3840 167 EMLDLVDELCrerglTVLMVTHD 189
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-179 |
3.86e-13 |
|
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: 66.29 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQvsyAPDHLPKSITLTVQQYLLFVE---- 90
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE---PLDYSRKGLLERRQRVGLVFQdpdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 91 QLYEV---QHSCFAL--------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:TIGR01166 80 QLFAAdvdQDVAFGPlnlglseaeverrvREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*..
gi 1248686454 154 KQSVSVLTSILKYLK-QYATVILTSHD 179
Cdd:TIGR01166 160 PAGREQMLAILRRLRaEGMTVVISTHD 186
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-178 |
4.05e-13 |
|
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: 65.80 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-QVSYAPDHLPKSITLTVQQYLLFVEQLY 93
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvPVSDLEKALSSLISVLNQRPYLFDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 94 EvqhscfaldDLIQRFhieaflsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQS-VSVLTSILKYLKQYAT 172
Cdd:cd03247 93 N---------NLGRRF-------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDKTL 150
|
....*.
gi 1248686454 173 VILTSH 178
Cdd:cd03247 151 IWITHH 156
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-153 |
5.73e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 33 IQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLtvQQYLLF----VEQ-----------LYEV 95
Cdd:PRK10771 28 VAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVSMLF--QENNLFshltVAQniglglnpglkLNAA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1248686454 96 QHScfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:PRK10771 106 QRE--KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-185 |
6.28e-13 |
|
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: 68.50 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVIN--GQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ------------VSYAPDH 73
Cdd:TIGR01257 932 KNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 LPKSITLTVQQYLLFVEQL--YEVQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSG 151
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLkgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190
....*....|....*....|....*....|....*..
gi 1248686454 152 LDKQS-VSVLTSILKYlKQYATVILTSH--DEAQHYG 185
Cdd:TIGR01257 1092 VDPYSrRSIWDLLLKY-RSGRTIIMSTHhmDEADLLG 1127
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-181 |
8.43e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 66.27 E-value: 8.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 3 LAIKG--KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHlpkSITL 80
Cdd:COG1116 8 LELRGvsKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 81 TVQQYLLF----VEQlyEVqhsCFAL--------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADI 142
Cdd:COG1116 85 VFQEPALLpwltVLD--NV---ALGLelrgvpkaerreraRELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1248686454 143 YILDEPFSGLDKQSVSVL-TSILKYLKQY-ATVILTSHD--EA 181
Cdd:COG1116 160 LLMDEPFGALDALTRERLqDELLRLWQETgKTVLFVTHDvdEA 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-178 |
1.16e-12 |
|
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: 65.18 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPdHLPKSITLTVQQYLLFV----EQLYE 94
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVS-QEPWIQNGTIRENILFGkpfdEERYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 95 -VQHSCfALDDLIQRFH------I-EAFLSqpikqCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTS--IL 164
Cdd:cd03250 99 kVIKAC-ALEPDLEILPdgdlteIgEKGIN-----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncIL 172
|
170
....*....|....
gi 1248686454 165 KYLKQYATVILTSH 178
Cdd:cd03250 173 GLLLNNKTRILVTH 186
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-180 |
1.16e-12 |
|
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: 65.59 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQ----VIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDH------ 73
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 -------------LPksiTLTVQQYLLFVEQLYEVQHSCFALD--DLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLK 138
Cdd:cd03255 81 rrhigfvfqsfnlLP---DLTALENVELPLLLAGVPKKERRERaeELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1248686454 139 QADIYILDEPFSGLDKQSVSVLTSILKYLKQYA--TVILTSHDE 180
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-223 |
2.03e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 20 FSDMTIEFPNQSIIQIVGANGSGK-SVTLKMLAQIYKPTVGNVTINGQVSYAPdHLPKSITLTVQQYLLFVEQlYEVQHS 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRGSVAYVP-QVSWIFNATVRENILFGSD-FESERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 99 CFALDDLIQRFHIEAFLSQPIKQC-------SKGTQQKLNLIQCLLKQADIYILDEPFSGLD----------------KQ 155
Cdd:PLN03232 711 WRAIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDahvahqvfdscmkdelKG 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248686454 156 SVSVL-TSILKYLKQYATVILTSHDEAQHYGLVTHQFKlSTQRLMKLTEQAQvsyKIIETQFVSQIDLN 223
Cdd:PLN03232 791 KTRVLvTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SGSLFKKLMENAG---KMDATQEVNTNDEN 855
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
35-179 |
2.85e-12 |
|
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: 66.08 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ----------------VSYA---PDHlpkSI--TLTVQQYLLFVEQLY 93
Cdd:COG1123 296 LVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelrrrVQMVfqdPYS---SLnpRMTVGDIIAEPLRLH 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 94 ------EVQHscfALDDLIQRFHI-EAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDkqsVSVLTSILKY 166
Cdd:COG1123 373 gllsraERRE---RVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD---VSVQAQILNL 446
|
170
....*....|....*...
gi 1248686454 167 LKQYA-----TVILTSHD 179
Cdd:COG1123 447 LRDLQrelglTYLFISHD 464
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-182 |
3.22e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 14 INGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPD--------HLPKSITLTVQQY 85
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqidaiKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 86 LLF--------------------VEQLYEVQHSCFALDDLIQRFHIEafLSQPIKQCSKGTQQKLNLIQCLLKQADIYIL 145
Cdd:PRK14246 100 NPFphlsiydniayplkshgikeKREIKKIVEECLRKVGLWKEVYDR--LNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1248686454 146 DEPFSGLDKQSVSVLTSILKYLKQYATVILTSHDEAQ 182
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQ 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-177 |
3.38e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ----------VSYAP--DHLPKSITLTV 82
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPqsEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 QQYLL--------FVEQLYEVQHSCfaLDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDK 154
Cdd:PRK15056 98 EDVVMmgryghmgWLRRAKKRDRQI--VTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|...
gi 1248686454 155 QSVSVLTSILKYLKQYATVILTS 177
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVS 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-179 |
1.27e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYkPTVGNVTINGQV-------------SYAPDHLPKSITLTVQQYL-LFVEQLYEVQH 97
Cdd:PRK03695 24 ILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPleawsaaelarhrAYLSQQQTPPFAMPVFQYLtLHQPDKTRTEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 98 SCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLK-------QADIYILDEPFSGLDKQSVSVLTSILKYL-KQ 169
Cdd:PRK03695 103 VASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELcQQ 182
|
170
....*....|
gi 1248686454 170 YATVILTSHD 179
Cdd:PRK03695 183 GIAVVMSSHD 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
105-187 |
1.55e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 105 LIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYL--KQYATV-ILTSHDE- 180
Cdd:PRK10938 119 LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLhqSGITLVlVLNRFDEi 198
|
90
....*....|
gi 1248686454 181 ---AQHYGLV 187
Cdd:PRK10938 199 pdfVQFAGVL 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-179 |
2.10e-11 |
|
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: 62.13 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-----VSYAPDHLPKSIT 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 80 LTVQQYLLF----VEQ-----LYEvqHSCFaLDDLIQ---RFHIEAF-LSQPIK----QCSKGTQQKLNLIQCLLKQADI 142
Cdd:cd03261 81 MLFQSGALFdsltVFEnvafpLRE--HTRL-SEEEIReivLEKLEAVgLRGAEDlypaELSGGMKKRVALARALALDPEL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1248686454 143 YILDEPFSGLDKQSVSVLTSILKYLKQY--ATVILTSHD 179
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHD 196
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-178 |
2.18e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.59 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 14 INGQVIFSDMTIEFPNQSIIQI----------------VGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLP 75
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVPVlkgltftlhpgevvalVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplVQYDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 76 KSITLTVQQYLLF----------------VEQLYEVQHSCFAlDDLIQRFH--IEAFLSQPIKQCSKGTQQKLNLIQCLL 137
Cdd:TIGR00958 555 RQVALVGQEPVLFsgsvreniaygltdtpDEEIMAAAKAANA-HDFIMEFPngYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1248686454 138 KQADIYILDEPFSGLDKQSVSVLTSILKylKQYATVILTSH 178
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAH 672
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-179 |
3.32e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQvsyaPDHLPKSITLTVQQYLLFVEQLYEVQ-- 96
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK----PLDYSKRGLLALRQQVATVFQDPEQQif 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 97 ------HSCFAL--------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQS 156
Cdd:PRK13638 92 ytdidsDIAFSLrnlgvpeaeitrrvDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180
....*....|....*....|....
gi 1248686454 157 VSVLTSILKYL-KQYATVILTSHD 179
Cdd:PRK13638 172 RTQMIAIIRRIvAQGNHVIISSHD 195
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-178 |
3.59e-11 |
|
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: 61.52 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLA---QIYKPTVGNVTINGQ----------VSYAPDH---LPksiTLTV 82
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQprkpdqfqkcVAYVRQDdilLP---GLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 QQYLLFVEQLY------EVQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDkqS 156
Cdd:cd03234 99 RETLTYTAILRlprkssDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD--S 176
|
170 180
....*....|....*....|....*.
gi 1248686454 157 VSVLtSILKYLKQYA----TVILTSH 178
Cdd:cd03234 177 FTAL-NLVSTLSQLArrnrIVILTIH 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-179 |
4.90e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.34 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 16 GQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-------------VSYAPDHLPKSITLTV 82
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 QQYLLFVEQLYEVQHSCFA------LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD-KQ 155
Cdd:PRK10575 103 RELVAIGRYPWHGALGRFGaadrekVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAH 182
|
170 180
....*....|....*....|....*
gi 1248686454 156 SVSVLTSILKYLKQYA-TVILTSHD 179
Cdd:PRK10575 183 QVDVLALVHRLSQERGlTVIAVLHD 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-181 |
5.04e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.04 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSyapdHLP---KSITLTVQ 83
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdVT----GLPpekRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 84 QYLLF----VEQlyevqHSCFAL--------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYIL 145
Cdd:COG3842 85 DYALFphltVAE-----NVAFGLrmrgvpkaeirarvAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1248686454 146 DEPFSGLDKQS-VSVLTSILKYLKQY-ATVILTSHD--EA 181
Cdd:COG3842 160 DEPLSALDAKLrEEMREELRRLQRELgITFIYVTHDqeEA 199
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-179 |
5.90e-11 |
|
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: 60.76 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 1 MDLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDhlpksit 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 80 ltvqqyllfvEQLYEV--------QHScfAL-DDL-----IqrfhieAFlsqPIKQCSKGTQQKLNLI--QCL----LKQ 139
Cdd:COG1127 75 ----------KELYELrrrigmlfQGG--ALfDSLtvfenV------AF---PLREHTDLSEAEIRELvlEKLelvgLPG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248686454 140 A--------------------------DIYILDEPFSGLDKQSVSVLTS-ILKYLKQY-ATVILTSHD 179
Cdd:COG1127 134 AadkmpselsggmrkrvalaralaldpEILLYDEPTAGLDPITSAVIDElIRELRDELgLTSVVVTHD 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-180 |
9.24e-11 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 58.91 E-value: 9.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 18 VIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAqiykptvgnvtingqvsyapdhlpksitltvqqYLLFVEQLYEVQH 97
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 98 SCFALDDLIQRFHIEAFLSqpIKQCSKGTQQK----LNLIQCLLKQADIYILDEPFSGLDKQSV-SVLTSILKYLKQYAT 172
Cdd:cd03227 56 SGVKAGCIVAAVSAELIFT--RLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGqALAEAILEHLVKGAQ 133
|
....*...
gi 1248686454 173 VILTSHDE 180
Cdd:cd03227 134 VIVITHLP 141
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-179 |
1.59e-10 |
|
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: 59.76 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 3 LAIKGksLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDH-------- 73
Cdd:cd03219 1 LEVRG--LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdITGLPPHeiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 --------LPKsitLTVQQYLLFVEQLYEVQHSCFAL------------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLI 133
Cdd:cd03219 79 rtfqiprlFPE---LTVLENVMVAAQARTGSGLLLARarreereareraEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1248686454 134 QCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQY-ATVILTSHD 179
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHD 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
35-179 |
1.66e-10 |
|
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: 59.66 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHlpKSITLTVQQYLLF----VE---------QLYEVQHSC 99
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILLNGKdiTNLPPEK--RDISYVPQNYALFphmtVYkniayglkkRKVDKKEIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 100 FALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYL-KQYA-TVILTS 177
Cdd:cd03299 108 RKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIrKEFGvTVLHVT 187
|
..
gi 1248686454 178 HD 179
Cdd:cd03299 188 HD 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-178 |
2.37e-10 |
|
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: 59.17 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 16 GQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLFVEQLY 93
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdiREVTLDSLRRAIGVVPQDTVLFNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 94 -------------EVQHSCFA--LDDLIQRFhieaflsqPIK----------QCSKGTQQKLNLIQCLLKQADIYILDEP 148
Cdd:cd03253 93 ynirygrpdatdeEVIEAAKAaqIHDKIMRF--------PDGydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190
....*....|....*....|....*....|
gi 1248686454 149 FSGLDKQSVSVLTSILKYLKQYATVILTSH 178
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGRTTIVIAH 194
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-178 |
2.87e-10 |
|
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: 58.00 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQV--SYAPDHLPKSITLTVQQYLLFveql 92
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisQWDPNELGDHVGYLPQDDELF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 yevqhscfalDDLIqrfhIEAFLsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLK-QYA 171
Cdd:cd03246 89 ----------SGSI----AENIL-------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGA 147
|
....*..
gi 1248686454 172 TVILTSH 178
Cdd:cd03246 148 TRIVIAH 154
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-182 |
3.51e-10 |
|
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: 58.40 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDHlPKSITLTVQ 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdITNLPPH-KRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 84 QYLLFvEQLYEVQHSCFAL-------DDLIQRFH-------IEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPF 149
Cdd:cd03300 80 NYALF-PHLTVFENIAFGLrlkklpkAEIKERVAealdlvqLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1248686454 150 SGLDKQSVSVLTSILKYLKQY--ATVILTSHDEAQ 182
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKElgITFVFVTHDQEE 193
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-153 |
5.33e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.24 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 4 AIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDH-------L 74
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRplADWSPAElarrravL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 75 PKSITLTvqqyllF---VEqlyEV------------QHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCL--L 137
Cdd:PRK13548 82 PQHSSLS------FpftVE---EVvamgraphglsrAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqL 152
|
170 180
....*....|....*....|
gi 1248686454 138 KQAD----IYILDEPFSGLD 153
Cdd:PRK13548 153 WEPDgpprWLLLDEPTSALD 172
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-175 |
5.37e-10 |
|
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: 57.83 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 17 QVIFsDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDH---------LPKS----ITLTV 82
Cdd:cd03224 14 QILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdITGLPPHeraragigyVPEGrrifPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 QQYLLFVEQLYEVQHSCFALDDLIQRFHI-EAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLT 161
Cdd:cd03224 93 EENLLLGAYARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170
....*....|....
gi 1248686454 162 SILKYLKQYATVIL 175
Cdd:cd03224 173 EAIRELRDEGVTIL 186
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-179 |
5.78e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.08 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 30 QSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDHL--PKSITLTVQQYLLF-----VEQLYEVQH---- 97
Cdd:PRK11300 31 QEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhIEGLPGHQiaRMGVVRTFQHVRLFremtvIENLLVAQHqqlk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 98 SCF----------------ALDDL---IQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVS 158
Cdd:PRK11300 111 TGLfsgllktpafrraeseALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETK 190
|
170 180
....*....|....*....|...
gi 1248686454 159 VLTSILKYLKQY--ATVILTSHD 179
Cdd:PRK11300 191 ELDELIAELRNEhnVTVLLIEHD 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-178 |
5.89e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.45 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 2 DLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSIT 79
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 80 LTVQQYLLFV----------------EQLYEVQHSCfALDDLIQRFH-IEAFLSQPIKQCSKGTQQKLNLIQCLLKQADI 142
Cdd:PRK11160 418 VVSQRVHLFSatlrdnlllaapnasdEALIEVLQQV-GLEKLLEDDKgLNAWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190
....*....|....*....|....*....|....*....
gi 1248686454 143 YILDEPFSGLDKQSVSvltSILKYLKQYA---TVILTSH 178
Cdd:PRK11160 497 LLLDEPTEGLDAETER---QILELLAEHAqnkTVLMITH 532
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-179 |
5.91e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.71 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPD---HLPKSITLTVQQ--YLLF 88
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKglmKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 89 VEQLY---------------EVQHScfaLDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:PRK13636 97 SASVYqdvsfgavnlklpedEVRKR---VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180
....*....|....*....|....*...
gi 1248686454 154 KQSVSVLTSILKYLKQYA--TVILTSHD 179
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELglTIIIATHD 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-236 |
5.95e-10 |
|
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: 57.54 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLA--QIYKPTVGNVTINGQvsyapdhlpkSIT-LTVQQ 84
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGE----------DITdLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 85 YL---LFVEQLYEVQHSCFALDDLIqRFHIEAFlsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLT 161
Cdd:cd03217 74 RArlgIFLAFQYPPEIPGVKNADFL-RYVNEGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248686454 162 SILKYLKQYATVILtshdeaqhygLVTHqfklsTQRLMKLteqaqvsykiIETQFVSQIDLNELVREFDMEIIEQ 236
Cdd:cd03217 145 EVINKLREEGKSVL----------IITH-----YQRLLDY----------IKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
35-178 |
6.42e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSvTL-KMLAQIYKPTVGNVTINGQVsYAPDHlPK-SITL---TVQQYLLFVEQL---------YEVQHSCF 100
Cdd:COG3845 36 LLGENGAGKS-TLmKILYGLYQPDSGEILIDGKP-VRIRS-PRdAIALgigMVHQHFMLVPNLtvaenivlgLEPTKGGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 101 --------ALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLK-QYA 171
Cdd:COG3845 113 ldrkaaraRIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAaEGK 192
|
....*..
gi 1248686454 172 TVILTSH 178
Cdd:COG3845 193 SIIFITH 199
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-178 |
8.22e-10 |
|
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: 57.55 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLF-------- 88
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdiRDLNLRWLRSQIGLVSQEPVLFdgtiaeni 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 89 --------VEQLYEVQHSCFALD---DLIQRFHIEafLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSV 157
Cdd:cd03249 98 rygkpdatDEEVEEAAKKANIHDfimSLPDGYDTL--VGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180
....*....|....*....|.
gi 1248686454 158 SVLTSILKYLKQYATVILTSH 178
Cdd:cd03249 176 KLVQEALDRAMKGRTTIVIAH 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
35-179 |
9.19e-10 |
|
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: 57.13 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLPKSI------------------TLTVQqyllfvEQLYEVQ 96
Cdd:cd03257 36 LVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrrkeiqmvfqdpmsslnpRMTIG------EQIAEPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 97 --HSCFALDDLIQRFHIEAF--LSQPIK-------QCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDkqsVSVLTSILK 165
Cdd:cd03257 110 riHGKLSKKEARKEAVLLLLvgVGLPEEvlnryphELSGGQRQRVAIARALALNPKLLIADEPTSALD---VSVQAQILD 186
|
170
....*....|....*....
gi 1248686454 166 YLKQYA-----TVILTSHD 179
Cdd:cd03257 187 LLKKLQeelglTLLFITHD 205
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-153 |
1.09e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 14 INGQVIFSDMTIEFPNQS--------------IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ----VSYAPdhLP 75
Cdd:PRK13657 331 VKGAVEFDDVSFSYDNSRqgvedvsfeakpgqTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtVTRAS--LR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 76 KSITLTVQQYLLFV----------------EQLYEVQHSCFALDDLIQRFH-IEAFLSQPIKQCSKGTQQKLNLIQCLLK 138
Cdd:PRK13657 409 RNIAVVFQDAGLFNrsiednirvgrpdatdEEMRAAAERAQAHDFIERKPDgYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170
....*....|....*
gi 1248686454 139 QADIYILDEPFSGLD 153
Cdd:PRK13657 489 DPPILILDEATSALD 503
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
34-190 |
1.18e-09 |
|
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: 57.40 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 34 QIVGANGSGKSVTLKMLA----QIYKPTV-------GNVTIN------GQVSYA-PDHLPKSITltvqqyllfVEQ---- 91
Cdd:COG1119 33 AILGPNGAGKSTLLSLITgdlpPTYGNDVrlfgerrGGEDVWelrkriGLVSPAlQLRFPRDET---------VLDvvls 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 92 -------LY----EVQHScfALDDLIQRFHIEAFLSQPIKQCSKGtQQKLNLI-QCLLKQADIYILDEPFSGLDKQSVSV 159
Cdd:COG1119 104 gffdsigLYreptDEQRE--RARELLELLGLAHLADRPFGTLSQG-EQRRVLIaRALVKDPELLILDEPTAGLDLGAREL 180
|
170 180 190
....*....|....*....|....*....|..
gi 1248686454 160 LTSILKYL-KQYATVILtshdeaqhygLVTHQ 190
Cdd:COG1119 181 LLALLDKLaAEGAPTLV----------LVTHH 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-179 |
1.25e-09 |
|
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: 56.65 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVI-NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPD----HLPKSI 78
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdVSDLRGraipYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 79 TLTVQQY-LLFVEQLYEvqHSCFALD------DLIQRFHIEAF----LSQPIK----QCSKGTQQKLNLIQCLLKQADIY 143
Cdd:cd03292 81 GVVFQDFrLLPDRNVYE--NVAFALEvtgvppREIRKRVPAALelvgLSHKHRalpaELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1248686454 144 ILDEPFSGLDKQSVSVLTSILKYLKQY-ATVILTSHD 179
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAgTTVVVATHA 195
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-169 |
1.51e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.96 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFpNQSiiQIV---GANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDH------- 73
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEV-NQG--EIVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdITHLPMHkrarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 --LP--KSI--TLTVQQYLLFVEQLYEVQHSCFA--LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYIL 145
Cdd:COG1137 81 gyLPqeASIfrKLTVEDNILAVLELRKLSKKEREerLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180
....*....|....*....|....
gi 1248686454 146 DEPFSGLDKQSVSVLTSILKYLKQ 169
Cdd:COG1137 161 DEPFAGVDPIAVADIQKIIRHLKE 184
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-178 |
1.67e-09 |
|
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: 56.44 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 16 GQVIFSDMTIEFPNQSI---------------IQIVGANGSGKSVTLKMLAQIYKPTVGNVTING----QVSyaPDHLPK 76
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpaldnvsltiragekVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirQLD--PADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 77 SITLTVQQYLLFVEQLYE--------------VQHSCFA-LDDLIQRfHIEAF---LSQPIKQCSKGTQQKLNLIQCLLK 138
Cdd:cd03245 79 NIGYVPQDVTLFYGTLRDnitlgapladderiLRAAELAgVTDFVNK-HPNGLdlqIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1248686454 139 QADIYILDEPFSGLDKQSVSVLTSILKYLKQYATVILTSH 178
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITH 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-180 |
2.24e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSvTL-KMLAQIYKPTVGNVTINGQVsYAPDHlPK-SITL---TVQQYLLFVEQL---------YEVQHSCF 100
Cdd:COG1129 35 LLGENGAGKS-TLmKILSGVYQPDSGEILLDGEP-VRFRS-PRdAQAAgiaIIHQELNLVPNLsvaeniflgREPRRGGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 101 aLD---------DLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLK-QY 170
Cdd:COG1129 112 -IDwramrrrarELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKaQG 190
|
170
....*....|..
gi 1248686454 171 ATVILTSH--DE 180
Cdd:COG1129 191 VAIIYISHrlDE 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-179 |
2.29e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.16 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 21 SDMTIEFPNQSIIQ-------------IVGANGSGKSVTLKMLAQIYKPTVGNVTING-------------QVSYAPDHL 74
Cdd:PRK09536 7 SDLSVEFGDTTVLDgvdlsvregslvgLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 75 PKSITLTVQQyllFVEQLYEVQHSCF---------ALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYIL 145
Cdd:PRK09536 87 SLSFEFDVRQ---VVEMGRTPHRSRFdtwtetdraAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1248686454 146 DEPFSGLD-KQSVSVLTSILKYLKQYATVILTSHD 179
Cdd:PRK09536 164 DEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-182 |
2.57e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.46 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 12 KVINGQV-IFSDMTIEFPNQSIIQIVGANGSGKSVTLKM---LAQIY-KPTV-GNVTINGQVSYAPD------------H 73
Cdd:PRK14247 10 KVSFGQVeVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYpEARVsGEVYLDGQDIFKMDvielrrrvqmvfQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 LPKSI-TLTVQQYLLFVEQLYEVQHSCFALDDLIQRF--------HIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYI 144
Cdd:PRK14247 90 IPNPIpNLSIFENVALGLKLNRLVKSKKELQERVRWAlekaqlwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1248686454 145 LDEPFSGLDKQSVSVLTSILKYLKQYATVILTSHDEAQ 182
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQ 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-180 |
2.72e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 17 QVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGnvtiNGQVSYAPDHLPKSITLtvqqyllfVEQLYEVQ 96
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV----AGCVDVPDNQFGREASL--------IDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 97 hscfALDDLIQRFHI----EAFL-SQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYL--KQ 169
Cdd:COG2401 111 ----DFKDAVELLNAvglsDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRA 186
|
170
....*....|.
gi 1248686454 170 YATVILTSHDE 180
Cdd:COG2401 187 GITLVVATHHY 197
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
32-179 |
3.10e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 56.24 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYApdhlpKSITLTVQQYLLFV-----EQLY------------ 93
Cdd:PRK13639 30 MVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYD-----KKSLLEVRKTVGIVfqnpdDQLFaptveedvafgp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 94 --------EVQHScfaLDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILK 165
Cdd:PRK13639 105 lnlglskeEVEKR---VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLY 181
|
170
....*....|....*
gi 1248686454 166 YL-KQYATVILTSHD 179
Cdd:PRK13639 182 DLnKEGITIIISTHD 196
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-179 |
3.76e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 21 SDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLFVE-QLYE--- 94
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItiTHKTKDKYIRPVRKRIGMVFQFPEsQLFEdtv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 95 ---------------VQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSV 159
Cdd:PRK13646 104 ereiifgpknfkmnlDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQ 183
|
170 180
....*....|....*....|..
gi 1248686454 160 LTSILKYL--KQYATVILTSHD 179
Cdd:PRK13646 184 VMRLLKSLqtDENKTIILVSHD 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-178 |
4.20e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 56.74 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEF-PNQSIIqIVGANGSGKSVTLKMLAQIYKPTVGNVTING--------QVSYAPD----------HLP 75
Cdd:COG4178 374 DGRPLLEDLSLSLkPGERLL-ITGPSGSGKSTLLRAIAGLWPYGSGRIARPAgarvlflpQRPYLPLgtlreallypATA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 76 KSITLtvqqyllfvEQLYEVQHSCfALDDLIQRFHIEAFLSQpikQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQ 155
Cdd:COG4178 453 EAFSD---------AELREALEAV-GLGHLAERLDEEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|...
gi 1248686454 156 SVSVLTSILKYLKQYATVILTSH 178
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGH 542
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
35-182 |
4.53e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ------------VSYAP--DHLPKSITLTvQQYLLFVEQLYEVQHSCF 100
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPqfDNLDPDFTVR-ENLLVFGRYFGLSAAAAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 101 AL-DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILK-YLKQYATVILTSH 178
Cdd:PRK13537 117 ALvPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRsLLARGKTILLTTH 196
|
....*.
gi 1248686454 179 --DEAQ 182
Cdd:PRK13537 197 fmEEAE 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
35-179 |
4.71e-09 |
|
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: 56.45 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTV---GNVTINGQ--VSYAPDHLPKSI------------TLTVQQYLLFVEQLYEVQH 97
Cdd:COG1123 37 LVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRdlLELSEALRGRRIgmvfqdpmtqlnPVTVGDQIAEALENLGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 98 SCF--ALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQY--ATV 173
Cdd:COG1123 117 AEAraRVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTV 196
|
....*.
gi 1248686454 174 ILTSHD 179
Cdd:COG1123 197 LLITHD 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-193 |
5.02e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.76 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITL-- 80
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLla 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 81 ---------TVQQYL---------LFVEQLYEVQHscfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADI 142
Cdd:PRK10253 88 qnattpgdiTVQELVargryphqpLFTRWRKEDEE---AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1248686454 143 YILDEPFSGLDKQSVSVLTSILKYLKQYATVILTS--HDEAQHYGLVTHQFKL 193
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAvlHDLNQACRYASHLIAL 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-179 |
6.21e-09 |
|
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: 56.10 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 2 DLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTInGQvsyapdhlpksitlT 81
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE--------------T 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 82 VQqyLLFVEQLYEvqhscfALD-------------DLIQ--------RFHIEAF------LSQPIKQCSKGTQQKLNLIQ 134
Cdd:TIGR03719 385 VK--LAYVDQSRD------ALDpnktvweeisgglDIIKlgkreipsRAYVGRFnfkgsdQQKKVGQLSGGERNRVHLAK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1248686454 135 CLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYATVIltSHD 179
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVI--SHD 499
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-178 |
6.56e-09 |
|
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: 54.93 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VS-YAPDHLPKSITLTVQQYLLFVEQLYE-- 94
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdVRdYTLASLRRQIGLVSQDVFLFNDTVAEni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 95 -----------VQHSCFA--LDDLIQRFH--IEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSV 159
Cdd:cd03251 97 aygrpgatreeVEEAARAanAHEFIMELPegYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERL 176
|
170
....*....|....*....
gi 1248686454 160 LTSILKYLKQYATVILTSH 178
Cdd:cd03251 177 VQAALERLMKNRTTFVIAH 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-178 |
6.71e-09 |
|
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: 54.78 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 14 INGQVIFSDMTIEFPNQSIIQI----------------VGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDH--LP 75
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVlqdvsftlhpgevtalVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHkyLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 76 KSITLTVQQYLLFVEQL-----YEVQHSCF-ALDDLIQRFHIEAFLS-----------QPIKQCSKGTQQKLNLIQCLLK 138
Cdd:cd03248 88 SKVSLVGQEPVLFARSLqdniaYGLQSCSFeCVKEAAQKAHAHSFISelasgydtevgEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1248686454 139 QADIYILDEPFSGLDKQSVSVLTSILKYLKQYATVILTSH 178
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAH 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
31-178 |
7.48e-09 |
|
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: 54.09 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 31 SIIQIVGANGSGKSVTLKMLA--QIYKPTVGNVTINGQVSYaPDHLPKSI-----------TLTVQQYLLFVEQLyevqh 97
Cdd:cd03213 36 ELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD-KRSFRKIIgyvpqddilhpTLTVRETLMFAAKL----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 98 scfalddliqrfhieaflsqpiKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDkqSVSVLtSILKYLKQYA----TV 173
Cdd:cd03213 110 ----------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD--SSSAL-QVMSLLRRLAdtgrTI 164
|
....*
gi 1248686454 174 ILTSH 178
Cdd:cd03213 165 ICSIH 169
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-182 |
8.01e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.61 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 2 DLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING------------QVSY 69
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 70 APDHLPKSITLTVQQYLLFVEQLY--EVQHSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDE 147
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFgmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190
....*....|....*....|....*....|....*...
gi 1248686454 148 PFSGLDKQSVSVLTSILK-YLKQYATVILTSH--DEAQ 182
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRsLLARGKTILLTTHfmEEAE 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-179 |
8.17e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.76 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 4 AIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPT-----VGNVTINGQVSYAPDhlpKSI 78
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirVGDITIDTARSLSQQ---KGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 79 TLTVQQYLLFVEQLYEVQHSCFALDDLIQ---------RFHIEAFLSQPI-------------KQCSKGTQQKLNLIQCL 136
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEgpvivkgepKEEATARARELLakvglagketsypRRLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1248686454 137 LKQADIYILDEPFSGLDKQSV-SVLTSILKYLKQYATVILTSHD 179
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVgEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-179 |
8.71e-09 |
|
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: 55.71 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 10 LTKVINGQ-VIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTI--NGQVSYAPDHLPKSITLTVQQ-- 84
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqpGIKVGYLPQEPQLDPTKTVREnv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 85 -----------------YLLFVE------QLYEVQHscfALDDLIQR---FHIEAFLSQ------------PIKQCSKGT 126
Cdd:TIGR03719 90 eegvaeikdaldrfneiSAKYAEpdadfdKLAAEQA---ELQEIIDAadaWDLDSQLEIamdalrcppwdaDVTKLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1248686454 127 QQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTsilKYLKQYA-TVILTSHD 179
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE---RHLQEYPgTVVAVTHD 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-183 |
1.06e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 14 INGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-------------QVSYAPdHLPKSITL 80
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCA-QTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 81 TVQQYLLFVEQLYEVQHSCFALDDLIQRFHI-EAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD---KQS 156
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnKHN 175
|
170 180 190
....*....|....*....|....*....|
gi 1248686454 157 VSVLtsILKYLKQYATVIL-TSHD--EAQH 183
Cdd:PRK10247 176 VNEI--IHRYVREQNIAVLwVTHDkdEINH 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
32-179 |
1.21e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.50 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPK----SITLTVQQYLLF----VEQLYEVQhSCFA 101
Cdd:PRK10535 36 MVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvATLDADALAQlrreHFGFIFQRYHLLshltAAQNVEVP-AVYA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 102 ----------LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYA 171
Cdd:PRK10535 115 glerkqrllrAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRG 194
|
....*....
gi 1248686454 172 -TVILTSHD 179
Cdd:PRK10535 195 hTVIIVTHD 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-203 |
1.25e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 4 AIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKpTVGNVTINGQVSYAP----------DH 73
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNqniyerrvnlNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 LPKSITLTVQQYLLFVEQLYE-----VQ----HSCFALDDLIQRFHIEAFLSQPIK--------QCSKGTQQKLNLIQCL 136
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDnvaygVKivgwRPKLEIDDIVESALKDADLWDEIKhkihksalDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248686454 137 LKQADIYILDEPFSGLDKQSVSVLTSILK--YLKQYATVILTSHDEAQHYGL--VTHQFKLSTQRLMKLTE 203
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLsdFTAFFKGNENRIGQLVE 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-178 |
1.31e-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: 55.22 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTV--GNVTINGQ---VSYAPDHLPKSITLtV 82
Cdd:TIGR02633 5 KGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSplkASNIRDTERAGIVI-I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 83 QQYLLFVEQL---------YEVQHSCFALDD---------LIQRFHIEAF-LSQPIKQCSKGTQQKLNLIQCLLKQADIY 143
Cdd:TIGR02633 84 HQELTLVPELsvaeniflgNEITLPGGRMAYnamylraknLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1248686454 144 ILDEPFSGLDKQSVSVLTSILKYLKQYATV-ILTSH 178
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAHGVAcVYISH 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-179 |
1.40e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPD--HLPKSITLTVQQYLlfveQLYE 94
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQklYLDTTLPLTVNRFL----RLRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 95 VQHSCFALDDLiQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQ--YAT 172
Cdd:PRK09544 95 GTKKEDILPAL-KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCA 173
|
....*..
gi 1248686454 173 VILTSHD 179
Cdd:PRK09544 174 VLMVSHD 180
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-179 |
1.66e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.96 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 26 EFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-QVSYAPdhlpksitltvqQYLlfveqlyevqhscfaldd 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKP------------QYI------------------ 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248686454 105 liqrfhieaflsqpikQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYA--TVILTSHD 179
Cdd:cd03222 71 ----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkkTALVVEHD 131
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-178 |
2.02e-08 |
|
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: 53.64 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLF---- 88
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAWLRRQVGVVLQENVLFnrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 89 ------------VEQLYEVQHSCFALDDLIQ-RFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQ 155
Cdd:cd03252 93 rdnialadpgmsMERVIEAAKLAGAHDFISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180
....*....|....*....|...
gi 1248686454 156 SVSVLTSILKYLKQYATVILTSH 178
Cdd:cd03252 173 SEHAIMRNMHDICAGRTVIIIAH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-153 |
3.07e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.57 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 23 MTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLPKSiTLTVQQYLLFVEQLYE-----VQH 97
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQ-NDSLRENILFGKALNEkyyqqVLE 735
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1248686454 98 SCFALDDL-IQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:TIGR00957 736 ACALLPDLeILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-179 |
3.25e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.48 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ----------------VSYAPDHlpKSITLTVQQYLLF------VEQL 92
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwdvrrqvgmVFQNPDN--QFVGATVQDDVAFglenigVPRE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 YEVQHscfaLDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQS-VSVLTSIlKYLK--Q 169
Cdd:PRK13635 116 EMVER----VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGrREVLETV-RQLKeqK 190
|
170
....*....|
gi 1248686454 170 YATVILTSHD 179
Cdd:PRK13635 191 GITVLSITHD 200
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-182 |
5.02e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.47 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQI--YKPTV---GNVTINGQVSYAPD----HLPKSITLTVQQYLLFVEQL 92
Cdd:PRK14239 23 SVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEVtitGSIVYNGHNIYSPRtdtvDLRKEIGMVFQQPNPFPMSI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 YEV---------QHSCFALDDLIQRFHIEAFLSQPIKQ--------CSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQ 155
Cdd:PRK14239 103 YENvvyglrlkgIKDKQVLDEAVEKSLKGASIWDEVKDrlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPI 182
|
170 180
....*....|....*....|....*..
gi 1248686454 156 SVSVLTSILKYLKQYATVILTSHDEAQ 182
Cdd:PRK14239 183 SAGKIEETLLGLKDDYTMLLVTRSMQQ 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-178 |
5.84e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDH-----LPKSIT 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaaqLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 80 ---LTVQQYLLFVEQLYEVQH---SCFALD------------DLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQAD 141
Cdd:PRK09700 86 yqeLSVIDELTVLENLYIGRHltkKVCGVNiidwremrvraaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1248686454 142 IYILDEPFSGLDKQSVSVLTSILKYLKQYATVIL-TSH 178
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISH 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-182 |
6.22e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYK--PTV---GNVTINGQVSYAPDHLP----KSITLTVQQYLLFVEQL 92
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYAPDVDPvevrRRIGMVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 YE-------VQHSCFALDDLIQRFHIEAFLSQPIK--------QCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSV 157
Cdd:PRK14243 108 YDniaygarINGYKGDMDELVERSLRQAALWDEVKdklkqsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIST 187
|
170 180
....*....|....*....|....*
gi 1248686454 158 SVLTSILKYLKQYATVILTSHDEAQ 182
Cdd:PRK14243 188 LRIEELMHELKEQYTIIIVTHNMQQ 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
35-178 |
8.58e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.86 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLF---VEQ--LY--------EVQHSC 99
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdiRDLTLESLRRQIGVVPQDTFLFsgtIREniRYgrpdatdeEVEEAA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 100 FA--LDDLIQRF------HIE---AFLSQpikqcskGTQQKLNLIQCLLKQADIYILDEPFSGLDKQS-VSVLTSILKYL 167
Cdd:COG1132 451 KAaqAHEFIEALpdgydtVVGergVNLSG-------GQRQRIAIARALLKDPPILILDEATSALDTETeALIQEALERLM 523
|
170
....*....|.
gi 1248686454 168 KQyATVILTSH 178
Cdd:COG1132 524 KG-RTTIVIAH 533
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-182 |
1.21e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYApdhlpkSITLTVQQYLLFVEQLyEVQHSCFA 101
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI------AISAGLSGQLTGIENI-EFKMLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 102 LD---------DLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQ-SVSVLTSILKYLKQYA 171
Cdd:PRK13546 115 FKrkeikamtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfAQKCLDKIYEFKEQNK 194
|
170
....*....|.
gi 1248686454 172 TVILTSHDEAQ 182
Cdd:PRK13546 195 TIFFVSHNLGQ 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-185 |
1.41e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.96 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING----QVSYAP--DHLPKSITLTVQQYLLfVEQLYEV 95
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKISDAElrEVRRKKIAMVFQSFAL-MPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 96 QHSCFALD--------------DLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLT 161
Cdd:PRK10070 125 DNTAFGMElaginaeerrekalDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180
....*....|....*....|....*...
gi 1248686454 162 SILKYL--KQYATVILTSH--DEAQHYG 185
Cdd:PRK10070 205 DELVKLqaKHQRTIVFISHdlDEAMRIG 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-147 |
1.66e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 51.72 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVsyapdhlpksIT-LTVQQYL-----------LFvEQLYEVQHsc 99
Cdd:COG4615 360 LVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP----------VTaDNREAYRqlfsavfsdfhLF-DRLLGLDG-- 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248686454 100 FALDDLIQ----RFHIE--------AF----LSQpikqcskGtQQK-LNLIQCLLKQADIYILDE 147
Cdd:COG4615 427 EADPARARelleRLELDhkvsvedgRFsttdLSQ-------G-QRKrLALLVALLEDRPILVFDE 483
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-178 |
1.79e-07 |
|
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: 50.69 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLFVEQL 92
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdiRDISRKSLRSMIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 YE-------------VQHSCFA--LDDLIQRFH--IEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQ 155
Cdd:cd03254 94 MEnirlgrpnatdeeVIEAAKEagAHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180
....*....|....*....|...
gi 1248686454 156 SVSVLTSILKYLKQYATVILTSH 178
Cdd:cd03254 174 TEKLIQEALEKLMKGRTSIIIAH 196
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-178 |
2.58e-07 |
|
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: 49.46 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLA--------QIYKPTVGNVTINGQVSYAPDHlpksiTLTvqqyl 86
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLFLPQRPYLPLG-----TLR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 87 lfvEQLyevqhsCFALDDLIqrfhieaflsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKy 166
Cdd:cd03223 82 ---EQL------IYPWDDVL----------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK- 135
|
170
....*....|..
gi 1248686454 167 lKQYATVILTSH 178
Cdd:cd03223 136 -ELGITVISVGH 146
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-179 |
2.87e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.50 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 1 MDLAIKGKSL-------TKVINGqvifsdMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDH 73
Cdd:PRK13647 1 MDNIIEVEDLhfrykdgTKALKG------LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 74 --LPKSITLTVQ----QylLFVEQLYE-----VQHSCFALDDLIQRFH-------IEAFLSQPIKQCSKGTQQKLNLIQC 135
Cdd:PRK13647 75 kwVRSKVGLVFQdpddQ--VFSSTVWDdvafgPVNMGLDKDEVERRVEealkavrMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1248686454 136 LLKQADIYILDEPFSGLDKQSVSVLTSILKYL-KQYATVILTSHD 179
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHD 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-179 |
3.47e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 3 LAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNV--TINGQVSY-APDH---LPK 76
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYyAQDHaydFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 77 SITLT--VQQY----------------LLFVEqlyevqhscfalDDliqrfhieafLSQPIKQCSKGTQQKLNLIQCLLK 138
Cdd:PRK15064 398 DLTLFdwMSQWrqegddeqavrgtlgrLLFSQ------------DD----------IKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1248686454 139 QADIYILDEPFSGLDKQSVSVLTSILKYLKqyATVILTSHD 179
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKYE--GTLIFVSHD 494
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-178 |
3.90e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 37 GANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPD---------HLPK-SITLTVQQYLLFVEQLY-----EVQHSCFA 101
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrsrfmaylgHLPGlKADLSTLENLHFLCGLHgrrakQMPGSALA 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248686454 102 LDDLIQrfHIEAFlsqpIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILK-YLKQYATVILTSH 178
Cdd:PRK13543 124 IVGLAG--YEDTL----VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-178 |
3.94e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYkPT---VGNVTINGQVSYApdhlpKSITLT--- 81
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQA-----SNIRDTera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 82 ----VQQYLLFVEQL---------YEVQHSCFALDD--------LIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQA 140
Cdd:PRK13549 83 giaiIHQELALVKELsvleniflgNEITPGGIMDYDamylraqkLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1248686454 141 DIYILDEPFSGLDKQSVSVLTSILKYLKQYA-TVILTSH 178
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGiACIYISH 201
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-181 |
4.26e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 4 AIKGKSLTKVINGQVIFSDMtiefpnqsiIQIVGANGSGKSVTLK-MLAQIyKPTVGNVTING--QVSYAPDHL----PK 76
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDK---------IALIGPNGCGKTTLLKlMLGQL-QADSGRIHCGTklEVAYFDQHRaeldPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 77 SitlTVQQYLLFVEQLYEV----QHSCFALDDLIqrFHIEAFLsQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGL 152
Cdd:PRK11147 398 K---TVMDNLAEGKQEVMVngrpRHVLGYLQDFL--FHPKRAM-TPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180 190
....*....|....*....|....*....|
gi 1248686454 153 DKQSVSVLTSIlkyLKQY-ATVILTSHDEA 181
Cdd:PRK11147 472 DVETLELLEEL---LDSYqGTVLLVSHDRQ 498
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-190 |
4.35e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 50.61 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 3 LAIKGKSLTKVINgqviFSdmtieFPNQSIIQIVGANGSGKSVTLKMLAQiYKPTVGNVTINGQ---------------- 66
Cdd:PRK11174 358 LSPDGKTLAGPLN----FT-----LPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIelreldpeswrkhlsw 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 67 VSYAPdHLPKSitlTVQQYLLfveqLYEVQHSCFALDDLIQRFHIEAFLSQ-------PIKQ----CSKGTQQKLNLIQC 135
Cdd:PRK11174 428 VGQNP-QLPHG---TLRDNVL----LGNPDASDEQLQQALENAWVSEFLPLlpqgldtPIGDqaagLSVGQAQRLALARA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1248686454 136 LLKQADIYILDEPFSGLDKQS-VSVLTSILKYLKQYATViltshdeaqhygLVTHQ 190
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSeQLVMQALNAASRRQTTL------------MVTHQ 543
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-180 |
5.35e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 49.95 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSyapDHLP--KSITLTV-QQ 84
Cdd:PRK09452 18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI---THVPaeNRHVNTVfQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 85 YLLFvEQLYEVQHSCFALD--------------DLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFS 150
Cdd:PRK09452 95 YALF-PHMTVFENVAFGLRmqktpaaeitprvmEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190
....*....|....*....|....*....|..
gi 1248686454 151 GLDKQSVSVLTSILKYL--KQYATVILTSHDE 180
Cdd:PRK09452 174 ALDYKLRKQMQNELKALqrKLGITFVFVTHDQ 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
115-179 |
5.66e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 5.66e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248686454 115 LSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTsilKYLKQYA-TVILTSHD 179
Cdd:PRK10636 143 LERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLE---KWLKSYQgTLILISHD 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-179 |
6.43e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.22 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-QVSYAP-DHLPKSITLTVQ----QYL-LFVEQ--L 92
Cdd:PRK13632 27 NVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGiTISKENlKEIRKKIGIIFQnpdnQFIgATVEDdiA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 YEVQHSCFA-------LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILK 165
Cdd:PRK13632 107 FGLENKKVPpkkmkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMV 186
|
170
....*....|....*.
gi 1248686454 166 YLKQYA--TVILTSHD 179
Cdd:PRK13632 187 DLRKTRkkTLISITHD 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-153 |
9.21e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 37 GANGSGKSVTLKMLAQIYKPTVGNVTINGQvsyAPDhlPKSIT-----------------LTVQQYLLFVEQLYEV--QH 97
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVD--AGDIAtrrrvgymsqafslygeLTVRQNLELHARLFHLpaAE 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1248686454 98 SCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:NF033858 374 IAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-182 |
1.00e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 1 MDLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYK-----PTVGNVTINGQVSYAPDHLP 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 76 KSIT---------------LTVQQYLLFVEQLYEVQHSCFALDDLIQRFHIEAFLSQPIK--------QCSKGTQQKLNL 132
Cdd:PRK14267 81 IEVRrevgmvfqypnpfphLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQRQRLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1248686454 133 IQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYATVILTSHDEAQ 182
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQ 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
76-207 |
1.09e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 76 KSITLTVQQYLLFVEQLYEVQHSCfALDDLIQRFHIEAFLSQ-PIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDk 154
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQ-IIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD- 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248686454 155 qsVSVLTSILKYLKQYA----TVILTSHDEAQHYG-----LVTHQFKLSTQRLMKLTEQAQV 207
Cdd:TIGR02633 436 --VGAKYEIYKLINQLAqegvAIIVVSSELAEVLGlsdrvLVIGEGKLKGDFVNHALTQEQV 495
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-153 |
1.18e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.25 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--------------VSYAPD-------HLPKSI----TLTVQQYL--- 86
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPEdrkgeglVLDLSIreniTLASLDRLsrg 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248686454 87 LFVEQLYEVQHScfalDDLIQRFHIEAF-LSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:COG1129 363 GLLDRRRERALA----EEYIKRLRIKTPsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-188 |
1.50e-06 |
|
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: 49.24 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ------------VSYAPDHLPKSITLTVQQYLLFVEQLYEVQHSCF-- 100
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisdvhqnMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIek 2049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 101 ALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVL-TSILKYLKQYATVILTSHD 179
Cdd:TIGR01257 2050 VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHS 2129
|
....*....
gi 1248686454 180 EAQHYGLVT 188
Cdd:TIGR01257 2130 MEECEALCT 2138
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-178 |
1.53e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 16 GQVIFsDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQV--SYAPDHLPKSITLTVQQYLLFVE-QL 92
Cdd:PRK13649 20 GRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitSTSKNKDIKQIRKKVGLVFQFPEsQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 YEVQhscfALDDLI---QRFHI-------------------EAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFS 150
Cdd:PRK13649 99 FEET----VLKDVAfgpQNFGVsqeeaealareklalvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180
....*....|....*....|....*....
gi 1248686454 151 GLDKQSVSVLTSILKYLKQYA-TVILTSH 178
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGmTIVLVTH 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-179 |
1.56e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 10 LTKVINGQ-VIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTI--NGQVSYAPDHLPKSITLTVQQyl 86
Cdd:PRK11819 12 VSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPapGIKVGYLPQEPQLDPEKTVRE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 87 lfveqlyEVQHSCFALDDLIQRFH----------------------------------IEAFLSQ------------PIK 120
Cdd:PRK11819 90 -------NVEEGVAEVKAALDRFNeiyaayaepdadfdalaaeqgelqeiidaadawdLDSQLEIamdalrcppwdaKVT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 121 QCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTsilKYLKQYA-TVILTSHD 179
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE---QFLHDYPgTVVAVTHD 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-179 |
1.58e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.04 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTIN-----------GQVSYAPDH----LPKSITLTVQQYLLF-----VEQ 91
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkdGQLKVADKNqlrlLRTRLTMVFQHFNLWshmtvLEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 92 LYEVQHSCFALDDLIQRFHIEAFLSQ-----------PIkQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVL 160
Cdd:PRK10619 113 VMEAPIQVLGLSKQEARERAVKYLAKvgideraqgkyPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEV 191
|
170 180
....*....|....*....|
gi 1248686454 161 TSILKYLKQYA-TVILTSHD 179
Cdd:PRK10619 192 LRIMQQLAEEGkTMVVVTHE 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-153 |
1.88e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.18 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLPKSITLTVQQYLL 87
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 88 F-------------------VEQLYEVQHSCFALDDLiqrfhiEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEP 148
Cdd:PRK11432 90 FphmslgenvgyglkmlgvpKEERKQRVKEALELVDL------AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
....*
gi 1248686454 149 FSGLD 153
Cdd:PRK11432 164 LSNLD 168
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-181 |
1.97e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 47.48 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 8 KSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTV---GNVTINGQvsyAPDHLP---KSITLT 81
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGR---RLTALPaeqRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 82 VQQYLLFvEQLYEVQHSCFALDDLIQR----FHIEAFLSQ---------PIKQCSKGTQQKLNLIQCLLKQADIYILDEP 148
Cdd:COG4136 82 FQDDLLF-PHLSVGENLAFALPPTIGRaqrrARVEQALEEaglagfadrDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1248686454 149 FSGLDKQ-SVSVLTSILKYLKQYAT-VILTSHDEA 181
Cdd:COG4136 161 FSKLDAAlRAQFREFVFEQIRQRGIpALLVTHDEE 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-178 |
1.99e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.12 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 3 LAIKGKSLTKVINGQVIFS-----DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTING------QVSYAp 71
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkKVKLS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 72 dHLPKSITLTVQ--QYLLFVEQLY---------------EVQHSCFALDDLIQrFHIEAFLSQPIKQCSKGTQQKLNLIQ 134
Cdd:PRK13637 80 -DIRKKVGLVFQypEYQLFEETIEkdiafgpinlglseeEIENRVKRAMNIVG-LDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1248686454 135 CLLKQADIYILDEPFSGLD-KQSVSVLTSILKYLKQY-ATVILTSH 178
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDpKGRDEILNKIKELHKEYnMTIILVSH 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-178 |
2.00e-06 |
|
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: 48.65 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQI--YKPTVGNVTINgqVSYAPD---------- 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH--VALCEKcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 73 ---------------------------HLPKSITLTVQQ-YLLFVEQL-------------YEVQHSCFALDDLIQRFHI 111
Cdd:TIGR03269 79 gepcpvcggtlepeevdfwnlsdklrrRIRKRIAIMLQRtFALYGDDTvldnvlealeeigYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248686454 112 EAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVS-VLTSILKYLKQYA-TVILTSH 178
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKlVHNALEEAVKASGiSMVLTSH 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-178 |
2.18e-06 |
|
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: 47.41 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDH-LPKSITLTVQQYLLFVEQLYEvq 96
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdISTIPLEdLRSSLTIIPQDPTLFSGTIRS-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 97 hscfALDDLIQRFHIEAFLSQPIKQ----CSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYAT 172
Cdd:cd03369 101 ----NLDPFDEYSDEEIYGALRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNST 176
|
....*.
gi 1248686454 173 VILTSH 178
Cdd:cd03369 177 ILTIAH 182
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-180 |
2.40e-06 |
|
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: 47.22 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 21 SDMTIEFpNQSIIQIVGANGSGKSVTLKMLaqiykptvgNVTINGQV---SYAPDHLPKSITLT---VQQYLLFVE---Q 91
Cdd:cd03240 14 ERSEIEF-FSPLTLIVGQNGAGKTTIIEAL---------KYALTGELppnSKGGAHDPKLIREGevrAQVKLAFENangK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 92 LYEVQHSCFALDDLIqrF----HIEAFLSQPIKQCSKGTQQKLNLI------QCLLKQADIYILDEPFSGLDKQSVS-VL 160
Cdd:cd03240 84 KYTITRSLAILENVI--FchqgESNWPLLDMRGRCSGGEKVLASLIirlalaETFGSNCGILALDEPTTNLDEENIEeSL 161
|
170 180
....*....|....*....|..
gi 1248686454 161 TSILKYLKQYAT--VILTSHDE 180
Cdd:cd03240 162 AEIIEERKSQKNfqLIVITHDE 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-178 |
2.41e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 37 GANGSGKSVTLKMLAQIYKPTVGNVTINGQ----------------VSYAPDHL-PKsitLTVQQYLL---------FV- 89
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagvaIIYQELHLvPE---MTVAENLYlgqlphkggIVn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 90 -EQLYEvqhscFALDDLiQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLK 168
Cdd:PRK11288 114 rRLLNY-----EAREQL-EHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELR 187
|
170
....*....|.
gi 1248686454 169 QYATVIL-TSH 178
Cdd:PRK11288 188 AEGRVILyVSH 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-179 |
2.64e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.49 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 28 PNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ----------------VSYAPDHlpKSITLTVQQYLLFVEQ 91
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvglVFQNPDD--QIFSPTVEQDIAFGPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 92 LYEVQHSCFA--LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYL-K 168
Cdd:PRK13652 106 NLGLDEETVAhrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpE 185
|
170
....*....|..
gi 1248686454 169 QYA-TVILTSHD 179
Cdd:PRK13652 186 TYGmTVIFSTHQ 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-185 |
3.09e-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: 48.37 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDH---LPKSITLTVQQYLLFVEQLY-E 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTswiMPGTIKDNIIFGLSYDEYRYtS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 95 VQHSCfALDDLIQRF--HIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD-----------------KQ 155
Cdd:TIGR01271 521 VIKAC-QLEEDIALFpeKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvtekeifesclcklmsNK 599
|
170 180 190
....*....|....*....|....*....|
gi 1248686454 156 SVSVLTSILKYLKQYATVILTSHDEAQHYG 185
Cdd:TIGR01271 600 TRILVTSKLEHLKKADKILLLHEGVCYFYG 629
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-182 |
3.50e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.40 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 4 AIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQI------YKPTvGNVTINGQVSY-------- 69
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYS-GDVLLGGRSIFnyrdvlef 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 70 ---------APDHLPKSITLTV-----QQYLLFVEQLYEVQHScfALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQC 135
Cdd:PRK14271 100 rrrvgmlfqRPNPFPMSIMDNVlagvrAHKLVPRKEFRGVAQA--RLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1248686454 136 LLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYATVILTSHDEAQ 182
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQ 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
35-179 |
4.25e-06 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 47.04 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLP---KSITLTVQ----QyllFVEQLYE--VqhsCFAL--- 102
Cdd:TIGR04520 33 IIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirKKVGMVFQnpdnQ---FVGATVEddV---AFGLenl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 103 -----------DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYA 171
Cdd:TIGR04520 107 gvpreemrkrvDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEE 186
|
170
....*....|
gi 1248686454 172 --TVILTSHD 179
Cdd:TIGR04520 187 giTVISITHD 196
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-179 |
5.13e-06 |
|
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: 45.89 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQvSYAPDHLPKSITLTVqqyllfveqlyevqhsCFALDDliqRFHI 111
Cdd:cd03215 28 IVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK-PVTRRSPRDAIRAGI----------------AYVPED---RKRE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248686454 112 EAFLSQPIK-------QCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD---KQSVSVLtsILKYLKQYATVILTSHD 179
Cdd:cd03215 88 GLVLDLSVAenialssLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvgaKAEIYRL--IRELADAGKAVLLISSE 163
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-173 |
6.39e-06 |
|
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: 45.72 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 31 SIIQIVGANGSGKSVTLKMLAQIykpTVGNVTINGQVSYaPDHLPKSITLTVQQYLLFVEQlyevQHSCFALddLIQRFH 110
Cdd:cd03233 34 EMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHY-NGIPYKEFAEKYPGEIIYVSE----EDVHFPT--LTVRET 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248686454 111 IEAFLS----QPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDkqSVSVLtSILKYLKQYATV 173
Cdd:cd03233 104 LDFALRckgnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SSTAL-EILKCIRTMADV 167
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-153 |
7.64e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 17 QVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHlPKSITLTVQQYLLFVEQLYEVQ 96
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ-AWIMNATVRGNILFFDEEDAAR 751
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248686454 97 hscfaLDDLIQRFHIEAFLSQ-------PIKQ----CSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:PTZ00243 752 -----LADAVRVSQLEADLAQlgggletEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-153 |
1.20e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 21 SDMTIEFPNQSIIQIVGANGSGK-SVTLKMLAQIYKPTVGNVTINGQVSYAPdHLPKSITLTVQQYLLF--------VEQ 91
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGTVAYVP-QVSWIFNATVRDNILFgspfdperYER 712
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248686454 92 LYEV---QHScfaLDDLIQRFHIEafLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:PLN03130 713 AIDVtalQHD---LDLLPGGDLTE--IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-179 |
1.65e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 2 DLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTInGQvsyapdhlpksitlT 81
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--------------T 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 82 VQqyLLFVEQLYEvqhscfALD-------------DLIQ--------RFHIEAF------LSQPIKQCSKGTQQKLNLIQ 134
Cdd:PRK11819 387 VK--LAYVDQSRD------ALDpnktvweeisgglDIIKvgnreipsRAYVGRFnfkggdQQKKVGVLSGGERNRLHLAK 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1248686454 135 cLLKQ-ADIYILDEPFSGLDkqsVSVLTSILKYLKQYA-TVILTSHD 179
Cdd:PRK11819 459 -TLKQgGNVLLLDEPTNDLD---VETLRALEEALLEFPgCAVVISHD 501
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-169 |
2.00e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 44.62 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 17 QVIFsDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ---VSYAPD-----HLPKSITLTVQQYLLF 88
Cdd:PRK11124 16 QALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSdkairELRRNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 89 -----VEQLYEVQHSCFALDD---------LIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDK 154
Cdd:PRK11124 95 phltvQQNLIEAPCRVLGLSKdqalaraekLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170
....*....|....*
gi 1248686454 155 QSVSVLTSILKYLKQ 169
Cdd:PRK11124 175 EITAQIVSIIRELAE 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-194 |
2.22e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 32 IIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAP-DHLPKSI----------------------TLTVQQYl 86
Cdd:PRK10762 280 ILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPqDGLANGIvyisedrkrdglvlgmsvkenmSLTALRY- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 87 lFVEQLYEVQHSC--FALDDLIQRFHIEA-FLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD---KQSVSVL 160
Cdd:PRK10762 359 -FSRAGGSLKHADeqQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgaKKEIYQL 437
|
170 180 190
....*....|....*....|....*....|....*....
gi 1248686454 161 tsILKYLKQYATVILTSHDEAQHYG-----LVTHQFKLS 194
Cdd:PRK10762 438 --INQFKAEGLSIILVSSEMPEVLGmsdriLVMHEGRIS 474
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-184 |
2.88e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.23 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 1 MDLAIKGKSLTKVINGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIY---KPTVGNVTINGQVSYAPDHLPKS 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 78 I------TLTVQQYLLFVEQLYEVQH-------------SCFALDDLIQ---------RFHIEAFLSQPIKQCSKGTQQK 129
Cdd:PRK09984 81 IrksranTGYIFQQFNLVNRLSVLENvligalgstpfwrTCFSWFTREQkqralqaltRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1248686454 130 LNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQY--ATVILTSH--DEAQHY 184
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHqvDYALRY 219
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
35-229 |
3.10e-05 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 45.18 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQiykptvgnvTINGQVSYAPDHLPksitltvqqylLFVEqlyevqhscfaLDDLIQRFHIEAF 114
Cdd:COG5635 185 ILGEPGSGKTTLLRYLAL---------ELAERYLDAEDPIP-----------ILIE-----------LRDLAEEASLEDL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 115 LSQPIKQCSKGTQQKLNLiqcLLKQAD-IYILDepfsGLD-----KQSVSVLTSILKYLKQY--ATVILTSHDEAQHYgl 186
Cdd:COG5635 234 LAEALEKRGGEPEDALER---LLRNGRlLLLLD----GLDevpdeADRDEVLNQLRRFLERYpkARVIITSRPEGYDS-- 304
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1248686454 187 vtHQFKLSTQ-RLMKLTEQAQVSY--KIIET------QFVSQIDLNELVREF 229
Cdd:COG5635 305 --SELEGFEVlELAPLSDEQIEEFlkKWFEAterkaeRLLEALEENPELREL 354
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-180 |
3.34e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 28 PNQSIIqIVGANGSGKSVTLKMLAQIYKPTVGNV-TINGQVSYAPDHLPKSITLTVQQYLLFveqlyevqhscfalddli 106
Cdd:smart00382 1 PGEVIL-IVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLIIVGGKKASG------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 107 qrfhieaflsqpikqcSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQY-------ATVILTSHD 179
Cdd:smart00382 62 ----------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLllkseknLTVILTTND 125
|
.
gi 1248686454 180 E 180
Cdd:smart00382 126 E 126
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-180 |
3.67e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.00 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 28 PNQSIiQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDH------LPKSITLTVQQYLLF--VEQLYEVQ--- 96
Cdd:PRK10584 35 RGETI-ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaklRAKHVGFVFQSFMLIptLNALENVElpa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 97 --------HSCFALDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYL- 167
Cdd:PRK10584 114 llrgessrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLn 193
|
170
....*....|....
gi 1248686454 168 KQYA-TVILTSHDE 180
Cdd:PRK10584 194 REHGtTLILVTHDL 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-153 |
5.28e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 43.69 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDH---LPKSITLTVQQYLLFVEQLYE- 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFswiMPGTIKENIIFGVSYDEYRYKs 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248686454 95 VQHSCfALDDLIQRF--HIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:cd03291 132 VVKAC-QLEEDITKFpeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-73 |
5.31e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.54 E-value: 5.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248686454 8 KSLTKVIN-GQV----IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ-VSYAPDH 73
Cdd:COG1101 5 KNLSKTFNpGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEY 76
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-156 |
5.98e-05 |
|
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: 44.04 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLFVEQLY--- 93
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdiRDVTQASLRAAIGIVPQDTVLFNDTIAyni 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 94 ----------EVQHScfalddlIQRFHIEAFlsqpIKQCSKG--TQ-------------QKLNLIQCLLKQADIYILDEP 148
Cdd:COG5265 453 aygrpdaseeEVEAA-------ARAAQIHDF----IESLPDGydTRvgerglklsggekQRVAIARTLLKNPPILIFDEA 521
|
....*...
gi 1248686454 149 FSGLDKQS 156
Cdd:COG5265 522 TSALDSRT 529
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-178 |
8.25e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLFV---------------EQLYEVQH 97
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvAKFGLTDLRRVLSIIPQSPVLFSgtvrfnidpfsehndADLWEALE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 98 SCFaLDDLIQR--FHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQYATVIL 175
Cdd:PLN03232 1347 RAH-IKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLV 1425
|
...
gi 1248686454 176 TSH 178
Cdd:PLN03232 1426 IAH 1428
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
33-179 |
9.91e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 42.67 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 33 IQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLP---------------KSITLTVQQYLLF-VEQL---- 92
Cdd:PRK13644 31 IGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirklvgivfqnpetQFVGRTVEEDLAFgPENLclpp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 YEVQHScfaLDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQS-VSVLTSILKYLKQYA 171
Cdd:PRK13644 111 IEIRKR---VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGK 187
|
....*...
gi 1248686454 172 TVILTSHD 179
Cdd:PRK13644 188 TIVYITHN 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-178 |
1.16e-04 |
|
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: 42.10 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 15 NGQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPKSITLTVQQYLLFVEQL 92
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiSKIGLHDLRSRISIIPQDPVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 93 YE-----VQHSCFALDDLIQRFHI-EAFLSQPIK----------QCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQS 156
Cdd:cd03244 95 RSnldpfGEYSDEELWQALERVGLkEFVESLPGGldtvveeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180
....*....|....*....|...
gi 1248686454 157 VSVLTSILK-YLKQyATVILTSH 178
Cdd:cd03244 175 DALIQKTIReAFKD-CTVLTIAH 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
101-153 |
1.44e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 1.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1248686454 101 ALDDLIQRFHIEAF-LSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD 153
Cdd:PRK13549 384 TILESIQRLKVKTAsPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-178 |
2.39e-04 |
|
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: 41.41 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 5 IKGKSLTKVINGQ----VIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ--VSYAPDHLPK-- 76
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdlTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 77 -SITLTVQQYLLF--------VEQLYEVQHSCFA-----LDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADI 142
Cdd:cd03258 82 rRIGMIFQHFNLLssrtvfenVALPLEIAGVPKAeieerVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1248686454 143 YILDEPFSGLDKQSVSvltSILKYLKQY-----ATVILTSH 178
Cdd:cd03258 162 LLCDEATSALDPETTQ---SILALLRDInrelgLTIVLITH 199
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-187 |
2.54e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 21 SDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTI-------------NGQVSYAPDHLPKSITLTVQQyll 87
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkgsaaliaissglNGQLTGIENIELKGLMMGLTK--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 88 fvEQLYEVqhscfaLDDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQ-SVSVLTSILKY 166
Cdd:PRK13545 118 --EKIKEI------IPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTfTKKCLDKMNEF 189
|
170 180 190
....*....|....*....|....*....|..
gi 1248686454 167 LKQYATVILTSHDEAQ-----------HYGLV 187
Cdd:PRK13545 190 KEQGKTIFFISHSLSQvksfctkalwlHYGQV 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-105 |
2.61e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 19 IFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDHLP---KSITLTVQQYLLFVEQLY-E 94
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKwwrSKIGVVSQDPLLFSNSIKnN 479
|
90
....*....|.
gi 1248686454 95 VQHSCFALDDL 105
Cdd:PTZ00265 480 IKYSLYSLKDL 490
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
117-201 |
3.72e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.58 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 117 QPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLD---------------KQSVSVL--TSILKYLKQYATVILTSHD 179
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDvsarndiyqlirsiaAQNVAVLfiSSDLEEIEQMADRVLVMHQ 478
|
90 100
....*....|....*....|..
gi 1248686454 180 EAQHYGLVTHQfkLSTQRLMKL 201
Cdd:PRK15439 479 GEISGALTGAA--INVDTIMRL 498
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
33-179 |
3.75e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 41.23 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 33 IQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPD--HLPKSITLTVQ----QYL-LFVEQ--LYEVQHSCFALD 103
Cdd:PRK13642 36 VSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwNLRRKIGMVFQnpdnQFVgATVEDdvAFGMENQGIPRE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 104 DLIQR-------FHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQ--YATVI 174
Cdd:PRK13642 116 EMIKRvdeallaVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVL 195
|
....*
gi 1248686454 175 LTSHD 179
Cdd:PRK13642 196 SITHD 200
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
9-213 |
3.97e-04 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 40.31 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 9 SLTKVINGQVIFSDmtIEFPNQSIIQIVGANGSGKSVTLKMLAQIykptvgnvTINGQV-SYAPdhlpksitltvqqyll 87
Cdd:cd03243 10 LLALTKGETFVPND--INLGSGRLLLITGPNMGGKSTYLRSIGLA--------VLLAQIgCFVP---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 88 fveqlyeVQHSCFALDDLIqrF-HIEAflSQPIKQCsKGTQQ----KLNLIQCLLKQADIYILDEPFSG---LDKQSVSV 159
Cdd:cd03243 64 -------AESASIPLVDRI--FtRIGA--EDSISDG-RSTFMaellELKEILSLATPRSLVLIDELGRGtstAEGLAIAY 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248686454 160 ltSILKYLKQY-ATVILTSH------DEAQHYGLVTHQFKlstqrLMKLTEQAQVSYKIIE 213
Cdd:cd03243 132 --AVLEHLLEKgCRTLFATHfheladLPEQVPGVKNLHME-----ELITTGGLTFTYKLID 185
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-180 |
4.61e-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: 40.32 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSV----------------TLKM-----LAQIYKPTVGNVTiNGQVSYAPD-----HLP 75
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveSLSAyarqfLGQMDKPDVDSIE-GLSPAIAIDqkttsRNP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 76 KSITLTVQQYLLFVEQLyevqhscFALDDLIQR--FHIEA-----FLSQPIKQCSKGTQQKLNLIQCLLKQAD--IYILD 146
Cdd:cd03270 92 RSTVGTVTEIYDYLRLL-------FARVGIRERlgFLVDVglgylTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLD 164
|
170 180 190
....*....|....*....|....*....|....*
gi 1248686454 147 EPFSGLDKQSVSVLTSILKYLKQYA-TVILTSHDE 180
Cdd:cd03270 165 EPSIGLHPRDNDRLIETLKRLRDLGnTVLVVEHDE 199
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
35-66 |
5.13e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.54 E-value: 5.13e-04
10 20 30
....*....|....*....|....*....|..
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ 66
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDH 75
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-178 |
6.67e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.05 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 16 GQVIFSDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKpTVGNVTINGqVSYAPDHLP---KSITLTVQQYLLFV--- 89
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG-VSWNSVTLQtwrKAFGVIPQKVFIFSgtf 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 90 ------------EQLYEVQHSCfALDDLIQRF--HIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQ 155
Cdd:TIGR01271 1309 rknldpyeqwsdEEIWKVAEEV-GLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180
....*....|....*....|...
gi 1248686454 156 SVSVLTSILKYLKQYATVILTSH 178
Cdd:TIGR01271 1388 TLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-66 |
8.61e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 39.80 E-value: 8.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248686454 6 KGKSLTKVINgqvifsDMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ 66
Cdd:PRK11629 17 EGSVQTDVLH------NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ 71
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-181 |
9.03e-04 |
|
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: 39.23 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 25 IEFPNQSIIQIVGANGSGKSvTLkMLAQIYKptVGNVTINGQVSYAPDHLpksitltvqqyLLFVEQLyevqhscfaldd 104
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKS-TL-VNEGLYA--SGKARLISFLPKFSRNK-----------LIFIDQL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 105 liqRFHIEA-----FLSQPIKQCSKGTQQKLNLIQCLLKQAD--IYILDEPFSGLDKQSVSVLTSILKYLKQYA-TVILT 176
Cdd:cd03238 69 ---QFLIDVglgylTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGnTVILI 145
|
....*
gi 1248686454 177 SHDEA 181
Cdd:cd03238 146 EHNLD 150
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
103-183 |
9.41e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 103 DDLIQRFHIEAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVS-VLTSILKYLKQYATVILTSH--D 179
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNeVWDEVRSMVRDGATVLLTTQymE 205
|
....
gi 1248686454 180 EAQH 183
Cdd:NF000106 206 EAEQ 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-184 |
1.03e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 39.62 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 22 DMTIEFPNQSIIQIVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYA---PDHLpKSITLTVQQYLLFVE-QLYE--V 95
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkkNKKL-KPLRKKVGIVFQFPEhQLFEetV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 96 QHS-CF-----------AL---DDLIQRFHI-EAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSV 159
Cdd:PRK13634 104 EKDiCFgpmnfgvseedAKqkaREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKE 183
|
170 180
....*....|....*....|....*....
gi 1248686454 160 LTSILKYLKQYA--TVILTSH--DEAQHY 184
Cdd:PRK13634 184 MMEMFYKLHKEKglTTVLVTHsmEDAARY 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
35-66 |
1.42e-03 |
|
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: 38.95 E-value: 1.42e-03
10 20 30
....*....|....*....|....*....|..
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ 66
Cdd:COG4181 43 IVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ 74
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
112-179 |
1.85e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 38.91 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248686454 112 EAFLSQPIKQCSKGTQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYL-KQYATVILTSHD 179
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHD 224
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
118-179 |
1.88e-03 |
|
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: 38.91 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248686454 118 PIKQCSKGTQQKLNLI---QCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQY-ATVILTSHD 179
Cdd:pfam13304 233 PAFELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgAQLILTTHS 298
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-178 |
2.17e-03 |
|
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: 39.54 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 33 IQIVGANGSGKSVTLKMLAQIYKPTVGNVTING-QVSYAPDH-LPKSITLTVQQYLLFVEQL---------YEVQHSCFA 101
Cdd:TIGR00957 1315 VGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAKIGLHdLRFKITIIPQDPVLFSGSLrmnldpfsqYSDEEVWWA 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248686454 102 LddliQRFHIEAFLS-QPIK---QCSKG-------TQQKLNLIQCLLKQADIYILDEPFSGLDKQSVSVLTSILKYLKQY 170
Cdd:TIGR00957 1395 L----ELAHLKTFVSaLPDKldhECAEGgenlsvgQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED 1470
|
....*...
gi 1248686454 171 ATVILTSH 178
Cdd:TIGR00957 1471 CTVLTIAH 1478
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
35-66 |
4.36e-03 |
|
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: 37.65 E-value: 4.36e-03
10 20 30
....*....|....*....|....*....|..
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQ 66
Cdd:COG0410 34 LLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE 65
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
20-51 |
8.12e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.90 E-value: 8.12e-03
10 20 30
....*....|....*....|....*....|...
gi 1248686454 20 FSDMTIEFPNQSIIQ-IVGANGSGKSVTLKMLA 51
Cdd:COG3950 14 FEDLEIDFDNPPRLTvLVGENGSGKTTLLEAIA 46
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-179 |
8.59e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 8.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248686454 115 LSQPIKQCSKGTQQKLNLIQCLL---KQADIYILDEPFSGLDKQSVSVLTSILKYL-KQYATVILTSHD 179
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLtHQGHTVVIIEHN 871
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
35-73 |
9.17e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 36.87 E-value: 9.17e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1248686454 35 IVGANGSGKSVTLKMLAQIYKPTVGNVTINGQVSYAPDH 73
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
|
| |
