|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-209 |
2.66e-80 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 242.66 E-value: 2.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN-DNVLEDFGIM 80
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDpAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IE-PVFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:COG1131 79 PQePALYPDLTVRENLRFFARLYGlpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 158 FVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:COG1131 159 TSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-213 |
4.84e-69 |
|
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: 212.85 E-value: 4.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDfySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI 81
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 E-PVFYPEMSVIDNLKFYLKLHGKKelYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVG 160
Cdd:cd03268 79 EaPGFYPNLTARENLRLLARLLGIR--KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 161 LDPVGVQKLIDILKKWSSErQISMLISSHQLGELEALCNRYIYIEGGKLAESF 213
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-249 |
6.66e-66 |
|
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: 206.25 E-value: 6.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-VLEDFGI 79
Cdd:COG4555 1 MIEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MI-EPVFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDE 156
Cdd:COG4555 79 LPdERGLYDRLTVRENIRYFAELYGlfDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 157 PFVGLDPVGVQKLIDILKKWSSERQIsMLISSHQLGELEALCNRYIYIEGGKLaesfigKAQPSlVVHLNSKYHMCNLKD 236
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKV------VAQGS-LDELREEIGEENLED 230
|
250
....*....|...
gi 1937413360 237 HISQGITLRDGLL 249
Cdd:COG4555 231 AFVALIGSEEGEA 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-209 |
1.07e-62 |
|
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: 195.31 E-value: 1.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPgnDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-VLEDFGIM 80
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IE-PVFYPEMSVIDNLKFylklhgkkelysniertlklvelwesrnrkpkgfSFGMKQRTALAIALVAEPDFLILDEPFV 159
Cdd:cd03230 79 PEePSLYENLTVRENLKL----------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 160 GLDPVGVQKLIDILKKWSSErQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-209 |
8.78e-57 |
|
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: 181.93 E-value: 8.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN-DNVLEDFGIM 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDrKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 ieP---VFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILD 155
Cdd:cd03263 81 --PqfdALFDELTVREHLRFYARLKGlpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 156 EPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-208 |
1.09e-56 |
|
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: 181.51 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 3 KIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMIE 82
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS--LKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 PVF-YPE-----MSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:cd03225 79 LVFqNPDdqffgPTVEEEVAFGLENLGlpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 155 DEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-210 |
3.43e-55 |
|
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: 178.29 E-value: 3.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGnDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND--NVLEDFGI 79
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlrELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 miepVF-YPE-----MSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:COG1122 80 ----VFqNPDdqlfaPTVEEDVAFGPENLGlpREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-208 |
3.77e-53 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 175.30 E-value: 3.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIM 80
Cdd:COG4152 1 MLELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED--RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IE-PVFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:COG4152 77 PEeRGLYPKMKVGEQLVYLARLKGlsKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 158 FVGLDPVGVQKLIDILKKwSSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:COG4152 157 FSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-211 |
7.23e-53 |
|
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: 172.31 E-value: 7.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYS--LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNV-LEDF 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIEPVFY-------PEMSVIDNLKFYLKLHGKKELYSNIERT----LKLVELWESR-NRKPKGFSFGMKQRTALAIAL 145
Cdd:cd03257 81 RKEIQMVFQdpmsslnPRMTIGEQIAEPLRIHGKLSKKEARKEAvlllLVGVGLPEEVlNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 146 VAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-208 |
6.70e-51 |
|
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: 166.50 E-value: 6.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN-DNVLEDFGI 79
Cdd:COG4133 2 MLEAENLSCRRGERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDArEDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MI-EPVFYPEMSVIDNLKFYLKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPF 158
Cdd:COG4133 80 LGhADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 159 VGLDPVGVQKLIDILKKWSSERQIsMLISSHQlgELEALCNRYIYIEGGK 208
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGA-VLLTTHQ--PLELAAARVLDLGDFK 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-212 |
1.08e-50 |
|
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: 166.21 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDfySLSDVSLEIEKGeIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDI-NSNDNVLEDFGIM 80
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 I-EPVFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:cd03264 78 PqEFGVYPNFTVREFLDYIAWLKGipSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 158 FVGLDPVGVQKLIDILKKWSSERQIsmLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-209 |
1.78e-49 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 163.34 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDfySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI 81
Cdd:TIGR03740 1 LETKNLSKRFGKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD--LHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 E-PVFYPEMSVIDNLKFYLKLHGKKElySNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVG 160
Cdd:TIGR03740 77 EsPPLYENLTARENLKVHTTLLGLPD--SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937413360 161 LDPVGVQKLIDILKKWSSErQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:TIGR03740 155 LDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-211 |
1.92e-49 |
|
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: 162.69 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI 81
Cdd:cd03259 1 LELKGLSKTYGSVRA--LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -EPVFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPF 158
Cdd:cd03259 79 qDYALFPHLTVAENIAFGLKLRGvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 159 VGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-212 |
7.64e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 169.31 E-value: 7.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFP---GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVLED 76
Cdd:COG1123 260 LLEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGIMIEPVF---Y----PEMSVIDNLKFYLKLHG---KKELYSNIERTLKLVELWES-RNRKPKGFSFGMKQRTALAIAL 145
Cdd:COG1123 340 LRRRVQMVFqdpYsslnPRMTVGDIIAEPLRLHGllsRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 146 VAEPDFLILDEPFVGLDpVGVQ-KLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:COG1123 420 ALEPKLLILDEPTSALD-VSVQaQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-211 |
8.54e-49 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 161.37 E-value: 8.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-------- 72
Cdd:COG2884 1 MIRFENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreipylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 ----VLEDFGIMiepvfyPEMSVIDNLKFYLKLHGK--KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:COG2884 80 rigvVFQDFRLL------PDRTVYENVALPLRVTGKsrKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKwSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-289 |
9.72e-48 |
|
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: 161.40 E-value: 9.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 9 KKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN-DNVLEDFGIMIE-PVFY 86
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREpRKVRRSIGIVPQyASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 87 PEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPV 164
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGlpKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 165 GVQKLIDILKKWSSErQISMLISSHQLGELEALCNRYIYIEGGKLA--------ESFIGK--------AQPSLVVHLNSK 228
Cdd:TIGR01188 159 TRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIaegtpeelKRRLGKdtlesrprDIQSLKVEVSML 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 229 YHMCNLKDHISQGITLRDGLLDIPISVDKEALNDIFGVLASESL-IESIEVKENHLKEVFMK 289
Cdd:TIGR01188 238 IAELGETGLGLLAVTVDSDRIKILVPDGDETVPEIVEAAIRNGIrIRSISTERPSLDDVFLK 299
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-200 |
1.15e-47 |
|
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: 158.40 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFY--SLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNvleDFGI 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MI-EPVFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDE 156
Cdd:cd03293 78 VFqQDALLPWLTVLDNVALGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937413360 157 PFVGLDPVGVQKLID-ILKKWSSERQISMLIsSHQLGELEALCNR 200
Cdd:cd03293 158 PFSALDALTREQLQEeLLDIWRETGKTVLLV-THDIDEAVFLADR 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-213 |
1.44e-47 |
|
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: 158.90 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGN--DFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN------ 72
Cdd:cd03258 1 MIELKNVSKVFGDTggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 ------VLEDFGIMIEPvfypemSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIA 144
Cdd:cd03258 81 rrrigmIFQHFNLLSSR------TVFENVALPLEIAGvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 145 LVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAESF 213
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-208 |
4.48e-47 |
|
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: 156.67 E-value: 4.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNvlEDFGIMI 81
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR--NRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPV-FYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPF 158
Cdd:cd03269 77 EERgLYPKMKVIDQLVYLAQLKGlkKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 159 VGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:cd03269 157 SGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-210 |
1.47e-46 |
|
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: 155.60 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF--PGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND-NVLEDF 77
Cdd:cd03266 1 MITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIEPV-FYPEMSVIDNLKFYLKLHGKK--ELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:cd03266 81 GFVSDSTgLYDRLTARENLEYFAGLYGLKgdELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 155 DEPFVGLDPVGVQKLIDILKKWSSErQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-208 |
7.91e-46 |
|
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: 152.34 E-value: 7.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDF---- 77
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMI-EPVFYPEMSVIDNLKFylklhgkkelysniertlklvelwesrnrkpkGFSFGMKQRTALAIALVAEPDFLILDE 156
Cdd:cd03229 79 GMVFqDFALFPHLTVLENIAL--------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 157 PFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-210 |
1.06e-45 |
|
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: 153.68 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN-DNVLEDFGIMI- 81
Cdd:cd03265 3 VENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREpREVRRRIGIVFq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVFYPEMSVIDNLKFYLKLHGKK--ELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFV 159
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPgaERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 160 GLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-211 |
5.75e-44 |
|
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: 149.51 E-value: 5.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVLEDFGI- 79
Cdd:cd03219 1 LEVRGLTKRFGG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIARLGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 ----MIEPvfYPEMSVIDNL------------KFYLKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAI 143
Cdd:cd03219 79 rtfqIPRL--FPELTVLENVmvaaqartgsglLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 144 ALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRyIYI--EGGKLAE 211
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADR-VTVldQGRVIAE 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-209 |
7.25e-44 |
|
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: 149.36 E-value: 7.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND-----NVLE 75
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 DFGImiepVF-----YPEMSVIDNLKFYLKLHGK---KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVA 147
Cdd:COG1127 83 RIGM----LFqggalFDSLTVFENVAFPLREHTDlseAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-209 |
2.35e-43 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 147.25 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGND--FYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVLEDF- 77
Cdd:cd03255 1 IELKNLSKTYGGGGekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 ----GImiepVF--Y---PEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:cd03255 81 rrhiGF----VFqsFnllPDLTALENVELPLLLAGvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLgELEALCNRYIYIEGGKL 209
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-211 |
2.82e-43 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 148.26 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDI------------- 67
Cdd:COG0411 4 LLEVRGLTKRFGG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriarlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 68 -----NSNdnvledfgimiepVFyPEMSVIDNLKFYLKLHGKKELYSNIERT-----------------LKLVELWESRN 125
Cdd:COG0411 82 artfqNPR-------------LF-PELTVLENVLVAAHARLGRGLLAALLRLprarreereareraeelLERVGLADRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 126 RKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRyIYI- 204
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR-IVVl 226
|
....*...
gi 1937413360 205 -EGGKLAE 211
Cdd:COG0411 227 dFGRVIAE 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
3.78e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 3.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDfySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS----------N 70
Cdd:COG1121 6 AIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRarrrigyvpqR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 71 DNVLEDFgimiepvfyPeMSVID----NLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIA 144
Cdd:COG1121 84 AEVDWDF---------P-ITVRDvvlmGRYGRRGLFRrpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 145 LVAEPDFLILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-200 |
5.14e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.93 E-value: 5.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFP--GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvlEDFG 78
Cdd:COG1116 7 ALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---PDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMI-EPVFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILD 155
Cdd:COG1116 84 VVFqEPALLPWLTVLDNVALGLELRGvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937413360 156 EPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNR 200
Cdd:COG1116 164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADR 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-211 |
8.53e-42 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 144.07 E-value: 8.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFP--------------------GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKI 60
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 61 SYNGTdINSndnvledfgiMIEP--VFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMK 136
Cdd:COG1134 84 EVNGR-VSA----------LLELgaGFHPELTGRENIYLNGRLLGlsRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 137 QRTALAIALVAEPDFLILDEPF-VGlDPVGVQKLIDILKKwSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:COG1134 153 ARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-210 |
3.75e-41 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 141.52 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS----------NDNVLEDFGIMIEPV---- 84
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKerkrigyvpqRRSIDRDFPISVRDVvlmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 85 FYPEMSVIDNLKfylklhgkKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPV 164
Cdd:cd03235 95 LYGHKGLFRRLS--------KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937413360 165 GVQKLIDILKKWSSERqISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:cd03235 167 TQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-208 |
2.06e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 3 KIENLSKKFPGNdfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGImie 82
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 pVFYPEMSVidnlkfylklhgkkelysniertlklvelwesrnrkpkgfsfGMKQRTALAIALVAEPDFLILDEPFVGLD 162
Cdd:cd00267 76 -GYVPQLSG------------------------------------------GQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937413360 163 PVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:cd00267 113 PASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-211 |
5.00e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 139.02 E-value: 5.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFP--GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVL--- 74
Cdd:COG1136 4 LLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 75 --EDFGImiepVF--Y---PEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIAL 145
Cdd:COG1136 84 rrRHIGF----VFqfFnllPELTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 146 VAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLgELEALCNRYIYIEGGKLAE 211
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-211 |
6.07e-40 |
|
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: 138.83 E-value: 6.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInSNDNVLEDFGIMI 81
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -----EPVFYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:cd03218 78 gylpqEASIFRKLTVEENILAVLEIRGlsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 155 DEPFVGLDPVGV---QKLIDILKkwssERQISMLISSHQLGELEALCNR-YIYIEGGKLAE 211
Cdd:cd03218 158 DEPFAGVDPIAVqdiQKIIKILK----DRGIGVLITDHNVRETLSITDRaYIIYEGKVLAE 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-209 |
7.60e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.03 E-value: 7.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI 81
Cdd:COG4619 1 LELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP--PPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -----EPVFYPEmSVIDNLKFYLKLHGKKELYSNIERTLKLVELWES-RNRKPKGFSFGMKQRTALAIALVAEPDFLILD 155
Cdd:COG4619 77 ayvpqEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 156 EPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-212 |
9.14e-40 |
|
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: 145.05 E-value: 9.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPT---SGKISYNGTDINSNDnvLEDF 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS--EALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIEPVFYPEMS------VIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEP 149
Cdd:COG1123 82 GRRIGMVFQDPMTqlnpvtVGDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 150 DFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-163 |
1.20e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 141.36 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvledfgim 80
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEP-------VF-----YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:COG3839 70 LPPkdrniamVFqsyalYPHMTVYENIAFPLKLRKvpKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170
....*....|....*..
gi 1937413360 147 AEPDFLILDEPFVGLDP 163
Cdd:COG3839 150 REPKVFLLDEPLSNLDA 166
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-209 |
2.49e-39 |
|
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: 137.63 E-value: 2.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInSNDNVLED------F 77
Cdd:cd03261 3 LRGLTKSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI-SGLSEAELyrlrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GImiepVF-----YPEMSVIDNLKFYLKLHGK--KELYSNIER-TLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEP 149
Cdd:cd03261 80 GM----LFqsgalFDSLTVFENVAFPLREHTRlsEEEIREIVLeKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 150 DFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-209 |
1.14e-38 |
|
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: 135.93 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKfpGNDFySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI 81
Cdd:cd03299 1 LKVENLSKD--WKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EP-VFYPEMSVIDNLKFYLK--LHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPF 158
Cdd:cd03299 78 QNyALFPHMTVYKNIAYGLKkrKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 159 VGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-212 |
1.47e-38 |
|
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: 135.39 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAK-----SQKPTSGKISYNGTDINSND-NVLE 75
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDvDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 ---DFGiMI--EPVFYPeMSVIDNLKFYLKLHG---KKELYSNIERTLKLVELWE--SRNRKPKGFSFGMKQRTALAIAL 145
Cdd:cd03260 79 lrrRVG-MVfqKPNPFP-GSIYDNVAYGLRLHGiklKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 146 VAEPDFLILDEPFVGLDPVGVQK---LIDILKKwsserQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKieeLIAELKK-----EYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-210 |
2.74e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 136.04 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLS----KKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNV-LED 76
Cdd:TIGR04521 1 IKLKNVSyiyqPGTP-FEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKkLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGIMIEPVF-YPEM-----SVIDNLKFYLKLHG--KKELYSNIERTLKLVELWES-RNRKPKGFSFGMKQRTALAIALVA 147
Cdd:TIGR04521 80 LRKKVGLVFqFPEHqlfeeTVYKDIAFGPKNLGlsEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-197 |
3.94e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.54 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvLE----D 76
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----LPpekrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGImiepVF--Y---PEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEP 149
Cdd:COG3842 79 VGM----VFqdYalfPHLTVAENVAFGLRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937413360 150 DFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGelEAL 197
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE--EAL 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-211 |
4.99e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.00 E-value: 4.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvledfgim 80
Cdd:COG1137 3 TLEAENLVKSYGKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 iEPVF--------Y-P-------EMSVIDNLKFYLKLHGKkelySNIERTLKLVELWE----SRNRKPKGFSF--GMKQR 138
Cdd:COG1137 70 -LPMHkrarlgigYlPqeasifrKLTVEDNILAVLELRKL----SKKEREERLEELLEefgiTHLRKSKAYSLsgGERRR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 139 TALAIALVAEPDFLILDEPFVGLDPVGV---QKLIDILKkwssERQISMLISSHQLGELEALCNR-YIYIEGGKLAE 211
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVadiQKIIRHLK----ERGIGVLITDHNVRETLGICDRaYIISEGKVLAE 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-211 |
6.61e-38 |
|
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: 133.43 E-value: 6.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGN--------------------DFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIS 61
Cdd:cd03220 1 IELENVSKSYPTYkggssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 62 YNGTDINsndnvLEDFGIMIEpvfyPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRT 139
Cdd:cd03220 81 VRGRVSS-----LLGLGGGFN----PELTGRENIYLNGRLLGlsRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 140 ALAIALVAEPDFLILDEPF-VGlDPVGVQKLIDILKKWSSERQIsMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:cd03220 152 AFAIATALEPDILLIDEVLaVG-DAAFQEKCQRRLRELLKQGKT-VILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-209 |
2.14e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.87 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-----VLE 75
Cdd:COG3638 2 MLELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 DFGiMIEPVFY--PEMSVIDNLkfylkLHG---------------KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQR 138
Cdd:COG3638 81 RIG-MIFQQFNlvPRLSVLTNV-----LAGrlgrtstwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 139 TALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-212 |
1.43e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 132.48 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGND--FYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKP---TSGKISYNGTDINS-NDNVL 74
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 75 EDF---GI-MI--EPV--FYPEMSVIDNLKFYLKLHG---KKELYSNIERTLKLVEL--WESR-NRKPKGFSFGMKQRTA 140
Cdd:COG0444 81 RKIrgrEIqMIfqDPMtsLNPVMTVGDQIAEPLRIHGglsKAEARERAIELLERVGLpdPERRlDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 141 LAIALVAEPDFLILDEPFVGLDpVGVQKLI-DILKKWSSERQISMLISSHQLGELEALCNR----YiyieGGKLAES 212
Cdd:COG0444 161 IARALALEPKLLIADEPTTALD-VTIQAQIlNLLKDLQRELGLAILFITHDLGVVAEIADRvavmY----AGRIVEE 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-159 |
4.41e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 126.22 E-value: 4.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI-----EPVFYPEMSVID 93
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--RKSLRKEIgyvfqDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 94 NLKFYLKLHGKKELYSN--IERTLKLVELWESRNRK----PKGFSFGMKQRTALAIALVAEPDFLILDEPFV 159
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDarAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-209 |
5.70e-36 |
|
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: 128.14 E-value: 5.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPgnDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInsNDNVLEDFGIMI 81
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--TDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epVF-----YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:cd03301 77 --VFqnyalYPHMTVYDNIAFGLKLRKvpKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 155 DEPFVGLDP-VGVQKLIDiLKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03301 155 DEPLSNLDAkLRVQMRAE-LKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-211 |
7.66e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 7.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPgnDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLE---DFg 78
Cdd:COG1118 3 IEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRErrvGF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 imiepVF--Y---PEMSVIDNLKFYL--KLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:COG1118 80 -----VFqhYalfPHMTVAENIAFGLrvRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 152 LILDEPFVGLDpVGVQK-----LIDILKkwssERQISMLISSHQLGE-LEaLCNRYIYIEGGKLAE 211
Cdd:COG1118 155 LLLDEPFGALD-AKVRKelrrwLRRLHD----ELGGTTVFVTHDQEEaLE-LADRVVVMNQGRIEQ 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-212 |
7.93e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 130.97 E-value: 7.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFP--GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVLEDF 77
Cdd:COG1135 1 MIELENLSKTFPtkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 --GI-MIepvF-----YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVA 147
Cdd:COG1135 81 rrKIgMI---FqhfnlLSSRTVAENVALPLEIAGvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-218 |
8.44e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 127.94 E-value: 8.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDfySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvLEDF---- 77
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG----LPPHerar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 -GIMIEP----VFyPEMSVIDNLKFYLKLHGKKELYSNIERTLKLV-ELWESRNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:cd03224 75 aGIGYVPegrrIF-PELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLAESfiGKAQ 218
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLE--GTAA 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-212 |
1.43e-35 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 134.96 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN--SNDNVLEDFG- 78
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRRQIGv 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMIEPVFYpEMSVIDNLKFylklhGKKEL-YSNIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALV 146
Cdd:COG2274 554 VLQDVFLF-SGTIRENITL-----GDPDAtDEEIIEAARLAGLHDFIEALPMGYdtvvgeggsnlSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSseRQISMLISSHQLgELEALCNRYIYIEGGKLAES 212
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRL-STIRLADRIIVLDKGRIVED 690
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
8-210 |
1.80e-35 |
|
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: 126.64 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 8 SKKFPGndfYSLsDVSLEIEkGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVL----EDFGIMI-- 81
Cdd:cd03297 7 EKRLPD---FTL-KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppQQRKIGLvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -EPVFYPEMSVIDNLKFYLKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVG 160
Cdd:cd03297 82 qQYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 161 LDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-210 |
2.26e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 127.30 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVLEDFGIM 80
Cdd:cd03256 1 IEVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEPVF-----YPEMSVIDNLkfylkLHGK----------KELYSNIER-----TLKLVELWESRNRKPKGFSFGMKQRTA 140
Cdd:cd03256 80 IGMIFqqfnlIERLSVLENV-----LSGRlgrrstwrslFGLFPKEEKqralaALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 141 LAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-209 |
4.21e-35 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 127.37 E-value: 4.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-------------VLEDFGIMiepvfyP 87
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelrrkkismVFQSFALL------P 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 88 EMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVG 165
Cdd:cd03294 116 HRTVLENVAFGLEVQGvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937413360 166 VQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-211 |
4.67e-35 |
|
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: 126.65 E-value: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNV--LEDFGI 79
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIEPV-FYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVEL--WESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:cd03295 80 VIQQIgLFPHMTVEENIALVPKLLKwpKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 155 DEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-209 |
9.18e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 124.95 E-value: 9.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI 81
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVF-----YPEMSVIDNLKFYL-KLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLI 153
Cdd:cd03262 79 GMVFqqfnlFPHLTVLENITLAPiKVKGmsKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 154 LDEPFVGLDPVGVQKLIDILKKWSSErQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-209 |
9.74e-35 |
|
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: 124.68 E-value: 9.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFPGNDFySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMIEP 83
Cdd:cd03226 2 IENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 84 --VFYPEmSVIDNLKFYLKLHGKKelYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGL 161
Cdd:cd03226 81 dyQLFTD-SVREELLLGLKELDAG--NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937413360 162 DPVGVQKLIDILKKWSSERQISMLIsSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVI-THDYEFLAKVCDRVLLLANGAI 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-201 |
1.14e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNdfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVL-EDFGI 79
Cdd:COG1129 4 LLEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 -MI--EPVFYPEMSVIDNLKF--YLKLHG---KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:COG1129 82 aIIhqELNLVPNLSVAENIFLgrEPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRY 201
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRV 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-162 |
1.94e-34 |
|
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: 124.66 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGImi 81
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNT-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epVF-----YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:cd03300 77 --VFqnyalFPHLTVFENIAFGLRLKKlpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
....*...
gi 1937413360 155 DEPFVGLD 162
Cdd:cd03300 155 DEPLGALD 162
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-209 |
2.50e-34 |
|
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: 123.67 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 5 ENLSKKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN------------SNDN 72
Cdd:cd03292 4 INVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgraipylrrKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 VLEDFGIMiepvfyPEMSVIDNLKFYLKL--HGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPD 150
Cdd:cd03292 83 VFQDFRLL------PDRNVYENVAFALEVtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 151 FLILDEPFVGLDPVGVQKLIDILKKwSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-212 |
2.69e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 127.22 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFP--GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVLEDF 77
Cdd:PRK11153 1 MIELKNISKVFPqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 --GI-MIEPVFYPEMS--VIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPD 150
Cdd:PRK11153 81 rrQIgMIFQHFNLLSSrtVFDNVALPLELAGtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 151 FLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-286 |
2.97e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 126.36 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF------PG-----NDFYS--------LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIS 61
Cdd:COG4586 1 IIEVENLSKTYrvyekePGlkgalKGLFRreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 62 YNGTDI--NSNDNvLEDFGImiepVF------YPEMSVIDNLKFYLKLHG--KKELYSNIER---TLKLVELWESRNRKp 128
Cdd:COG4586 81 VLGYVPfkRRKEF-ARRIGV----VFgqrsqlWWDLPAIDSFRLLKAIYRipDAEYKKRLDElveLLDLGELLDTPVRQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 129 kgFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:COG4586 155 --LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 209 LA-----ESFIGKAQPS--LVVHLNSKYHMCNLKDHISqgITLRDGlLDIPISVD-KEALNDIFGVLASESLIESIEVKE 280
Cdd:COG4586 233 IIydgslEELKERFGPYktIVLELAEPVPPLELPRGGE--VIEREG-NRVRLEVDpRESLAEVLARLLARYPVRDLTIEE 309
|
....*.
gi 1937413360 281 NHLKEV 286
Cdd:COG4586 310 PPIEEV 315
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-208 |
4.50e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 121.72 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD--LESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -----EPVFYpEMSVIDNLkfylklhgkkelysniertlklvelwesrnrkpkgFSFGMKQRTALAIALVAEPDFLILDE 156
Cdd:cd03228 79 ayvpqDPFLF-SGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 157 PFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLGELEaLCNRYIYIEGGK 208
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
7.90e-34 |
|
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: 121.00 E-value: 7.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNdnvledfgimi 81
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epvfypemSVIDNLKfylklHGkkelysnIERTLKLvelwesrnrkpkgfSFGMKQRTALAIALVAEPDFLILDEPFVGL 161
Cdd:cd03216 68 --------SPRDARR-----AG-------IAMVYQL--------------SVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937413360 162 DPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:cd03216 114 TPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-209 |
1.35e-33 |
|
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: 122.44 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN-DNVLEDFGIMI---EPVFYpEMSVIDN 94
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRrKKFLRRIGVVFgqkTQLWW-DLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 95 LKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDI 172
Cdd:cd03267 116 FYLLAAIYDlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937413360 173 LKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03267 196 LKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-209 |
4.32e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 119.46 E-value: 4.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 3 KIENLSKKFPGNDfySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvledfgimie 82
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 pvfypeMSvidnlkfylklhgKKELYSNI---ERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFV 159
Cdd:cd03214 66 ------LS-------------PKELARKIayvPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 160 GLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-162 |
4.69e-33 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 121.29 E-value: 4.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPgnDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI 81
Cdd:cd03296 3 IEVRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epVF-----YPEMSVIDNLKFYLKLHGKKELYS------NIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPD 150
Cdd:cd03296 79 --VFqhyalFRHMTVFDNVAFGLRVKPRSERPPeaeiraKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170
....*....|..
gi 1937413360 151 FLILDEPFVGLD 162
Cdd:cd03296 157 VLLLDEPFGALD 168
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-210 |
9.50e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.24 E-value: 9.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFyslsDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS----------- 69
Cdd:COG3840 1 MLRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlppaerpvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 70 -NDNVLedfgimiepvfYPEMSVIDNLkfYLKLHGKKELYSN----IERTLKLVELWESRNRKPKGFSFGMKQRTALAIA 144
Cdd:COG3840 77 fQENNL-----------FPHLTVAQNI--GLGLRPGLKLTAEqraqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 145 LVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-210 |
1.83e-32 |
|
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: 120.15 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-------- 72
Cdd:COG1120 1 MLEAENLSVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelarria 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 VLEDFGIMIEPvfypeMSVIDNLKF----YLKLHGK--KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:COG1120 79 YVPQEPPAPFG-----LTVRELVALgrypHLGLFGRpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-259 |
2.34e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 122.64 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNdfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIM 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEP-VFYPEMSVIDNLKFYLKLH--GKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:PRK11607 97 FQSyALFPHMTVEQNIAFGLKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 158 FVGLDpvgvQKL--------IDILKKWSserqISMLISSHQLGELEALCNRYIYIEGGKLAEsfIGKAQpSLVVHLNSKY 229
Cdd:PRK11607 177 MGALD----KKLrdrmqlevVDILERVG----VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ--IGEPE-EIYEHPTTRY 245
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1937413360 230 HM----------CNLKDHISQGITLRDGLLDIPISVDKEA 259
Cdd:PRK11607 246 SAefigsvnvfeGVLKERQEDGLVIDSPGLVHPLKVDADA 285
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-209 |
7.80e-32 |
|
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: 117.31 E-value: 7.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 5 ENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND--NVLEDFGIMIE 82
Cdd:cd03245 6 RNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDpaDLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 PVFYPEMSVIDNLKFYLKLHGKKElysnIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAEPDF 151
Cdd:cd03245 86 DVTLFYGTLRDNITLGAPLADDER----ILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLGELEaLCNRYIYIEGGKL 209
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-212 |
1.34e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.40 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVL----ED 76
Cdd:COG1126 1 MIEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGImiepVF-----YPEMSVIDNLKFYL-KLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:COG1126 79 VGM----VFqqfnlFPHLTVLENVTLAPiKVKKmsKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 149 PDFLILDEPFVGLDPVGVQKLIDILKKWSSERqISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEE 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-212 |
1.82e-31 |
|
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: 122.57 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN--SNDNVLEDFGI 79
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIE--PVFYpeMSVIDNLKFylklhGKKELySN--IERTLKLVELWESRNRKPKG-----------FSFGMKQRTALAIA 144
Cdd:COG4987 414 VPQrpHLFD--TTLRENLRL-----ARPDA-TDeeLWAALERVGLGDWLAALPDGldtwlgeggrrLSGGERRRLALARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 145 LVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLGELEAlCNRYIYIEGGKLAES 212
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQ 550
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-218 |
3.25e-31 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 116.63 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDI-NSNDNVLEDFGI 79
Cdd:TIGR02315 1 MLEVENLSKVYPNGK-QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItKLRGKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIEPVF-----YPEMSVIDNLkfylkLHG-------------------KKELYSNIERtlklVELWESRNRKPKGFSFGM 135
Cdd:TIGR02315 80 RIGMIFqhynlIERLTVLENV-----LHGrlgykptwrsllgrfseedKERALSALER----VGLADKAYQRADQLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 136 KQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAesFIG 215
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV--FDG 228
|
...
gi 1937413360 216 KAQ 218
Cdd:TIGR02315 229 APS 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-210 |
5.42e-30 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 112.59 E-value: 5.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI-EPVFYPEMSVIDNLKFYL 99
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFqENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 100 --KLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWS 177
Cdd:cd03298 96 spGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|...
gi 1937413360 178 SERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-209 |
7.53e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.86 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGtdinsndnvledfGIMI-- 81
Cdd:COG0488 1 LENLSKSFGGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-------------GLRIgy 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 ---EPVFYPEMSVID----------------------------NLKFYLKLHGKKE------LYSNIERTLKLVELWES- 123
Cdd:COG0488 66 lpqEPPLDDDLTVLDtvldgdaelraleaeleeleaklaepdeDLERLAELQEEFEalggweAEARAEEILSGLGFPEEd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 124 RNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSerqiSMLISSHQLGELEALCNRYIY 203
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHDRYFLDRVATRILE 221
|
....*.
gi 1937413360 204 IEGGKL 209
Cdd:COG0488 222 LDRGKL 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-218 |
1.19e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 112.00 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLskkfpgNDFYS----LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN---SNDNV 73
Cdd:COG0410 3 MLEVENL------HAGYGgihvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglpPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 LEdfGIMIEP----VFyPEMSVIDNLK--FYLkLHGKKELYSNIERTLKLV-ELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:COG0410 77 RL--GIGYVPegrrIF-PSLTVEENLLlgAYA-RRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLAESfiGKAQ 218
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLE--GTAA 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-200 |
1.66e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 116.66 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPG---NDfyslsDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNG--TDINS-NDNVl 74
Cdd:COG3845 5 ALELRGITKRFGGvvaND-----DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSpRDAI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 75 eDFGI-MI--EPVFYPEMSVIDNLkfYLKLHGKKELYSNIERTLKLV-ELweSR--------NRKPKGFSFGMKQRTALA 142
Cdd:COG3845 79 -ALGIgMVhqHFMLVPNLTVAENI--VLGLEPTKGGRLDRKAARARIrEL--SErygldvdpDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 143 IALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSErQISMLISSHQLGELEALCNR 200
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADR 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
1.92e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInSNDNVLeDFGIMI 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVW-DVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVFY-PE-----MSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLI 153
Cdd:PRK13635 84 GMVFQnPDnqfvgATVQDDVAFGLENIGvpREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 154 LDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELeALCNRYIYIEGGKLAE 211
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILE 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-212 |
3.25e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 116.40 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI 81
Cdd:COG4988 337 IELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD--PASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -----EPVFYPeMSVIDNLKFYLKLHGKKELysniERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIAL 145
Cdd:COG4988 414 awvpqNPYLFA-GTIRENLRLGRPDASDEEL----EAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARAL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 146 VAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLgELEALCNRYIYIEGGKLAES 212
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRL-ALLAQADRILVLDDGRIVEQ 552
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-210 |
6.94e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 6.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKF-PGNDFYS--LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFG 78
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMIEPVF-YPEM-----SVIDNLKFYLKLHG--KKELYSNIERTLKLVEL--WESRNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:PRK13637 83 KKVGLVFqYPEYqlfeeTIEKDIAFGPINLGlsEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 149 PDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-189 |
1.97e-28 |
|
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: 107.89 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLED-----FGIMIEP---VFYPemS 90
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLErrqrvGLVFQDPddqLFAA--D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 91 VIDNLKFYLKLHGKK--ELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQK 168
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSeaEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQ 165
|
170 180
....*....|....*....|.
gi 1937413360 169 LIDILKKWSSErQISMLISSH 189
Cdd:TIGR01166 166 MLAILRRLRAE-GMTVVISTH 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-208 |
1.09e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.40 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIM 80
Cdd:PRK13636 5 ILKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEPVFY-PE-----MSVIDNLKF---YLKLhGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:PRK13636 84 VGMVFQdPDnqlfsASVYQDVSFgavNLKL-PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-212 |
2.62e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 110.54 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPG---------NDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQkPTSGKISYNGTDINS-ND 71
Cdd:COG4172 276 LEARDLKVWFPIkrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGlSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 72 NVLEDFGIMIEPVF---Y----PEMSVIDNLKFYLKLHG----KKELYSNIERTLKLVEL-WESRNRKPKGFSFGMKQRT 139
Cdd:COG4172 355 RALRPLRRRMQVVFqdpFgslsPRMTVGQIIAEGLRVHGpglsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRI 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 140 ALAIALVAEPDFLILDEPFVGLDpVGVQK-LIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALD-VSVQAqILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQ 507
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-216 |
3.00e-27 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 105.63 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN----VLEDFGIMiepvfyPEMSVIDN 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPdrmvVFQNYSLL------PWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 95 LKFYLK--LH--GKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLI 170
Cdd:TIGR01184 75 IALAVDrvLPdlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937413360 171 DILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGklAESFIGK 216
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG--PAANIGQ 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-162 |
5.96e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.48 E-value: 5.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpGNDfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDI---NSNDN----VL 74
Cdd:PRK10851 3 IEIANIKKSF-GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlHARDRkvgfVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 75 EDFGImiepvfYPEMSVIDNLKFYLKLHGKKE------LYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:PRK10851 81 QHYAL------FRHMTVFDNIAFGLTVLPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170
....*....|....
gi 1937413360 149 PDFLILDEPFVGLD 162
Cdd:PRK10851 155 PQILLLDEPFGALD 168
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-208 |
6.11e-27 |
|
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: 102.14 E-value: 6.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTdinsndnvledfgimI 81
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVFYPEMSvidnlkfylklhGkkelysniertlklvelwesrnrkpkgfsfGMKQRTALAIALVAEPDFLILDEPFVGL 161
Cdd:cd03221 64 KIGYFEQLS------------G------------------------------GEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937413360 162 DPVGVQKLIDILKKWsserQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:cd03221 102 DLESIEALEEALKEY----PGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-216 |
7.31e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.81 E-value: 7.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIsYNGtDINSNDNVLEDFGI-MiepVF-----YPEMSVIDN 94
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIG-EKRMNDVPPAERGVgM---VFqsyalYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 95 LKFYLKLHG--KKELYSNIE---RTLKLVELWEsrnRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDP-VGVQK 168
Cdd:PRK11000 96 MSFGLKLAGakKEEINQRVNqvaEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAaLRVQM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937413360 169 LIDIlKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAEsfIGK 216
Cdd:PRK11000 173 RIEI-SRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ--VGK 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-211 |
9.74e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.79 E-value: 9.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInsNDNVLEDFGIM 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEP--VF-----YPEMSVIDNLKF---YLKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPD 150
Cdd:PRK09493 77 QEAgmVFqqfylFPHLTALENVMFgplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 151 FLILDEPFVGLDPVGVQKLIDILKKWSSErQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-212 |
2.80e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.95 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIeNLSKKFPgnDFySLsDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTdinsndnVLED--FG 78
Cdd:COG4148 2 MLEV-DFRLRRG--GF-TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-------VLQDsaRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMIEP-------VF-----YPEMSVIDNLKFYLKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:COG4148 70 IFLPPhrrrigyVFqearlFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:COG4148 150 SSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-193 |
4.33e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND--NVLEDFG 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfeKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMIEPvfyPE-----MSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:PRK13648 87 IVFQN---PDnqfvgSIVKYDVAFGLENHAvpYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGE 193
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-209 |
4.63e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.05 E-value: 4.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS---NDNVLEDFG 78
Cdd:PRK10895 4 LTAKNLAKAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMI-EPVFYPEMSVIDNLKFYLKLhgKKELYSNiERTLKLVELWES------RNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:PRK10895 82 YLPqEASIFRRLSVYDNLMAVLQI--RDDLSAE-QREDRANELMEEfhiehlRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 152 LILDEPFVGLDPVGV---QKLIDILKkwssERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:PRK10895 159 ILLDEPFAGVDPISVidiKRIIEHLR----DSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-210 |
8.93e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 104.42 E-value: 8.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNvledfGIMIEP-------VF-----YPE 88
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRK-----GIFLPPekrrigyVFqearlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 89 MSVIDNLKFYLKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQK 168
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937413360 169 LIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-209 |
1.42e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.06 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINsndNVLEDFGIMI 81
Cdd:PRK11247 13 LLLNAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA---EAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -EPVFYPEMSVIDNLKFYLKLHGKKElysnIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVG 160
Cdd:PRK11247 88 qDARLLPWKKVIDNVGLGLKGQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 161 LDP---VGVQKLIDILkkWsSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:PRK11247 164 LDAltrIEMQDLIESL--W-QQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-209 |
1.57e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.47 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF----PGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLE- 75
Cdd:PRK13633 4 MIKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 -----------DFGIMIEPV-----FYPEMSVIDnlkfylklhgKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRT 139
Cdd:PRK13633 84 rnkagmvfqnpDNQIVATIVeedvaFGPENLGIP----------PEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 140 ALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELeALCNRYIYIEGGKL 209
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-209 |
3.92e-25 |
|
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: 105.10 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN-DNVLEDFGIMIE 82
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNlDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 -PVFYPEMSVIDNLKFYLKLHGK--KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFV 159
Cdd:TIGR01257 1011 hNILFHHLTVAEHILFYAQLKGRswEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 160 GLDPVGVQKLIDILKKWSSERQISMliSSHQLGELEALCNRYIYIEGGKL 209
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIM--STHHMDEADLLGDRIAIISQGRL 1138
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-215 |
3.98e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIsyngtdinsndnvleDFGIM 80
Cdd:COG0488 315 VLELEGLSKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---------------KLGET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEPVFY--------PEMSVIDNLKFYLKLHGKKELYSNIERTLklveLWESRNRKP-KGFSFGMKQRTALAIALVAEPDF 151
Cdd:COG0488 378 VKIGYFdqhqeeldPDKTVLDELRDGAPGGTEQEVRGYLGRFL----FSGDDAFKPvGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWSSerqiSMLISSH--QLgeLEALCNRYIYIEGGKLAEsFIG 215
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDFPG----TVLLVSHdrYF--LDRVATRILEFEDGGVRE-YPG 512
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-207 |
4.22e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.10 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLE-DFGI 79
Cdd:PRK09700 5 YISMAGIGKSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIepvFYPEMSVIDNLK-----FYLKLHGKK----------ELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIA 144
Cdd:PRK09700 83 GI---IYQELSVIDELTvlenlYIGRHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 145 LVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLIsSHQLGELEALCNRYIYIEGG 207
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYI-SHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-276 |
4.45e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.84 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSnDNVLE---DF 77
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEirkKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIEPvfyPE-----MSVIDNLKFYL--KLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPD 150
Cdd:PRK13632 86 GIIFQN---PDnqfigATVEDDIAFGLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 151 FLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELeALCNRYIYIEGGKLaesfIGKAQPSLVvhLNSKYh 230
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKL----IAQGKPKEI--LNNKE- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1937413360 231 mcnlkdhisqgiTLRDGLLDIPISVD-KEALNDIFGVLASESLIESI 276
Cdd:PRK13632 235 ------------ILEKAKIDSPFIYKlSKKLKGIDPTYNEEELIEQI 269
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-211 |
4.59e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 14 NDFYS----LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMIEP----VF 85
Cdd:COG4161 9 NCFYGshqaLFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLLRQkvgmVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 86 -----YPEMSVIDNL-KFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:COG4161 89 qqynlWPHLTVMENLiEAPCKVLGlsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 158 FVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:COG4161 169 TAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-162 |
5.36e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.72 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDfgimI 81
Cdd:PRK09452 15 VELRGISKSFDGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH----V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVF-----YPEMSVIDNLKFYLKLH--GKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK09452 89 NTVFqsyalFPHMTVFENVAFGLRMQktPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
....*...
gi 1937413360 155 DEPFVGLD 162
Cdd:PRK09452 169 DESLSALD 176
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-211 |
5.78e-25 |
|
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: 104.11 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMM--AKSQKPTSGKISYN---------------- 63
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 64 GTDINSNDNVLE----DF---------------GIMIEPVF--YPEMSVIDNLKFYLKLHGKKELYSnIERTLKLVELWE 122
Cdd:TIGR03269 79 GEPCPVCGGTLEpeevDFwnlsdklrrrirkriAIMLQRTFalYGDDTVLDNVLEALEEIGYEGKEA-VGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 123 SRNRK---PKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCN 199
Cdd:TIGR03269 158 LSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|..
gi 1937413360 200 RYIYIEGGKLAE 211
Cdd:TIGR03269 238 KAIWLENGEIKE 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-211 |
7.00e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.15 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYS-------LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDN 72
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 VLEDFGIMIEPVFYPEMSVIDN-----------LKFYLKLHgKKELYSNIERTLKLVELWES-RNRKPKGFSFGMKQRTA 140
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSISAVNPrktvreiirepLRHLLSLD-KAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 141 LAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-212 |
7.04e-25 |
|
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: 98.15 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFgimi 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epvfypeMSVIdNLKFYLKlhgKKELYSNIERTlklvelwesrnrkpkgFSFGMKQRTALAIALVAEPDFLILDEPFVGL 161
Cdd:cd03247 77 -------ISVL-NQRPYLF---DTTLRNNLGRR----------------FSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 162 DPVGVQKLIDILKKWSSERQISMLisSHQLGELEALcNRYIYIEGGKLAES 212
Cdd:cd03247 130 DPITERQLLSLIFEVLKDKTLIWI--THHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-217 |
7.24e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.57 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN---SNDNVLEDF 77
Cdd:PRK11614 5 MLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIE--PVFyPEMSVIDNLKFYLKLHGKKELYSNIERTLKLV-ELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK11614 83 AIVPEgrRVF-SRMTVEENLAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 155 DEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEaLCNRYIYIEGGKLAESFIGKA 217
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALK-LADRGYVLENGHVVLEDTGDA 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
7.45e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.82 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIM 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 ------IEPVF-----YPEMSVIDNL---KFYLKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:PRK11264 81 rqlrqhVGFVFqnfnlFPHRTVLENIiegPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQiSMLISSHQLGELEALCNRYIYIEGGKLAESFIGKA 217
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-206 |
7.99e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.79 E-value: 7.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInsndnvleDFGIMIEPVFY--------PEMS 90
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--------DDPDVAEACHYlghrnamkPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 91 VIDNLKFYLKLHGKKELysNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLI 170
Cdd:PRK13539 90 VAENLEFWAAFLGGEEL--DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937413360 171 DILKKwSSERQISMLISSHQlgELEALCNRYIYIEG 206
Cdd:PRK13539 168 ELIRA-HLAQGGIVIAATHI--PLGLPGARELDLGP 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-209 |
1.45e-24 |
|
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: 96.90 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD--PNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPV------FypEMSVIDNLkfylklhgkkelysniertlklvelwesrnrkpkgFSFGMKQRTALAIALVAEPDFLILD 155
Cdd:cd03246 79 GYLpqddelF--SGSIAENI-----------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 156 EPFVGLDPVGVQKLIDILKKWSSERQISMLIsSHQLgELEALCNRYIYIEGGKL 209
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVI-AHRP-ETLASADRILVLEDGRV 173
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-200 |
1.66e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 103.28 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 5 ENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND-----NVledfGI 79
Cdd:NF033858 270 RGLTMRF--GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDiatrrRV----GY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIEpVF--YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILD 155
Cdd:NF033858 344 MSQ-AFslYGELTVRQNLELHARLFHlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937413360 156 EPFVGLDPVGV----QKLIDIlkkwSSERQISMLISSHQLGELEaLCNR 200
Cdd:NF033858 423 EPTSGVDPVARdmfwRLLIEL----SREDGVTIFISTHFMNEAE-RCDR 466
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-211 |
1.89e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.68 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNvLEDFGIMIEPVF---YPEMSVIDNL 95
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-LARARIGVVPQFdnlDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 96 KFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPvGVQKLIdil 173
Cdd:PRK13536 136 LVFGRYFGmsTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP-HARHLI--- 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937413360 174 kkWSSERQI-----SMLISSHQLGELEALCNRYIYIEGG-KLAE 211
Cdd:PRK13536 212 --WERLRSLlargkTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-175 |
4.63e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.80 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMK----M--MAKSQKpTSGKISYNGTDINSND-NVL 74
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrMndLIPGAR-VEGEILLDGEDIYDPDvDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 75 E---DFGiMiepVF-----YPeMSVIDNLKFYLKLHG---KKELYSNIERTLKLVELWE---SRNRKP-KGFSFGMKQRT 139
Cdd:COG1117 89 ElrrRVG-M---VFqkpnpFP-KSIYDNVAYGLRLHGiksKSELDEIVEESLRKAALWDevkDRLKKSaLGLSGGQQQRL 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937413360 140 ALAIALVAEPDFLILDEPFVGLDPVGVQK---LIDILKK 175
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKieeLILELKK 202
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
13-211 |
5.20e-24 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 97.96 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 13 GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGtDINSndnvledfgIMIEPVFYPEMSVI 92
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSV---------IAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 93 DNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLI 170
Cdd:PRK13546 104 ENIEFKMLCMGfkRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937413360 171 DILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK13546 184 DKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-211 |
6.62e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 6.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEdFGIMI 81
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVFY---PEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDE 156
Cdd:PRK13537 85 VPQFDnldPDFTVRENLLVFGRYFGlsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 157 PFVGLDPVGVQKLIDILKKWSSeRQISMLISSHQLGELEALCNRYIYIEGG-KLAE 211
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGrKIAE 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
7.58e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAK-----SQKPTSGKISYNGTDI---NSNDNV 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRmneleSEVRVEGRVEFFNQNIyerRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 LEDFGIMI--EPVFYPeMSVIDNLKFYLKL---HGKKELYSNIERTLKLVELW-ESRNRKPKG---FSFGMKQRTALAIA 144
Cdd:PRK14258 86 LRRQVSMVhpKPNLFP-MSVYDNVAYGVKIvgwRPKLEIDDIVESALKDADLWdEIKHKIHKSaldLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 145 LVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGklaESFIGK 216
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGN---ENRIGQ 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-193 |
8.35e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 8.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDfySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN----SNDNVLED 76
Cdd:PRK11248 1 MLQISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGIMiepvfyPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK11248 79 EGLL------PWRNVQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937413360 155 DEPFVGLDPVG---VQKLidILKKWSSERQISMLIsSHQLGE 193
Cdd:PRK11248 153 DEPFGALDAFTreqMQTL--LLKLWQETGKQVLLI-THDIEE 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-212 |
8.79e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 100.62 E-value: 8.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN--SNDNVLEDFGiMI--EPVFYpEMSVIDN 94
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdlTLESLRRQIG-VVpqDTFLF-SGTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 95 LKFylklhGKKElYSN--IERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAEPDFLILDEPFVGL 161
Cdd:COG1132 434 IRY-----GRPD-ATDeeVEEAAKAAQAHEFIEALPDGYdtvvgergvnlSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 162 DPVGVQKLIDILKKWSSERqiSMLISSHQLGELEAlCNRYIYIEGGKLAES 212
Cdd:COG1132 508 DTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-162 |
1.75e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 97.99 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNdFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvLE--DFG 78
Cdd:PRK11650 3 GLKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE----LEpaDRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 I-MiepVF-----YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPD 150
Cdd:PRK11650 78 IaM---VFqnyalYPHMSVRENMAYGLKIRGmpKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170
....*....|..
gi 1937413360 151 FLILDEPFVGLD 162
Cdd:PRK11650 155 VFLFDEPLSNLD 166
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-162 |
1.79e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInsNDNVLEDFGIMI 81
Cdd:PRK11432 7 VVLKNITKRFGSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV--THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epVF-----YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK11432 83 --VFqsyalFPHMSLGENVGYGLKMLGvpKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
....*...
gi 1937413360 155 DEPFVGLD 162
Cdd:PRK11432 161 DEPLSNLD 168
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-196 |
2.19e-23 |
|
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: 94.73 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINsndnvlEDFGIMIEPVFY--------PEMS 90
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA------EQRDEPHENILYlghlpglkPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 91 VIDNLKFYLKLHGKKELysNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLI 170
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQR--TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
170 180
....*....|....*....|....*..
gi 1937413360 171 DILKKwSSERQISMLISSHQ-LGELEA 196
Cdd:TIGR01189 168 GLLRA-HLARGGIVLLTTHQdLGLVEA 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-212 |
5.35e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGN-DFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGtDINSNDNVLeDFGI 79
Cdd:PRK13650 4 IIEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVW-DIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIEPVF------YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:PRK13650 82 KIGMVFqnpdnqFVGATVEDDVAFGLENKGipHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELeALCNRYIYIEGGKLAES 212
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVEST 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-209 |
6.29e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.14 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND----NVLED 76
Cdd:PRK13639 1 ILETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksllEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGIMIE----PVFYPemSVIDNLKF---YLKLhGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEP 149
Cdd:PRK13639 80 VGIVFQnpddQLFAP--TVEEDVAFgplNLGL-SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 150 DFLILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-211 |
6.88e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 14 NDFY----SLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGK--ISYNGTDINSNDNVLE------DFGImi 81
Cdd:PRK11124 9 NCFYgahqALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlnIAGNHFDFSKTPSDKAirelrrNVGM-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epVF-----YPEMSVIDNL-KFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLI 153
Cdd:PRK11124 87 --VFqqynlWPHLTVQQNLiEAPCRVLGlsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 154 LDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-209 |
7.04e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 7.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGN---DFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFG 78
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMIEPVFY-PEMSVIDNLKFYLKLHG-----------------------------KKELYSNIERTLKLVELWESR-NRK 127
Cdd:PRK13651 83 VLEKLVIQkTRFKKIKKIKEIRRRVGvvfqfaeyqlfeqtiekdiifgpvsmgvsKEEAKKRAAKYIELVGLDESYlQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 128 PKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQiSMLISSHQLGELEALCNRYIYIEGG 207
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 1937413360 208 KL 209
Cdd:PRK13651 242 KI 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-194 |
7.14e-23 |
|
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: 94.38 E-value: 7.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGK------ISYNGTDIN---------SNDnvLEDFgimiep 83
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVWelrkriglvSPA--LQLR------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 84 vFYPEMSVIDNLkfylkLHGkkeLYSNI--------------ERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEP 149
Cdd:COG1119 91 -FPRDETVLDVV-----LSG---FFDSIglyreptdeqreraRELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937413360 150 DFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGEL 194
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEI 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-163 |
1.02e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.93 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKP---TSGKISYNGTDINSNDNVLEDF 77
Cdd:COG4136 1 MLSLENLTITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMI-EPVFYPEMSVIDNLKFYL-KLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILD 155
Cdd:COG4136 79 GILFqDDLLFPHLSVGENLAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
....*...
gi 1937413360 156 EPFVGLDP 163
Cdd:COG4136 159 EPFSKLDA 166
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-210 |
1.02e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.49 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 23 SLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI-EPVFYPEMSVIDN----LKF 97
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFqENNLFSHLTVAQNiglgLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 98 YLKL-HGKKELYSNIERTLKLVELWEsrnRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKW 176
Cdd:PRK10771 99 GLKLnAAQREKLHAIARQMGIEDLLA---RLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190
....*....|....*....|....*....|....
gi 1937413360 177 SSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:PRK10771 176 CQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-211 |
1.53e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.03 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN--VLEDFGI 79
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIE----PVFypEMSVIDNLKF---YLKLhGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFL 152
Cdd:PRK13647 84 VFQdpddQVF--SSTVWDDVAFgpvNMGL-DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 153 ILDEPFVGLDPVGVQKLIDILKKWSSERQiSMLISSHQLgELEALCNRYIYI--EGGKLAE 211
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDV-DLAAEWADQVIVlkEGRVLAE 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-211 |
3.76e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.10 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-------------VLEDFGIMiepvf 85
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevrrkkiamVFQSFALM----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 86 yPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDP 163
Cdd:PRK10070 119 -PHMTVLDNTAFGMELAGinAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937413360 164 VGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-211 |
3.94e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.02 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF--PGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKS----TLMKMMAKSQKpTSGKISYNGTDI-NSNDNV 73
Cdd:PRK09473 12 LLDVKDLRVTFstPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREIlNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 L-----EDFGiMI--EPV--FYPEMSVIDNLKFYLKLH---GKKELYSNIERTLKLVELWESRNRK---PKGFSFGMKQR 138
Cdd:PRK09473 91 LnklraEQIS-MIfqDPMtsLNPYMRVGEQLMEVLMLHkgmSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 139 TALAIALVAEPDFLILDEPFVGLDpVGVQKLI-DILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALD-VTVQAQImTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-208 |
4.02e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.91 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 20 SDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND-----NVLEDFGIMIEP-VFYPEMSVID 93
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlyTVRKRMSMLFQSgALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 94 NLKFYLKLHGK---KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLI 170
Cdd:PRK11831 104 NVAYPLREHTQlpaPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1937413360 171 DILKKWSSERQISMLISSHQLGELEALCNrYIYIEGGK 208
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIAD-HAYIVADK 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-212 |
4.45e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.68 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGtdinsNDNVLEDFGIM 80
Cdd:PRK11701 6 LLSVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM-----RDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEPV-------------------FYPEMSVIDNLKFYLKLHGKKElYSNIERT----LKLVELWESR-NRKPKGFSFGMK 136
Cdd:PRK11701 79 SEAErrrllrtewgfvhqhprdgLRMQVSAGGNIGERLMAVGARH-YGDIRATagdwLERVEIDAARiDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 137 QRTALAIALVAEPDFLILDEPFVGLDpVGVQ-KLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLD-VSVQaRLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-163 |
5.56e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.58 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS---NDNVLEDFGIMiePV-----FYPEMS 90
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADarhRRAVCPRIAYM--PQglgknLYPTLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 91 VIDNLKFYLKL--HGKKELYSNIERTLKLVELWESRNRkPKG-FSFGMKQRTALAIALVAEPDFLILDEPFVGLDP 163
Cdd:NF033858 95 VFENLDFFGRLfgQDAAERRRRIDELLRATGLAPFADR-PAGkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-191 |
8.72e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 8.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF-PG--NDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvLEDF 77
Cdd:COG1101 1 MLELKNLSKTFnPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK----LPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GI--MIEPVFY-------PEMSVIDNL--------KFYLKLHGKKELYSNIERTLKLVEL-WESRNRKPKGF-SFGmkQR 138
Cdd:COG1101 77 KRakYIGRVFQdpmmgtaPSMTIEENLalayrrgkRRGLRRGLTKKRRELFRELLATLGLgLENRLDTKVGLlSGG--QR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 139 TALA--IALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQL 191
Cdd:COG1101 155 QALSllMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-211 |
1.27e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.99 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAK-----SQKPTSGKISYNGTDINS--NDNV 73
Cdd:PRK14239 5 ILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlnPEVTITGSIVYNGHNIYSprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 --LEDFGIMIE-PVFYPeMSVIDNLKFYLKLHGKKE---LYSNIERTLKLVELW-ESRNR---KPKGFSFGMKQRTALAI 143
Cdd:PRK14239 83 dlRKEIGMVFQqPNPFP-MSIYENVVYGLRLKGIKDkqvLDEAVEKSLKGASIWdEVKDRlhdSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 144 ALVAEPDFLILDEPFVGLDPVGVQKLIDILkkWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-211 |
1.35e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPG---------NDFYSLSDVSLEIEKGEIVGLIGKNGAGKST----LMKMMAkSQkptsGKISYNGTDI 67
Cdd:PRK15134 275 LLDVEQLQVAFPIrkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-SQ----GEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 68 -NSNDNVLEDFGIMIEPVFY-------PEMSVIDNLKFYLKLHgKKELySNIERTLKLVELW-------ESRNRKPKGFS 132
Cdd:PRK15134 350 hNLNRRQLLPVRHRIQVVFQdpnsslnPRLNVLQIIEEGLRVH-QPTL-SAAQREQQVIAVMeevgldpETRHRYPAEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 133 FGMKQRTALAIALVAEPDFLILDEPFVGLDPVgVQKLI-DILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKT-VQAQIlALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-192 |
1.37e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 93.98 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYS--LSDVSLEIEKGEIVGLIGKNGAGKS----TLMKMMAKSQKPTSGKISYNGTDINS-NDNV 73
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVeaVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 LEdfGI------MI--EPV--FYPEMSVIDNLKFYLKLH---GKKELYSNIERTLKLVELWESRNR---KPKGFSFGMKQ 137
Cdd:COG4172 86 LR--RIrgnriaMIfqEPMtsLNPLHTIGKQIAEVLRLHrglSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 138 RTALAIALVAEPDFLILDEPFVGLDpVGVQKLI-DILKKWSSERQISMLISSHQLG 192
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALD-VTVQAQIlDLLKDLQRELGMALLLITHDLG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-209 |
1.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.59 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDiNSNDNVLEDFGIM 80
Cdd:PRK13644 1 MIRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEPVFY-PEM-----SVIDNLKFylklhGKK-------ELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVA 147
Cdd:PRK13644 79 VGIVFQnPETqfvgrTVEEDLAF-----GPEnlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEAlCNRYIYIEGGKL 209
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHD-ADRIIVMDRGKI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-288 |
1.54e-21 |
|
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: 94.70 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN-DNVLEDFGi 79
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNiSDVHQNMG- 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 miepvFYPEMSVIDNLkfylkLHGKKELY----------SNIER----TLKLVELWESRNRKPKGFSFGMKQRTALAIAL 145
Cdd:TIGR01257 2016 -----YCPQFDAIDDL-----LTGREHLYlyarlrgvpaEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 146 VAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQiSMLISSHQLGELEALCNRY-IYIEGgklAESFIGKAQpslvvH 224
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLaIMVKG---AFQCLGTIQ-----H 2156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 225 LNSKY---HMCNLKDHisqgiTLRDGLL------------DIPISVDKE-------------ALNDIFGVLASES---LI 273
Cdd:TIGR01257 2157 LKSKFgdgYIVTMKIK-----SPKDDLLpdlnpveqffqgNFPGSVQRErhynmlqfqvsssSLARIFQLLISHKdslLI 2231
|
330
....*....|....*
gi 1937413360 274 ESIEVKENHLKEVFM 288
Cdd:TIGR01257 2232 EEYSVTQTTLDQVFV 2246
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-208 |
2.41e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.43 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN-------SNDNV 73
Cdd:PRK11300 5 LLSVSGLMMRFGG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghqiARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 LEDFgimiEPV-FYPEMSVIDNLKFYLKLHGKKELYSNIERT-----------------LKLVELWESRNRKPKGFSFGM 135
Cdd:PRK11300 83 VRTF----QHVrLFREMTVIENLLVAQHQQLKTGLFSGLLKTpafrraesealdraatwLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 136 KQRTALAIALVAEPDFLILDEPFVGLDP---VGVQKLIDILKKwssERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPketKELDELIAELRN---EHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-209 |
2.76e-21 |
|
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: 88.64 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKfpgndfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-------- 72
Cdd:cd03215 4 VLEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdairagi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 --VLED---FGIMiepvfyPEMSVIDNLkfylklhgkkelysNIERTLklvelwesrnrkpkgfSFGMKQRTALAIALVA 147
Cdd:cd03215 78 ayVPEDrkrEGLV------LDLSVAENI--------------ALSSLL----------------SGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 148 EPDFLILDEPFVGLDpVG----VQKLIDILKkwssERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:cd03215 122 DPRVLILDEPTRGVD-VGakaeIYRLIRELA----DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-210 |
3.21e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.22 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS----------- 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaelarrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 70 ----NDNVLEDFGImIEPVfypEMSVIDNlkfylkLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIAL 145
Cdd:PRK13548 80 vlpqHSSLSFPFTV-EEVV---AMGRAPH------GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 146 V------AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGeLEAL-CNRYIYIEGGKLA 210
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLN-LAARyADRIVLLHQGRLV 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-209 |
3.78e-21 |
|
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: 92.94 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGND---FYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIsyngtdinsNDNVLEDF 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV---------NVRVGDEW 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIEPVF-------------------YPEMSVIDNLKFYLKLHGKKEL-YSNIERTLKLVELWESR-----NRKPKGFS 132
Cdd:TIGR03269 350 VDMTKPGPdgrgrakryigilhqeydlYPHRTVLDNLTEAIGLELPDELaRMKAVITLKMVGFDEEKaeeilDKYPDELS 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 133 FGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-197 |
4.73e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 92.73 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD--ADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -----EPVFYPEmSVIDNLKFYLKlhGKKElySNIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIAL 145
Cdd:TIGR02857 399 awvpqHPFLFAG-TIAENIRLARP--DASD--AEIREALERAGLDEFVAALPQGLdtpigeggaglSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 146 VAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLGELEAL 197
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALA 523
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-209 |
5.34e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKF-PGNDFYS--LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN--DNVLED 76
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGIMIEPVF-YPEM-----SVIDNLKFYLKLHG--KKELYSNIERTLKLVELWES-RNRKPKGFSFGMKQRTALAIALVA 147
Cdd:PRK13641 83 LRKKVSLVFqFPEAqlfenTVLKDVEFGPKNFGfsEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLIsSHQLGELEALCNRYIYIEGGKL 209
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILV-THNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
5.74e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNdFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND--NVLEDFG 78
Cdd:PRK13652 3 LIETRDLCYSYSGS-KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENirEVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMIE----PVFYPemSVIDNLKFYLKLHGKKE--LYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFL 152
Cdd:PRK13652 82 LVFQnpddQIFSP--TVEQDIAFGPINLGLDEetVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 153 ILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLgELEALCNRYIYI 204
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQL-DLVPEMADYIYV 210
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-211 |
7.26e-21 |
|
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: 88.83 E-value: 7.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN--SNDNVLEDFGI 79
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIEPVFYPEMSVIDNLKFYLKLHGKKElysnIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAE 148
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREE----VEEAARAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 149 PDFLILDEPFVGLDPVG---VQKLIDILkkwsSERQISMLIsSHQLGELEAlCNRYIYIEGGKLAE 211
Cdd:cd03251 157 PPILILDEATSALDTESerlVQAALERL----MKNRTTFVI-AHRLSTIEN-ADRIVVLEDGKIVE 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-210 |
7.96e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 87.61 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 5 ENLSKKFPGNDFYS----LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA--KSQKPTSGKISYNGTDINsndnvLEDFG 78
Cdd:cd03213 7 RNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD-----KRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMI-----EPVFYPEMSVIDNLKFYLKLhgkkelysniertlklvelwesrnrkpKGFSFGMKQRTALAIALVAEPDFLI 153
Cdd:cd03213 82 KIIgyvpqDDILHPTLTVRETLMFAAKL---------------------------RGLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 154 LDEPFVGLDPVGVQKLIDILKKWSSErQISMLISSHQL-GELEALCNRYIYIEGGKLA 210
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-208 |
1.93e-20 |
|
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: 90.65 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAK--SQKPTSGKISYNGTDIN-SNDNVLEDF 77
Cdd:TIGR02633 1 LLEMKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKaSNIRDTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMI---EPVFYPEMSVIDN--LKFYLKLHGKK----ELYSNIERTLKLVELWESRNRKPKG-FSFGMKQRTALAIALVA 147
Cdd:TIGR02633 79 GIVIihqELTLVPELSVAENifLGNEITLPGGRmaynAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSeRQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-163 |
2.37e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpGNDFySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-------- 72
Cdd:COG4604 1 MIEIKNVSKRY-GGKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 VLEDfgimiEPVFYPEMSVIDNLKF----YLKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:COG4604 79 ILRQ-----ENHINSRLTVRELVAFgrfpYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170
....*....|....*
gi 1937413360 149 PDFLILDEPFVGLDP 163
Cdd:COG4604 154 TDYVLLDEPLNNLDM 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-211 |
4.70e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 14 NDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAK------SQKPTSGKISYNGTDINSNDNV--LEDFGIMI-EPV 84
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiydSKIKVDGKVLYFGKDIFQIDAIklRKEVGMVFqQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 85 FYPEMSVIDNLKFYLKLHG---KKELYSNIERTLKLVELW----ESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGikeKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 158 FVGLDPVG---VQKLIDILKKwsserQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK14246 181 TSMIDIVNsqaIEKLITELKN-----EIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-210 |
6.60e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.86 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 14 NDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN------------SNDNVLEDFGIMI 81
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqalqknlvayvpQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVF----YPEMSVIDnlkfylklHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:PRK15056 98 EDVVmmgrYGHMGWLR--------RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 158 FVGLDPVGVQKLIDILKKWSSERQiSMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVKGTVLA 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-213 |
1.07e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNdNVLEDF--GI 79
Cdd:PRK11288 5 LSFDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA-STTAALaaGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MI---EPVFYPEMSVIDNLkfYL-KL---HG---KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEP 149
Cdd:PRK11288 82 AIiyqELHLVPEMTVAENL--YLgQLphkGGivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 150 DFLILDEPFVGLDPVGVQKLIDILKKWSSERQIsMLISSHQLGELEALCNRYIYIEGGKLAESF 213
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGRYVATF 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-212 |
1.23e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 84.50 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA--KSQKPTSGKISYNGTDINS---NDNVLEd 76
Cdd:cd03217 1 LEIKDLHVSV--GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDlppEERARL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 fGIMI---EPVFYPEMSVIDNLKfylklhgkkelYSNiertlklvelwesrnrkpKGFSFGMKQRTALAIALVAEPDFLI 153
Cdd:cd03217 78 -GIFLafqYPPEIPGVKNADFLR-----------YVN------------------EGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 154 LDEPFVGLDPVGVQKLIDILKKWSSERQiSMLISSHQLGELEALCNRYIYI-EGGKLAES 212
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIKPDRVHVlYDGRIVKS 186
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-211 |
1.78e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.41 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN-----------SN 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 71 DNVLEDFGIMIEPVF-----YPEMSVIDN-LKFYLKLHG--KKELYSNIERTLKLVELWE-SRNRKPKGFSFGMKQRTAL 141
Cdd:PRK10619 84 KNQLRLLRTRLTMVFqhfnlWSHMTVLENvMEAPIQVLGlsKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 142 AIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQiSMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-212 |
2.18e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.57 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 18 SLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND------NVLEDFGIMIEpvfYPEM-- 89
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQIRKKVGLVFQ---FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 90 ---SVIDNLKFYLKLHG--KKELYSNIERTLKLVELWES-RNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDP 163
Cdd:PRK13649 99 feeTVLKDVAFGPQNFGvsQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 164 VGVQKLIDILKKWsSERQISMLISSHQLGELEALCNrYIYI-EGGKLAES 212
Cdd:PRK13649 179 KGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYAD-FVYVlEKGKLVLS 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-191 |
2.28e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.44 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMIEPVFY-PEMSV----ID 93
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQdPEQQIfytdID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 94 -NLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLI 170
Cdd:PRK13638 97 sDIAFSLRNLGvpEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180
....*....|....*....|.
gi 1937413360 171 DILKKWSSERQiSMLISSHQL 191
Cdd:PRK13638 177 AIIRRIVAQGN-HVIISSHDI 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-196 |
2.43e-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: 83.70 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI--EPVFYPEMSVIDNLK 96
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLghAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 97 FYLKLHGKkelySNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKW 176
Cdd:cd03231 96 FWHADHSD----EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170 180
....*....|....*....|
gi 1937413360 177 SSERQISMLISSHQLGELEA 196
Cdd:cd03231 172 CARGGMVVLTTHQDLGLSEA 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-190 |
2.62e-19 |
|
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: 84.24 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 5 ENLSKKFPGNDFYS--LSDVSLEIEKGEIVGLIGKNGAGKSTLMKM---MAKSQKPTSGKISYNGTDIN---SNDNV--L 74
Cdd:cd03234 7 WDVGLKAKNWNKYAriLNDVSLHVESGQVMAILGSSGSGKTTLLDAisgRVEGGGTTSGQILFNGQPRKpdqFQKCVayV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 75 EDFGImiepvFYPEMSVIDNLKFYLKLHGKKELYSNIER------TLKLVELWESRNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:cd03234 87 RQDDI-----LLPGLTVRETLTYTAILRLPRKSSDAIRKkrvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937413360 149 PDFLILDEPFVGLDPVGVQKLIDILKKWSSERQIsMLISSHQ 190
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRI-VILTIHQ 202
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-228 |
4.59e-19 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 83.85 E-value: 4.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA--KSQKPTSGKISYNGTDINS-NDNVLEDFG 78
Cdd:TIGR01978 1 LKIKDLHVSV--EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLElEPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMIEPVFYPEMSVIDNLKFY-------LKLHGK---------KELYSNIErTLKLVELWESRNRKpKGFSFGMKQRTALA 142
Cdd:TIGR01978 79 LFLAFQYPEEIPGVSNLEFLrsalnarRSARGEepldlldfeKLLKEKLA-LLDMDEEFLNRSVN-EGFSGGEKKRNEIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 143 IALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQiSMLISSHQLGELEALCNRYIYI-EGGKLAESfigkAQPSL 221
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRLLNYIKPDYVHVlLDGRIVKS----GDVEL 231
|
....*..
gi 1937413360 222 VVHLNSK 228
Cdd:TIGR01978 232 AKELEAK 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-190 |
5.97e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.58 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA--KSQKPTSGKISYNGTDINS---NDNVLEd 76
Cdd:COG0396 1 LEIKNLHVSVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILElspDERARA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 fGIMI---EPVFYPEMSVIDNLKFYLKLHGKKEL-----YSNIERTLKLVELWESRNRKP--KGFSFGMKQRTALAIALV 146
Cdd:COG0396 78 -GIFLafqYPVEIPGVSVSNFLRTALNARRGEELsarefLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSErQISMLISSHQ 190
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHY 199
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-209 |
6.98e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYS--LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLE--- 75
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 ---DFGIMIEpvFY---PEMSVIDNLKFYLKLHGKK--ELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVA 147
Cdd:PRK11629 85 rnqKLGFIYQ--FHhllPDFTALENVAMPLLIGKKKpaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLgELEALCNRYIYIEGGKL 209
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRL 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-202 |
7.74e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 82.87 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFP-----GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYN----GTDINSND 71
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 72 -------------------NVL-----EDfgIMIEPVFypEMSVidnlkfylklhGKKELYSNIERTLKLV----ELWES 123
Cdd:COG4778 84 preilalrrrtigyvsqflRVIprvsaLD--VVAEPLL--ERGV-----------DREEARARARELLARLnlpeRLWDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 124 rnrKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDIL--KKwssERQISMLISSHQLGELEALCNRY 201
Cdd:COG4778 149 ---PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIeeAK---ARGTAIIGIFHDEEVREAVADRV 222
|
.
gi 1937413360 202 I 202
Cdd:COG4778 223 V 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-218 |
8.85e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.35 E-value: 8.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAK-----SQKPTSGKISYNGTDINSND----NVLEDFGIMIE-PVFYPE 88
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllelnEEARVEGEVRLFGRNIYSPDvdpiEVRREVGMVFQyPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 89 MSVIDNLKFYLKLHG----KKELYSNIERTLKLVELW-ESRNR---KPKGFSFGMKQRTALAIALVAEPDFLILDEPFVG 160
Cdd:PRK14267 100 LTIYDNVAIGVKLNGlvksKKELDERVEWALKKAALWdEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 161 LDPVGVQKLIDILKKWSSERQIsmLISSHQLGELEALCNRYIYIEGGKLAEsfIGKAQ 218
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIE--VGPTR 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-191 |
1.04e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.29 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQK--PT---SGKISYNGTDINSND----N 72
Cdd:PRK14243 11 LRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDvdpvE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 VLEDFGIMIE-PVFYPEmSVIDNLKFYLKLHG-KKELYSNIERTLKLVELWESRNRKPK----GFSFGMKQRTALAIALV 146
Cdd:PRK14243 89 VRRRIGMVFQkPNPFPK-SIYDNIAYGARINGyKGDMDELVERSLRQAALWDEVKDKLKqsglSLSGGQQQRLCIARAIA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937413360 147 AEPDFLILDEPFVGLDPVG---VQKLIDILKkwsseRQISMLISSHQL 191
Cdd:PRK14243 168 VQPEVILMDEPCSALDPIStlrIEELMHELK-----EQYTIIIVTHNM 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-220 |
2.37e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPG-NDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND--NVLEDF 77
Cdd:PRK13642 4 ILEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIEPV--FYPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLI 153
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 154 LDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGElEALCNRYIYIEGGKLaesfIGKAQPS 220
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDE-AASSDRILVMKAGEI----IKEAAPS 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-212 |
3.06e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.54 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTS---GKISYNGTDINSND--NVLED 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTvwDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGImiepVF------YPEMSVIDNLKFYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:PRK13640 86 VGI----VFqnpdnqFVGATVGDDVAFGLENRAvpRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 149 PDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGElEALCNRYIYIEGGKLAES 212
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQ 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-191 |
3.92e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 83.95 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI 81
Cdd:TIGR02868 335 LELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EP----VFypEMSVIDNLKFYLKLHGKKELYSNIERtlklVELWESRNRKPKG-----------FSFGMKQRTALAIALV 146
Cdd:TIGR02868 414 CAqdahLF--DTTVRENLRLARPDATDEELWAALER----VGLADWLRALPDGldtvlgeggarLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQL 191
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-208 |
5.54e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAkSQKPT---SGKISYNGTDIN-SNDNVLED 76
Cdd:PRK13549 5 LLEMKNITKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS-GVYPHgtyEGEIIFEGEELQaSNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGIMI---EPVFYPEMSVIDNLkfYLK---LHGKK----ELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:PRK13549 82 AGIAIihqELALVKELSVLENI--FLGneiTPGGImdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSeRQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-173 |
8.64e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.46 E-value: 8.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 20 SDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvlEDF-----------GImiepvfYPE 88
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR---DEYhqdllylghqpGI------KTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 89 MSVIDNLKFYLKLHGkkeLYSN--IERTLKLVELwesrnrkpKGF--------SFGMKQRTALAIALVAEPDFLILDEPF 158
Cdd:PRK13538 89 LTALENLRFYQRLHG---PGDDeaLWEALAQVGL--------AGFedvpvrqlSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170
....*....|....*
gi 1937413360 159 VGLDPVGVQKLIDIL 173
Cdd:PRK13538 158 TAIDKQGVARLEALL 172
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-211 |
1.15e-17 |
|
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: 80.22 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 5 ENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN--VLEDFGIMIE 82
Cdd:cd03252 4 EHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 PVFYPEMSVIDNLKF------------YLKLHGKKELysnierTLKLVELWES-RNRKPKGFSFGMKQRTALAIALVAEP 149
Cdd:cd03252 84 ENVLFNRSIRDNIALadpgmsmervieAAKLAGAHDF------ISELPEGYDTiVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 150 DFLILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLGELEAlCNRYIYIEGGKLAE 211
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVE 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-212 |
1.61e-17 |
|
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: 79.58 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND--NVLEDFGIMIEPVFYPEMSVIDNLK 96
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 97 fYLKLHGKKELysnIERTLKLVELWESRNRKPKG-----------FSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVG 165
Cdd:cd03254 99 -LGRPNATDEE---VIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937413360 166 VQKLIDILKKWSSERqiSMLISSHQLGELEAlCNRYIYIEGGKLAES 212
Cdd:cd03254 175 EKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-200 |
1.78e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAkSQKPT---SGKISYNGT-----DINSNdn 72
Cdd:NF040905 1 ILEMRGITKTFPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-GVYPHgsyEGEILFDGEvcrfkDIRDS-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 vlEDFGIMI---EPVFYPEMSVIDNLkFYLKLHGKK------ELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAI 143
Cdd:NF040905 76 --EALGIVIihqELALIPYLSIAENI-FLGNERAKRgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 144 ALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLIsSHQLGELEALCNR 200
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIII-SHKLNEIRRVADS 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-179 |
2.66e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.39 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND--------- 71
Cdd:COG4559 1 MLEAENLSVRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelarrra 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 72 ------------NVLEDFGIMIEPVFYPemsvidnlkfylklhgKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRT 139
Cdd:COG4559 79 vlpqhsslafpfTVEEVVALGRAPHGSS----------------AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937413360 140 ALAIAL--VAEPD-----FLILDEPFVGLDPVGVQKLIDILKKWSSE 179
Cdd:COG4559 143 QLARVLaqLWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARR 189
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-209 |
3.68e-17 |
|
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: 78.28 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGN-DFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-VLEDFGI 79
Cdd:cd03248 12 VKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHkYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MI--EPVFYPEmSVIDNLKFYL---------KLHGKKELYSNIERTLKlvELWESRNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:cd03248 92 LVgqEPVLFAR-SLQDNIAYGLqscsfecvkEAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 149 PDFLILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLGELEAlCNRYIYIEGGKL 209
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-211 |
3.83e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAK-----SQKPTSGKISYNGTDINSNDnvLE 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMD--VI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 DFGIMIEPVF-----YPEMSVIDNLKFYLKLH----GKKELYSNIERTLKLVELWES-RNR--KPKG-FSFGMKQRTALA 142
Cdd:PRK14247 79 ELRRRVQMVFqipnpIPNLSIFENVALGLKLNrlvkSKKELQERVRWALEKAQLWDEvKDRldAPAGkLSGGQQQRLCIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 143 IALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLisSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLV--THFPQQAARISDYVAFLYKGQIVE 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-212 |
4.86e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvledfgimi 81
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD------------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epvfYPE------MSVI------------DNLKFYLKLHGKKELysniERTLKLVELwESRNRKPKGF-----------S 132
Cdd:PRK11160 407 ----YSEaalrqaISVVsqrvhlfsatlrDNLLLAAPNASDEAL----IEVLQQVGL-EKLLEDDKGLnawlgeggrqlS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 133 FGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQLGELEALcNRYIYIEGGKLAES 212
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-211 |
1.81e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.51 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 15 DFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS--NDNVLEDFGIMIEPVF-YPEMSV 91
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktKDKYIRPVRKRIGMVFqFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 92 IDNLKFYLKLHGKKELYSNIERTLK-----LVELWESRN---RKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDP 163
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKMNLDEVKNyahrlLMDLGFSRDvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937413360 164 VGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-211 |
1.82e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 79.16 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 17 YSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIsyngtDINSNDNVledfgIMIEPVFYPEMSVIDNLK 96
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAAL-----IAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 97 FYLKLHG--KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILK 174
Cdd:PRK13545 108 LKGLMMGltKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937413360 175 KWsSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK13545 188 EF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-212 |
1.94e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.37 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN------VLEDFGImiepVF-YPEM-- 89
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklkpLRKKVGI----VFqFPEHql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 90 ---SVIDNLKFYLKLHG--KKELYSNIERTLKLVELWES-RNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDP 163
Cdd:PRK13634 99 feeTVEKDICFGPMNFGvsEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937413360 164 VGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-204 |
1.94e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKfpgndfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-------- 72
Cdd:COG1129 256 VLEVEGLSVG------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdairagi 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 --VLED---FGIMiepvfyPEMSVIDN-----LKFYLK---LHGKKElysnIERTLKLVELWE----SRNRKPKGFSFGM 135
Cdd:COG1129 330 ayVPEDrkgEGLV------LDLSIRENitlasLDRLSRgglLDRRRE----RALAEEYIKRLRiktpSPEQPVGNLSGGN 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 136 KQRTALAIALVAEPDFLILDEPFVGLDpVG----VQKLIDILkkwsSERQISMLISSHQLGELEALCNRyIYI 204
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGID-VGakaeIYRLIREL----AAEGKAVIVISSELPELLGLSDR-ILV 466
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-208 |
3.20e-16 |
|
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: 75.20 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGND---FYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTdinsndnvledfg 78
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 imiepVFY-------PEMSVIDNLKFYLKLHgkKELYsniERTLKLVELWESRNRKPKG-----------FSFGMKQRTA 140
Cdd:cd03250 68 -----IAYvsqepwiQNGTIRENILFGKPFD--EERY---EKVIKACALEPDLEILPDGdlteigekginLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 141 LAIALVAEPDFLILDEPFVGLDPVGVQKLID--ILKKWSSERQIsmLISSHQLgELEALCNRYIYIEGGK 208
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTR--ILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-222 |
6.36e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpGNDFYsLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVL-EDFG 78
Cdd:PRK11231 2 TLRTENLTVGY-GTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLaRRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 IMIEPVFYPE-MSVIDNLKF----YLKLHGK--KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDF 151
Cdd:PRK11231 80 LLPQHHLTPEgITVRELVAYgrspWLSLWGRlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 152 LILDEPFVGLDPVGVQKLIDILKKWSSERQ--ISMLissHQLGELEALCNRYIYIEGGKLaesfIGKAQPSLV 222
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKtvVTVL---HDLNQASRYCDHLVVLANGHV----MAQGTPEEV 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
6.39e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.91 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN-------- 72
Cdd:PRK10908 1 MIRFEHVSKAYLGGR-QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNrevpflrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 ----VLEDFGIMIepvfypEMSVIDNLKFYLKLHGK--KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALV 146
Cdd:PRK10908 80 qigmIFQDHHLLM------DRTVYDNVAIPLIIAGAsgDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLAESFIGK 216
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-212 |
6.70e-16 |
|
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: 75.27 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN--VLEDFGIMI-EPVFYpEMSVIDNL 95
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIGLVSqEPVLF-DGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 96 KFylklhGKKELY-SNIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAEPDFLILDEPFVGLDP 163
Cdd:cd03249 98 RY-----GKPDATdEEVEEAAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 164 VG---VQKLIDILKKwssERQIsmLISSHQLGELEAlCNRYIYIEGGKLAES 212
Cdd:cd03249 173 ESeklVQEALDRAMK---GRTT--IVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-195 |
8.89e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 8.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNV-LEDFGIMIEPVF---Y----PEMS 90
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaQKLLRQKIQIVFqnpYgslnPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 91 VIDNLKFYLKLH---GKKELYSNIERTLKLVELW-ESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDpVGV 166
Cdd:PRK11308 111 VGQILEEPLLINtslSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD-VSV 189
|
170 180 190
....*....|....*....|....*....|
gi 1937413360 167 Q-KLIDILKKWSSERQISMLISSHQLGELE 195
Cdd:PRK11308 190 QaQVLNLMMDLQQELGLSYVFISHDLSVVE 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-212 |
8.93e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDI-NSNDNVLEDFGI 79
Cdd:PRK15439 11 LLCARSISKQYSGVEV--LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MI---EPVFYPEMSVIDNLKFYLKLHGKKElysniER-TLKLVELWESRNRKPKGFSFGMKQRTALAI--ALVAEPDFLI 153
Cdd:PRK15439 89 YLvpqEPLLFPNLSVKENILFGLPKRQASM-----QKmKQLLAALGCQLDLDSSAGSLEVADRQIVEIlrGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 154 LDEPFVGLDPVGVQKLIdilkkwsseRQISMLIS--------SHQLGELEALCNRYIYIEGGKLAES 212
Cdd:PRK15439 164 LDEPTASLTPAETERLF---------SRIRELLAqgvgivfiSHKLPEIRQLADRISVMRDGTIALS 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-206 |
9.93e-16 |
|
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: 74.75 E-value: 9.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 17 YSLSDVSLEIEKG-----EIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNvledfgiMIEPVFypEMSV 91
Cdd:cd03237 8 KTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ-------YIKADY--EGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 92 IDNLKFYLKLHGKKELY-SNIERTLKLVELWESRNRKPKGfsfGMKQRTALAIALVAEPDFLILDEPFVGLDpvGVQKLI 170
Cdd:cd03237 79 RDLLSSITKDFYTHPYFkTEIAKPLQIEQILDREVPELSG---GELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1937413360 171 --DILKKWSSERQISMLISSHQLGELEALCNRYIYIEG 206
Cdd:cd03237 154 asKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-190 |
1.21e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 16 FYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAK--SQKPTSGKIsyngtDINSNDnvledfgimiepvFYPEMSVID 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCV-----DVPDNQ-------------FGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 94 NLKFYLKLHGKKELYSNIertlKLVELWESRnRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDIL 173
Cdd:COG2401 105 AIGRKGDFKDAVELLNAV----GLSDAVLWL-RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179
|
170
....*....|....*..
gi 1937413360 174 KKWSSERQISMLISSHQ 190
Cdd:COG2401 180 QKLARRAGITLVVATHH 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-219 |
1.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.43 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 8 SKKFPgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKM-----MAKSQKPTSG--KISYNGTDINSNDNVLEDFGIM 80
Cdd:PRK13645 17 AKKTP-FEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGdyAIPANLKKIKEVKRLRKEIGLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEpvfYPEMSV----IDNLKFYLKLH---GKKELYSNIERTLKLVELWESR-NRKPKGFSFGMKQRTALAIALVAEPDFL 152
Cdd:PRK13645 96 FQ---FPEYQLfqetIEKDIAFGPVNlgeNKQEAYKKVPELLKLVQLPEDYvKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 153 ILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLaesfIGKAQP 219
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV----ISIGSP 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-204 |
1.32e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.16 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF-PGNDFYS--LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDN----- 72
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPFASraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 -VLEDFGIMIEpvfYPEM-----SVIDNLKFYLKLHG--KKELYSNIERTLKLV----ELWEsrnRKPKGFSFGMKQRTA 140
Cdd:PRK13643 81 pVRKKVGVVFQ---FPESqlfeeTVLKDVAFGPQNFGipKEKAEKIAAEKLEMVgladEFWE---KSPFELSGGQMRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 141 LAIALVAEPDFLILDEPFVGLDPvgvQKLIDILKKWSSERQI--SMLISSHQLGELEALCNrYIYI 204
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDP---KARIEMMQLFESIHQSgqTVVLVTHLMDDVADYAD-YVYL 216
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-156 |
1.86e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.16 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--PEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVFypemsvidnLKFYL--KLHGKK------ELYSNIERTLKL---VELWESRNRKPKgFSFGMKQRTALAIALVAEPD 150
Cdd:PRK10522 400 SAVF---------TDFHLfdQLLGPEgkpanpALVEKWLERLKMahkLELEDGRISNLK-LSKGQKKRLALLLALAEERD 469
|
....*.
gi 1937413360 151 FLILDE 156
Cdd:PRK10522 470 ILLLDE 475
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-211 |
1.88e-15 |
|
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: 73.68 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND-NVLEDFGIM 80
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 I--EPVFYpEMSVIDNLKFyLKLHGKKELYsnieRTLKLVELWESRNRKPKG-----------FSFGMKQRTALAIALVA 147
Cdd:cd03244 83 IpqDPVLF-SGTIRSNLDP-FGEYSDEELW----QALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSERqiSMLISSHQlgeLEAL--CNRYIYIEGGKLAE 211
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHR---LDTIidSDRILVLDKGRVVE 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-211 |
1.97e-15 |
|
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: 73.80 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMIEPVfyPEMSVI------ 92
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT--LDSLRRAIGVV--PQDTVLfndtig 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 93 DNLKfYLKLHGKKElysNIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAEPDFLILDEPFVGL 161
Cdd:cd03253 93 YNIR-YGRPDATDE---EVIEAAKAAQIHDKIMRFPDGYdtivgerglklSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 162 DPVGVQKLIDILKKWSSERqiSMLISSHQLGELeALCNRYIYIEGGKLAE 211
Cdd:cd03253 169 DTHTEREIQAALRDVSKGR--TTIVIAHRLSTI-VNADKIIVLKDGRIVE 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-211 |
2.18e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 74.07 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN-----------S 69
Cdd:COG4598 8 ALEVRDLHKSFGDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 70 NDNVLEDFGIMIEPVF-----YPEMSVIDNLKF----YLKLhGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTA 140
Cdd:COG4598 86 DRRQLQRIRTRLGMVFqsfnlWSHMTVLENVIEapvhVLGR-PKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 141 LAIALVAEPDFLILDEPFVGLDP--VG-VQKLIDILkkwsSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPelVGeVLKVMRDL----AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEE 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-208 |
2.39e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.91 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIeNLSKKFPGNDFyslsDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNvledfGIM 80
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL----TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEK-----GIC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEP-------VF-----YPEMSVIDNLKFYLKlHGKKELYSNIERTLKLVELWesrNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:PRK11144 71 LPPekrrigyVFqdarlFPHYKVRGNLRYGMA-KSMVAQFDKIVALLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 149 PDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:PRK11144 147 PELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-211 |
2.99e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF--PGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKS-TLMKMMAKSQKP----TSGKISYNGTDI-NSNDN 72
Cdd:PRK15134 5 LLAIENLSVAFrqQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 VLEDF-GIMIEPVFYPEMSVIDNL-----KFY--LKLH---GKKELYSNIERTLKLVELWESRNRK---PKGFSFGMKQR 138
Cdd:PRK15134 85 TLRGVrGNKIAMIFQEPMVSLNPLhtlekQLYevLSLHrgmRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 139 TALAIALVAEPDFLILDEPFVGLDpVGVQ-KLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALD-VSVQaQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-191 |
3.82e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 74.36 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDI-NSNDNVLEDFGIMIEPVFY-------PEMSVI 92
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDEWRAVRSDIQMIFQdplaslnPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 93 D----NLK-FYLKLHgKKELYSNIERTLKLVELWESR-NRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDpVGV 166
Cdd:PRK15079 119 EiiaePLRtYHPKLS-RQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD-VSI 196
|
170 180
....*....|....*....|....*.
gi 1937413360 167 Q-KLIDILKKWSSERQISMLISSHQL 191
Cdd:PRK15079 197 QaQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-212 |
3.83e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNdfySLSDVSLEIEKGEIVGLIGKNGAGKS----TLMKMMAKSQKPTSGKISYNGTDINSNDnvLEdf 77
Cdd:PRK10418 5 IELRNIALQAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCA--LR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIEPV-------FYPEMSVIDNLKFYLKLHGKKELYSNIERTLKLVELwESRNRKPKGFSF----GMKQRTALAIALV 146
Cdd:PRK10418 78 GRKIATImqnprsaFNPLHTMHTHARETCLALGKPADDATLTAALEAVGL-ENAARVLKLYPFemsgGMLQRMMIALALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQ 222
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-174 |
5.27e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLskKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA--KSQKPTSGKISYNGTDINSND-NVLEDF 77
Cdd:CHL00131 7 ILEIKNL--HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEpEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIE---PVFYPEMSVIDNLKFYL----KLHGKKEL-----YSNIERTLKLVELWES---RNRKpKGFSFGMKQRTALA 142
Cdd:CHL00131 85 GIFLAfqyPIEIPGVSNADFLRLAYnskrKFQGLPELdplefLEIINEKLKLVGMDPSflsRNVN-EGFSGGEKKRNEIL 163
|
170 180 190
....*....|....*....|....*....|..
gi 1937413360 143 IALVAEPDFLILDEPFVGLDpvgvqklIDILK 174
Cdd:CHL00131 164 QMALLDSELAILDETDSGLD-------IDALK 188
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-209 |
7.29e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMIEP 83
Cdd:PRK10575 14 LRNVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 84 VFYPE---MSVIDNLKF-YLKLHGK-----KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK10575 92 QQLPAaegMTVRELVAIgRYPWHGAlgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 155 DEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-216 |
1.04e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.93 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKP---TSGKISYNGTDINSNDNVLEDFGIMIEPVFYPEMSVIDNL 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 96 KF--YLKLH------GKKELYSNIERTLKLVELWESRNRKP---KGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPV 164
Cdd:TIGR00955 121 MFqaHLRMPrrvtkkEKRERVDEVLQALGLRKCANTRIGVPgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 165 GVQKLIDILKKWSSERQIsMLISSHQ-LGELEALCNRYIYIEGGKLAesFIGK 216
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKT-IICTIHQpSSELFELFDKIILMAEGRVA--YLGS 250
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-212 |
1.15e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 74.01 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND-NVLEDFGIMI--EPVFYpEMSVIDNL 95
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrHTLRQFINYLpqEPYIF-SGSILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 96 kfylkLHGKKELYS--NIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAEPDFLILDEPFVGLD 162
Cdd:TIGR01193 569 -----LLGAKENVSqdEIWAACEIAEIKDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 163 PVGVQKLIDILKKWSSErqiSMLISSHQLgELEALCNRYIYIEGGKLAES 212
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRL-SVAKQSDKIIVLDHGKIIEQ 689
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-211 |
1.23e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.13 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKK-------FPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNV 73
Cdd:PRK15112 4 LLEVRNLSKTfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 LEDFGI-MI--EPV--FYPEMSVIDNLKFYLKLHGK---KELYSNIERTLKLVELW-ESRNRKPKGFSFGMKQRTALAIA 144
Cdd:PRK15112 84 YRSQRIrMIfqDPStsLNPRQRISQILDFPLRLNTDlepEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937413360 145 LVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-211 |
1.31e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNV------LEDFGIMIEP-VFYPEMSV 91
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraklrAKHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 92 IDNLKFYLKLHGKKELYSNiERTLKLVE---LWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQK 168
Cdd:PRK10584 106 LENVELPALLRGESSRQSR-NGAKALLEqlgLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937413360 169 LIDILKKWSSERQISMLISSHQLgELEALCNRYIYIEGGKLAE 211
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQLQE 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-217 |
1.46e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.47 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpGND---FYSLSDVSLEIEKGEIVGLIGKNGAGKS----TLMKMMAKSQKPTSGKISYNGTDIN--SND 71
Cdd:PRK11022 3 LLNVDKLSVHF-GDEsapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQriSEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 72 NVLEDFGIMIEPVFYPEMSVID-------NLKFYLKLHGKKELYSNIERTLKLVELW-----ESR-NRKPKGFSFGMKQR 138
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNpcytvgfQIMEAIKVHQGGNKKTRRQRAIDLLNQVgipdpASRlDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 139 TALAIALVAEPDFLILDEPFVGLDpVGVQ-KLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAESfiGKA 217
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALD-VTIQaQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET--GKA 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-211 |
2.72e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.83 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI---EPVFYpEMSVIDNL 95
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALvgqEPVLF-SGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 96 KFYLKLHGKKELY-----SNIERTLKLVELWESRNRKPKG--FSFGMKQRTALAIALVAEPDFLILDEPFVGLDpVGVQK 168
Cdd:TIGR00958 576 AYGLTDTPDEEIMaaakaANAHDFIMEFPNGYDTEVGEKGsqLSGGQKQRIAIARALVRKPRVLILDEATSALD-AECEQ 654
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937413360 169 LIDILKKWSSErqiSMLISSHQLGELEAlCNRYIYIEGGKLAE 211
Cdd:TIGR00958 655 LLQESRSRASR---TVLLIAHRLSTVER-ADQILVLKKGSVVE 693
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
7.59e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.65 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF---PGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIS----YNGTDINSNDNV 73
Cdd:PRK13631 21 ILRVKNLYCVFdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 -------LEDFGIM---IEPVF-YPEMSVIDNL-----------------------KFYLKLHGKKELYsniertlklve 119
Cdd:PRK13631 101 tnpyskkIKNFKELrrrVSMVFqFPEYQLFKDTiekdimfgpvalgvkkseakklaKFYLNKMGLDDSY----------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 120 lwesRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLIsSHQLGELEALCN 199
Cdd:PRK13631 170 ----LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVI-THTMEHVLEVAD 244
|
250
....*....|...
gi 1937413360 200 RYIYIEGGKLAES 212
Cdd:PRK13631 245 EVIVMDKGKILKT 257
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-206 |
8.01e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGndfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSG------KISYNGTDINSNdnvl 74
Cdd:PRK13409 340 LVEYPDLTKKLGD---FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpelKISYKPQYIKPD---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 75 edfgimiepvfyPEMSVIDNLKFYLKLHGKKELYSNIERTLKLVELWEsrnRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK13409 413 ------------YDGTVEDLLRSITDDLGSSYYKSEIIKPLQLERLLD---KNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 155 DEPFVGLD---PVGVQKLIdilKKWSSERQISMLISSHQLGELEALCNRYIYIEG 206
Cdd:PRK13409 478 DEPSAHLDveqRLAVAKAI---RRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-175 |
8.04e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.15 E-value: 8.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 5 ENLSKKFPGNDfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInsNDNVLEDFGIMIEPV 84
Cdd:PRK13657 338 DDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI--RTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 85 FYPEM----SVIDNLKFylklhGK-----KELYsnieRTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIA 144
Cdd:PRK13657 415 FQDAGlfnrSIEDNIRV-----GRpdatdEEMR----AAAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRLAIARA 485
|
170 180 190
....*....|....*....|....*....|....
gi 1937413360 145 LVAEPDFLILDEPFVGLDPVG---VQKLIDILKK 175
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETeakVKAALDELMK 519
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-211 |
1.10e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 6 NLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSG-----KISYNGTDINSNDNVLE---DF 77
Cdd:PRK14271 26 NLTLGFAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEfrrRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIE-PVFYPeMSVIDNLKFYLKLHG---KKELYSNIERTLKLVELWES-RNR---KPKGFSFGMKQRTALAIALVAEP 149
Cdd:PRK14271 104 GMLFQrPNPFP-MSIMDNVLAGVRAHKlvpRKEFRGVAQARLTEVGLWDAvKDRlsdSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 150 DFLILDEPFVGLDPVGVQKLIDILKKWSSerQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-190 |
1.16e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.04 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA--KSQKPTSGKISYNGTDINsndnvlEDFGIMI-----EPVFYPEMSV 91
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLD------KNFQRSTgyveqQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 92 IDNLKFYLKLhgkkelysniertlklvelwesrnrkpKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLID 171
Cdd:cd03232 97 REALRFSALL---------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170
....*....|....*....
gi 1937413360 172 ILKKWSSERQiSMLISSHQ 190
Cdd:cd03232 150 FLKKLADSGQ-AILCTIHQ 167
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-206 |
1.32e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGtdinsndnvledfGIM 80
Cdd:PRK09544 4 LVSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------------KLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEPVfyPEMSVID-----NLKFYLKLH-GKKElySNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK09544 69 IGYV--PQKLYLDttlplTVNRFLRLRpGTKK--EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 155 DEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGEL-----EALC-NRYIYIEG 206
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmaktdEVLClNHHICCSG 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-189 |
2.73e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.54 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 5 ENLSKKFPGNDFYslsdvsleiekgeivGLIGKNGAGKSTLMKMMAKSQKPTSGKISyngtdINSNDNVledfGIMIEPV 84
Cdd:PRK15064 18 ENISVKFGGGNRY---------------GLIGANGCGKSTFMKILGGDLEPSAGNVS-----LDPNERL----GKLRQDQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 85 F-YPEMSVIDNLkfylkLHGKKEL----------YSNIERT----LKLVEL-----------WESRNRK-------PKGF 131
Cdd:PRK15064 74 FaFEEFTVLDTV-----IMGHTELwevkqerdriYALPEMSeedgMKVADLevkfaemdgytAEARAGElllgvgiPEEQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 132 SFGM--------KQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILkkwsSERQISMLISSH 189
Cdd:PRK15064 149 HYGLmsevapgwKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISH 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-211 |
3.28e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 69.66 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN--SNDNVLEDFGI 79
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIEPVFYPEMSVIDNLKFylklhGKKELYS--NIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALV 146
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAY-----ARTEQYSreQIEEAARMAYAMDFINKMDNGLdtvigengvllSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 147 AEPDFLILDEPFVGLD---PVGVQKLIDILKKwssERqiSMLISSHQLGELEAlCNRYIYIEGGKLAE 211
Cdd:PRK11176 497 RDSPILILDEATSALDtesERAIQAALDELQK---NR--TSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-194 |
3.86e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.05 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNvlEDFGIMIE-----PVFYPEmSVID 93
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP--EIYRQQVSycaqtPTLFGD-TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 94 NLKFYLKLHGKKELYSNIERTLKLVELWESRNRKP-KGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDI 172
Cdd:PRK10247 100 NLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
|
170 180
....*....|....*....|..
gi 1937413360 173 LKKWSSERQISMLISSHQLGEL 194
Cdd:PRK10247 180 IHRYVREQNIAVLWVTHDKDEI 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-209 |
4.00e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.37 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGND--FYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVL--- 74
Cdd:PRK10535 4 LLELKDIRRSYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 75 --EDFGIMIEPV-FYPEMSVIDNLKF---YLKLhGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAE 148
Cdd:PRK10535 84 rrEHFGFIFQRYhLLSHLTAAQNVEVpavYAGL-ERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 149 PDFLILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQlGELEALCNRYIYIEGGKL 209
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-211 |
4.69e-13 |
|
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: 66.67 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFG--- 78
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP--LEDLRssl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 --IMIEPVFYpEMSVIDNLKFYLKlhgkkelYSNiertlklVELWESRNRKPKG--FSFGMKQRTALAIALVAEPDFLIL 154
Cdd:cd03369 85 tiIPQDPTLF-SGTIRSNLDPFDE-------YSD-------EEIYGALRVSEGGlnLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 155 DEPFVGLD---PVGVQKLIDilkkwSSERQISMLISSHQLGELeALCNRYIYIEGGKLAE 211
Cdd:cd03369 150 DEATASIDyatDALIQKTIR-----EEFTNSTILTIAHRLRTI-IDYDKILVMDAGEVKE 203
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-194 |
5.59e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 11 FPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNgtDINSNDNVLED----FGIMIEPVFY 86
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH--DIPLTKLQLDSwrsrLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 87 PEMSVIDNLKFylklhGKKE-LYSNIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK10789 401 FSDTVANNIAL-----GRPDaTQQEIEHVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937413360 155 DEPFVGLDPVGVQKLIDILKKWSSERQIsmLISSHQLGEL 194
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRLSAL 513
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-213 |
5.61e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKkfPGndfysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN---DNVleDFG 78
Cdd:PRK10762 258 LKVDNLSG--PG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqDGL--ANG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 79 ImiepVFYPE----------MSVIDN-----LKFYLKLHGKKELYSNIERTLKLVELWE----SRNRKPKGFSFGMKQRT 139
Cdd:PRK10762 329 I----VYISEdrkrdglvlgMSVKENmsltaLRYFSRAGGSLKHADEQQAVSDFIRLFNiktpSMEQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 140 ALAIALVAEPDFLILDEPFVGLDpVGVQK----LIDILKKwsseRQISMLISSHQLGELEALCNRYIYIEGGKLAESF 213
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVD-VGAKKeiyqLINQFKA----EGLSIILVSSEMPEVLGMSDRILVMHEGRISGEF 477
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-162 |
6.22e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.33 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND--------- 71
Cdd:PRK09536 3 MIDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSaraasrrva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 72 ------NVLEDFGI--MIEPVFYPEMSVIDNlkfylklHGKKElYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAI 143
Cdd:PRK09536 81 svpqdtSLSFEFDVrqVVEMGRTPHRSRFDT-------WTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170
....*....|....*....
gi 1937413360 144 ALVAEPDFLILDEPFVGLD 162
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLD 171
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-209 |
6.27e-13 |
|
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: 69.17 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKpTSGKISYNGTDINSN--DNVLEDFGI 79
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVtlQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MIEPVFYPEMSVIDNLKFYlklhgkkELYSNIE--RTLKLVELWESRNRKPKGFSF-----------GMKQRTALAIALV 146
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPY-------EQWSDEEiwKVAEEVGLKSVIEQFPDKLDFvlvdggyvlsnGHKQLMCLARSIL 1369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSErqISMLISSHQlgeLEAL--CNRYIYIEGGKL 209
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHR---VEALleCQQFLVIEGSSV 1429
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-211 |
7.23e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFP---------GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-N 70
Cdd:PRK10261 313 ILQVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 71 DNVLEDFGIMIEPVFY-------PEMSVIDNLKFYLKLHGKKELYSNIERTLKLVE----LWESRNRKPKGFSFGMKQRT 139
Cdd:PRK10261 393 PGKLQALRRDIQFIFQdpyasldPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLErvglLPEHAWRYPHEFSGGQRQRI 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 140 ALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-217 |
7.38e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSkkfpGNDFyslSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLE-DFGIm 80
Cdd:PRK15439 269 LTVEDLT----GEGF---RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGL- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 iepVFYPEMSVIDNLkfYLK----------LHGKKELYSNIERTLKLVELW--------ESRNRKPKGFSFGMKQRTALA 142
Cdd:PRK15439 341 ---VYLPEDRQSSGL--YLDaplawnvcalTHNRRGFWIKPARENAVLERYrralnikfNHAEQAARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 143 IALVAEPDFLILDEPFVGLDpVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAESFIGKA 217
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVD-VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-206 |
7.92e-13 |
|
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: 68.27 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGndfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSG------KISYNGTDINSndnvle 75
Cdd:COG1245 342 VEYPDLTKSYGG---FSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlKISYKPQYISP------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 DFgimiepvfypEMSVIDNLKFYLK-LHGKKELYSNIERTLKLVELWEsrnRKPKGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:COG1245 413 DY----------DGTVEEFLRSANTdDFGSSYYKTEIIKPLGLEKLLD---KNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 155 DEPFVGLD---PVGVQKLIdilKKWSSERQISMLISSHQLGELEALCNRYIYIEG 206
Cdd:COG1245 480 DEPSAHLDveqRLAVAKAI---RRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-207 |
8.22e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.96 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDfySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA---KSQKPTSGKISYNGTDINSNDNVLEDF 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELLGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 -------GIMIEPV-FYPEMSVIDN---------------LKFYLKLHGKKELysnieRTLKLVELWESRNRKPKGFSFG 134
Cdd:PRK09984 82 rksrantGYIFQQFnLVNRLSVLENvligalgstpfwrtcFSWFTREQKQRAL-----QALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 135 MKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGG 207
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-206 |
1.16e-12 |
|
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: 64.90 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 25 EIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGtdinsndnvledfgimIEPVFYPEmsvidnlkfYLKLHGk 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------ITPVYKPQ---------YIDLSG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 105 kelysniertlklvelwesrnrkpkgfsfGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISM 184
Cdd:cd03222 75 -----------------------------GELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|..
gi 1937413360 185 LISSHQLGELEALCNRYIYIEG 206
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-213 |
1.22e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 9 KKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSN---DNVLEDFGIMIEPV- 84
Cdd:PRK09700 269 RNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsplDAVKKGMAYITESRr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 85 ---FYPEMSVIDNLKF--YLKLHGKKELYSNI---------ERTLKLVEL-WESRNRKPKGFSFGMKQRTALAIALVAEP 149
Cdd:PRK09700 349 dngFFPNFSIAQNMAIsrSLKDGGYKGAMGLFhevdeqrtaENQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 150 DFLILDEPFVGLDpVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAESF 213
Cdd:PRK09700 429 EVIIFDEPTRGID-VGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-166 |
2.35e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.87 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 11 FPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMIEPVFYPEMS 90
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 91 VIDNLKFYLKLHGK--KELYSNierTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGV 166
Cdd:PRK13543 99 TLENLHFLCGLHGRraKQMPGS---ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-215 |
2.77e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSND-NVLEDFGI 79
Cdd:PRK10762 4 LLQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MI---EPVFYPEMSVIDNL---KFYLKLHGK---KELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPD 150
Cdd:PRK10762 82 GIihqELNLIPQLTIAENIflgREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 151 FLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLIsSHQLGELEALCNRYIYIEGGKlaesFIG 215
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYI-SHRLKEIFEICDDVTVFRDGQ----FIA 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-191 |
3.98e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAkSQKPTSGKISYNGTDinsndnvLEDFG-------------------I 79
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMA-GLLPGSGSIQFAGQP-------LEAWSaaelarhraylsqqqtppfA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 MiePVFYpemsvidnlkfYLKLHG-----KKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIAL-----VAEP 149
Cdd:PRK03695 84 M--PVFQ-----------YLTLHQpdktrTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937413360 150 D--FLILDEPFVGLDpVGVQKLIDILKKWSSERQISMLISSHQL 191
Cdd:PRK03695 151 AgqLLLLDEPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-191 |
4.12e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQkPTSGKISYNGTDINSND-------------NVLEDFGImiePVF 85
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSaaelarhraylsqQQSPPFAM---PVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 86 YpemsvidnlkfYLKLHGKKELYSNIERTLkLVELWESRNRKPK------GFSFGMKQRTALAIALV-----AEPD--FL 152
Cdd:COG4138 88 Q-----------YLALHQPAGASSEAVEQL-LAQLAEALGLEDKlsrpltQLSGGEWQRVRLAAVLLqvwptINPEgqLL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937413360 153 ILDEPFVGLDpVGVQKLIDILKKWSSERQISMLISSHQL 191
Cdd:COG4138 156 LLDEPMNSLD-VAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-189 |
4.94e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIsYNGT--DINSNDNVLEDFGimi 81
Cdd:PRK11147 322 MENVNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTklEVAYFDQHRAELD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epvfyPEMSVIDNLKfylklHGKKELYSN-IERTLkLVELWE-----SRNRKP-KGFSFGMKQRTALAIALVAEPDFLIL 154
Cdd:PRK11147 396 -----PEKTVMDNLA-----EGKQEVMVNgRPRHV-LGYLQDflfhpKRAMTPvKALSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190
....*....|....*....|....*....|....*
gi 1937413360 155 DEPFVGLDpvgVQKLiDILKKWSSERQISMLISSH 189
Cdd:PRK11147 465 DEPTNDLD---VETL-ELLEELLDSYQGTVLLVSH 495
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-212 |
5.18e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF--PGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKS----TLMKMMAKSqkptSGKISYNGTDINS-NDNV 73
Cdd:PRK10261 12 VLAVENLNIAFmqEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQA----GGLVQCDKMLLRRrSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 LE---------------DFG-IMIEPV--FYPEMSVIDNLKFYLKLH---GKKELYSNIERTLKLVELWESR---NRKPK 129
Cdd:PRK10261 88 IElseqsaaqmrhvrgaDMAmIFQEPMtsLNPVFTVGEQIAESIRLHqgaSREEAMVEAKRMLDQVRIPEAQtilSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 130 GFSFGMKQRTALAIALVAEPDFLILDEPFVGLDpVGVQ----KLIDILKKwssERQISMLISSHQLGELEALCNRYIYIE 205
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALD-VTIQaqilQLIKVLQK---EMSMGVIFITHDMGVVAEIADRVLVMY 243
|
....*..
gi 1937413360 206 GGKLAES 212
Cdd:PRK10261 244 QGEAVET 250
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-75 |
1.27e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.57 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGT-----------DINSN 70
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvklayvdqsrdALDPN 400
|
....*
gi 1937413360 71 DNVLE 75
Cdd:TIGR03719 401 KTVWE 405
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-215 |
1.41e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNgTDI-----------NSNDNV-------LEDFGIM 80
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLivarlqqdpprNVEGTVydfvaegIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IEPvfYPEMSVI-------DNLKFYLKLHGKKE------LYSNIERTLKLVELweSRNRKPKGFSFGMKQRTALAIALVA 147
Cdd:PRK11147 98 LKR--YHDISHLvetdpseKNLNELAKLQEQLDhhnlwqLENRINEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSerqiSMLISSHQLGELEALCNRYIYIEGGKLAeSFIG 215
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV-SYPG 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-209 |
2.13e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.95 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKpTSGKISYNGtdINSNDNVLED----F 77
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG--VSWNSVPLQKwrkaF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 78 GIMIEPVFYPEMSVIDNLKFYLKlHGKKELYSNIERT-LKLVelwesRNRKPKGFSF-----------GMKQRTALAIAL 145
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGK-WSDEEIWKVAEEVgLKSV-----IEQFPGQLDFvlvdggcvlshGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 146 VAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSErqISMLISSHQlgeLEAL--CNRYIYIEGGKL 209
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHR---IEAMleCQRFLVIEENKV 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-213 |
3.43e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSkkFPGND-FYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDInSNDNVLEdfgiM 80
Cdd:COG3845 258 LEVENLS--VRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSPRE----R 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 IE-PVFY-----------PEMSVIDNLkfYLKLHGKKELYSNI--------ERTLKLVELWESRNRKP----KGFSFGMK 136
Cdd:COG3845 331 RRlGVAYipedrlgrglvPDMSVAENL--ILGRYRRPPFSRGGfldrkairAFAEELIEEFDVRTPGPdtpaRSLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 137 QRTALAIALVAEPDFLILDEPFVGLDpVG----VQKLIDILKkwssERQISMLISSHQLGELEALCNRYIYIEGGKLAES 212
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLD-VGaiefIHQRLLELR----DAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
.
gi 1937413360 213 F 213
Cdd:COG3845 484 V 484
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-208 |
6.99e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFPGndFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN--SNDNVLEDFGIMI 81
Cdd:PRK10982 1 MSNISKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 --EPVFYPEMSVIDNL-------KFYLKLHGKkeLYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFL 152
Cdd:PRK10982 79 hqELNLVLQRSVMDNMwlgryptKGMFVDQDK--MYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 153 ILDEPFVGLDPVGVQKLIDILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-156 |
7.21e-11 |
|
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: 62.51 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 22 VSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDnvLEDFGIMIEPVF---------YPEMSVI 92
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN--REAYRQLFSAVFsdfhlfdrlLGLDGEA 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 93 DNLKF-----YLKLHGKKELYSNIERTLKLvelwesrnrkpkgfSFGMKQRTALAIALVAEPDFLILDE 156
Cdd:COG4615 429 DPARArelleRLELDHKVSVEDGRFSTTDL--------------SQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-186 |
7.62e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 17 YSLSDV------SLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGK----------ISY-------------NGTDI 67
Cdd:PRK10938 11 FRLSDTktlqlpSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrLSFeqlqklvsdewqrNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 68 NSNDNvlEDFGIMIEPVFYPEMSVIDNLKFYLKLHGkkelysnIERTLklvelwesrNRKPKGFSFGMKQRTALAIALVA 147
Cdd:PRK10938 91 LSPGE--DDTGRTTAEIIQDEVKDPARCEQLAQQFG-------ITALL---------DRRFKYLSTGETRKTLLCQALMS 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937413360 148 EPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLI 186
Cdd:PRK10938 153 EPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-214 |
8.46e-11 |
|
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: 62.15 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGN-DFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKS-QKPTSGKISYNG--TDINSNDNVLED 76
Cdd:TIGR02633 257 ILEARNLTCWDVINpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGkpVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 fGIMIEPV------FYPEM--------SVIDNLKFYLKLHGKKELYSnIERTLKLVELWESRNRKPKG-FSFGMKQRTAL 141
Cdd:TIGR02633 337 -GIAMVPEdrkrhgIVPILgvgknitlSVLKSFCFKMRIDAAAELQI-IGSAIQRLKVKTASPFLPIGrLSGGNQQKAVL 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 142 AIALVAEPDFLILDEPFVGLDpVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAESFI 214
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVD-VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFV 486
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-211 |
2.01e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.01 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 22 VSLEIEKGEIVGLIGKNGAGKSTLMKMMAkSQKPTSGKISYNGTDINSNDnvLEDFGIMI-----EPVFyPEMSVIDNLk 96
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELD--PESWRKHLswvgqNPQL-PHGTLRDNV- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 97 fylkLHGKKELY-SNIERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAEPDFLILDEPFVGLDPV 164
Cdd:PRK11174 444 ----LLGNPDASdEQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937413360 165 GVQKLIDILKKwSSERQISMLIsSHQLGELEAlCNRYIYIEGGKLAE 211
Cdd:PRK11174 520 SEQLVMQALNA-ASRRQTTLMV-THQLEDLAQ-WDQIWVMQDGQIVQ 563
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-210 |
2.29e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 20 SDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNG--TDINSNDNVLEDfGIMIEPV------FYPEMSV 91
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRA-GIMLCPEdrkaegIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 92 IDN---------LKFYLKLHGKKELySNIERTLKLVEL-WESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGL 161
Cdd:PRK11288 349 ADNinisarrhhLRAGCLINNRWEA-ENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937413360 162 DpVGVQKLI-DILKKWsSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:PRK11288 428 D-VGAKHEIyNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-156 |
3.18e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.34 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINsndNVLEDFGIMI--EPVFYPEMSVIDNLK 96
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN---NIAKPYCTYIghNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 97 FYLKLHGKKELYSNIERTLKLVELWEsrnRKPKGFSFGMKQRTALAIALVAEPDFLILDE 156
Cdd:PRK13541 93 FWSEIYNSAETLYAAIHYFKLHDLLD---EKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-190 |
4.13e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSkkFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIM 80
Cdd:PRK13540 1 MLDVIELD--FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 81 I--EPVFYPEMSVIDNLKFYLKLHGKKELYSNIERTLKLVELWESrnrkPKG-FSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:PRK13540 79 VghRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDY----PCGlLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1937413360 158 FVGLDPVGvqkLIDILKKWSSERQI--SMLISSHQ 190
Cdd:PRK13540 155 LVALDELS---LLTIITKIQEHRAKggAVLLTSHQ 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-60 |
4.60e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 4.60e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 5 ENLSKKFPGNDFYSlsDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKI 60
Cdd:PRK11819 328 ENLSKSFGDRLLID--DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-206 |
5.62e-10 |
|
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: 57.16 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYngtdinsndnvLEDFGIMi 81
Cdd:cd03223 1 IELENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLL- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 epvFYPEmsvidnlKFYLKLhGkkelysnierTLK--LVELWESRnrkpkgFSFGMKQRTALAIALVAEPDFLILDEPFV 159
Cdd:cd03223 68 ---FLPQ-------RPYLPL-G----------TLReqLIYPWDDV------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937413360 160 GLDPVGVQKLIDILKkwssERQISmLIS-SHQlGELEALCNRYIYIEG 206
Cdd:cd03223 121 ALDEESEDRLYQLLK----ELGIT-VISvGHR-PSLWKFHDRVLDLDG 162
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-190 |
8.45e-10 |
|
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: 57.27 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 14 NDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA---KSQKPTSGKISYNGTDINSNDNVLEDFGIMI--EPVFYPE 88
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAnrtEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVseEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 89 MSVIDNLKFYLKLHGkkelysniertlklvelwesrNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQK 168
Cdd:cd03233 98 LTVRETLDFALRCKG---------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170 180
....*....|....*....|..
gi 1937413360 169 LIDILKKWSSERQISMLISSHQ 190
Cdd:cd03233 157 ILKCIRTMADVLKTTTFVSLYQ 178
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-208 |
9.72e-10 |
|
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: 57.76 E-value: 9.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 29 GEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIS-----------YNGTDI-NSNDNVLEDfgiMIEPVFYPEM------- 89
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELqNYFTKLLEG---DVKVIVKPQYvdlipka 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 90 ---SVIDNLKfylklhgKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLD---P 163
Cdd:cd03236 103 vkgKVGELLK-------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937413360 164 VGVQKLIDILkkwsSERQISMLISSHQLGELEALCNrYIYIEGGK 208
Cdd:cd03236 176 LNAARLIREL----AEDDNYVLVVEHDLAVLDYLSD-YIHCLYGE 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-162 |
1.05e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 27 EKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISyngtDINSNDNVLEDF-GIMIEPVFYP----EMSV------IDNL 95
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD----EEPSWDEVLKRFrGTELQDYFKKlangEIKVahkpqyVDLI 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 96 KFYLKlhGK-KELYSNI-ERTL-----KLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLD 162
Cdd:COG1245 173 PKVFK--GTvRELLEKVdERGKldelaEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-209 |
1.30e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQ---KPTSGKISYN-----GTDINSNDNV 73
Cdd:PLN03073 178 IHMENFSISVGGRDL--IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQILHVeqevvGDDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 74 L-----------EDFGIMIEPVFYPEMSVIDNLKFYLKLHGKKELYS----NIERTLKLVELW--ESR------------ 124
Cdd:PLN03073 256 LntdiertqlleEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSqrleEIYKRLELIDAYtaEARaasilaglsftp 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 125 ---NRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSerqiSMLISSHQLGELEALCNRY 201
Cdd:PLN03073 336 emqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAREFLNTVVTDI 411
|
....*...
gi 1937413360 202 IYIEGGKL 209
Cdd:PLN03073 412 LHLHGQKL 419
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-162 |
2.39e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.00 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGND---FYS---------LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTdins 69
Cdd:TIGR01271 413 IKQNNKARKQPNGDdglFFSnfslyvtpvLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 70 ndnvledfgIMIEPVFYPEM--SVIDNLKFYLKLHGKKelYSNIERTLKLVE---LWESRNRKPKG-----FSFGMKQRT 139
Cdd:TIGR01271 489 ---------ISFSPQTSWIMpgTIKDNIIFGLSYDEYR--YTSVIKACQLEEdiaLFPEKDKTVLGeggitLSGGQRARI 557
|
170 180
....*....|....*....|...
gi 1937413360 140 ALAIALVAEPDFLILDEPFVGLD 162
Cdd:TIGR01271 558 SLARAVYKDADLYLLDSPFTHLD 580
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-211 |
2.49e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvledFGIM----------IEPVFYpE 88
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK-------FGLMdlrkvlgiipQAPVLF-S 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 89 MSVIDNLKFYLKlHGKKELYSNIERTlklvELWESRNRKPKG-----------FSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:PLN03130 1327 GTVRFNLDPFNE-HNDADLWESLERA----HLKDVIRRNSLGldaevseagenFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 158 FVGLDpVGVQKLIDilKKWSSE-RQISMLISSHQLGELeALCNRYIYIEGGKLAE 211
Cdd:PLN03130 1402 TAAVD-VRTDALIQ--KTIREEfKSCTMLIIAHRLNTI-IDCDRILVLDAGRVVE 1452
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-209 |
3.11e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.53 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN--SNDNVLEDFGIMIEPVFYPEMSVIDNLKFY 98
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARRIGLLAQNATTPGDITVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 99 -------LKLHGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLID 171
Cdd:PRK10253 105 gryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 1937413360 172 ILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKL 209
Cdd:PRK10253 185 LLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-211 |
4.17e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTD----INSNDNVLEdfgimIEPVFYpemsVIDN 94
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawVNQETPALP-----QPALEY----VIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 95 LKFYLKLhgKKELYSNIERT-----------LKLVELWESRNR----------------KP-KGFSFGMKQRTALAIALV 146
Cdd:PRK10636 88 DREYRQL--EAQLHDANERNdghaiatihgkLDAIDAWTIRSRaasllhglgfsneqleRPvSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 147 AEPDFLILDEPFVGLDPVGVqklidI-LKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLAE 211
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDAV-----IwLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-162 |
1.11e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.88 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 4 IENLSKKFpGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS-NDNVLEDFGIMIE 82
Cdd:PRK10790 343 IDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 --PVFYPEmSVIDNLKFylklhGKKELYSNIERTLKLVELWESRNRKPKG-----------FSFGMKQRTALAIALVAEP 149
Cdd:PRK10790 422 qdPVVLAD-TFLANVTL-----GRDISEEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTP 495
|
170
....*....|...
gi 1937413360 150 DFLILDEPFVGLD 162
Cdd:PRK10790 496 QILILDEATANID 508
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-190 |
1.71e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA----KSQKPTSGKISYNGTDinsndnvLEDF-----GIMI----EPVF 85
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT-------PEEIkkhyrGDVVynaeTDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 86 YPEMSVIDNLKFYLKLHGKKELYSNIER----------TLKLVELWESRNRKP-----KGFSFGMKQRTALAIALVAEPD 150
Cdd:TIGR00956 150 FPHLTVGETLDFAARCKTPQNRPDGVSReeyakhiadvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937413360 151 FLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQ 190
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQ 269
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-60 |
1.78e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 1.78e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 2 LKIENLSKKFPGNDFYSlsDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKI 60
Cdd:PRK15064 320 LEVENLTKGFDNGPLFK--NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-162 |
2.16e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 6 NLSKKFPGNDfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAksqkptsgkisynGTDINSNDNVLEDFGIMI---- 81
Cdd:TIGR03719 9 RVSKVVPPKK-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKDFNGEARPQPGIKVgylp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -EPVFYPEMSVIDNLKfyLKLHGKK-------ELYSN-----------IERTLKLVELWESRN---------------RK 127
Cdd:TIGR03719 75 qEPQLDPTKTVRENVE--EGVAEIKdaldrfnEISAKyaepdadfdklAAEQAELQEIIDAADawdldsqleiamdalRC 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937413360 128 PKG------FSFGMKQRTALAIALVAEPDFLILDEPFVGLD 162
Cdd:TIGR03719 153 PPWdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-208 |
2.22e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 26 IEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKisYNGTDinSNDNVLEDF-------------GIMIEPVFYPEMsvI 92
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEP--SWDEVLKRFrgtelqnyfkklyNGEIKVVHKPQY--V 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 93 DNLKFYLKlhGK-KELYSNI-ER-----TLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVG 165
Cdd:PRK13409 170 DLIPKVFK--GKvRELLKKVdERgkldeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937413360 166 VQKLIDILKKWSSERqiSMLISSHQLGELEALCNrYIYIEGGK 208
Cdd:PRK13409 248 RLNVARLIRELAEGK--YVLVVEHDLAVLDYLAD-NVHIAYGE 287
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-207 |
3.81e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.04 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNgtdinSNDNVLedfgimiepvFYPEMSvidnlkfY 98
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP-----AGARVL----------FLPQRP-------Y 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 99 LKLHGKKE--LYSN---------IERTLKLVEL------------WESRnrkpkgFSFGMKQRTALAIALVAEPDFLILD 155
Cdd:COG4178 437 LPLGTLREalLYPAtaeafsdaeLREALEAVGLghlaerldeeadWDQV------LSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 156 EPFVGLDPVGVQKLIDILKKwssERQISMLIS-SHQlGELEALCNRYIYIEGG 207
Cdd:COG4178 511 EATSALDEENEAALYQLLRE---ELPGTTVISvGHR-STLAAFHDRVLELTGD 559
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-246 |
4.55e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTS--GKISYNGTDINSNdnVLEDFGIMIEP-VFYPEMSVIDNL 95
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQ--ILKRTGFVTQDdILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 96 KFYLKLHGKKELySNIERTLK----LVELWESR-------NRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPV 164
Cdd:PLN03211 162 VFCSLLRLPKSL-TKQEKILVaesvISELGLTKcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 165 GVQKLIDILKKWS-------------SERQISMLISSHQLGElealcNRYIYIEGGKLAESFIGKAQPSLVVHLNSKYHM 231
Cdd:PLN03211 241 AAYRLVLTLGSLAqkgktivtsmhqpSSRVYQMFDSVLVLSE-----GRCLFFGKGSDAMAYFESVGFSPSFPMNPADFL 315
|
250
....*....|....*..
gi 1937413360 232 CNLKDHISQ--GITLRD 246
Cdd:PLN03211 316 LDLANGVCQtdGVSERE 332
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-194 |
5.01e-08 |
|
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: 51.22 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 28 KGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMIepvfypemsvidnlkfylklhgkkel 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 108 ysniertlklvelwesrNRKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDI-----LKKWSSERQI 182
Cdd:smart00382 55 -----------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNL 117
|
170
....*....|..
gi 1937413360 183 SMLISSHQLGEL 194
Cdd:smart00382 118 TVILTTNDEKDL 129
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-190 |
7.09e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAksQKPTSGKISynGTDINSNDNVL-EDFGIMI-----EPVFYPEMSVI 92
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT--GGDRLVNGRPLdSSFQRSIgyvqqQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 93 DNLKF--YLKLHG---KKELYSNIERTLKLVELwESRNRKPKGFS---FGMKQRTALAIA--LVAEPDFLI-LDEPFVGL 161
Cdd:TIGR00956 855 ESLRFsaYLRQPKsvsKSEKMEYVEEVIKLLEM-ESYADAVVGVPgegLNVEQRKRLTIGveLVAKPKLLLfLDEPTSGL 933
|
170 180
....*....|....*....|....*....
gi 1937413360 162 DPVGVQKLIDILKKWSSERQiSMLISSHQ 190
Cdd:TIGR00956 934 DSQTAWSICKLMRKLADHGQ-AILCTIHQ 961
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-214 |
1.01e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKS-QKPTSGKISYNGTDI---NSNDN-------VLED---FGIMiepvfy 86
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVkirNPQQAiaqgiamVPEDrkrDGIV------ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 87 PEMSVIDNL------KFYLK--LHGKKELySNIERTLKLVELWESRNRKPKG-FSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:PRK13549 354 PVMGVGKNItlaaldRFTGGsrIDDAAEL-KTILESIQRLKVKTASPELAIArLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 158 FVGLDpVG----VQKLIDILKKwsseRQISMLISSHQLGELEALCNRYIYIEGGKLAESFI 214
Cdd:PRK13549 433 TRGID-VGakyeIYKLINQLVQ----QGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLI 488
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-174 |
1.42e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFysLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQ--KPTSGKISYNGTDI---NSNDNVLE 75
Cdd:PRK09580 1 MLSIKDLHVSVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLlelSPEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 dfGIMIEPVFYPEMSVIDNlKFYL--------KLHGKKEL-----YSNIERTLKLVE-----LWESRNrkpKGFSFGMKQ 137
Cdd:PRK09580 79 --GIFMAFQYPVEIPGVSN-QFFLqtalnavrSYRGQEPLdrfdfQDLMEEKIALLKmpedlLTRSVN---VGFSGGEKK 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937413360 138 RTALAIALVAEPDFLILDEPFVGLDpvgvqklIDILK 174
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLD-------IDALK 182
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-288 |
1.66e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTlMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMI 81
Cdd:NF000106 14 VEVRGLVKHF--GEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 EPVFY---PEMSVIDNLKF---YLKLhGKKELYSNIERTLKLVELWESRNRKPKGFSFGMKQRTALAIALVAEPDFLILD 155
Cdd:NF000106 91 RPVR*grrESFSGRENLYMigr*LDL-SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 156 EPFVGLDPVGVQKLIDILKKWSSErQISMLISSHQLGELEALCNRYIYIEGGK-LAESFIGKAQP-----SLVVHLNSKY 229
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRvIADGKVDELKTkvggrTLQIRPAHAA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 230 HMCNLKDHISQ-------GITL--RDGLLDIPIsVDKEALNDIFGVLASESL-IESIEVKENHLKEVFM 288
Cdd:NF000106 249 ELDRMVGAIAQagldgiaGATAdhEDGVVNVPI-VSDEQLSAVVGMLGERGFtISGHQHPSAQL*EVFL 316
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-162 |
2.19e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 18 SLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTS-------GKISY--------NGTdinSNDNVLedFGIMIE 82
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirGSVAYvpqvswifNAT---VRENIL--FGSDFE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 PVFYPEMSVIDNLKFYLKLHGKKELYSNIERTLKLvelwesrnrkpkgfSFGMKQRTALAIALVAEPDFLILDEPFVGLD 162
Cdd:PLN03232 707 SERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNI--------------SGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-156 |
5.10e-07 |
|
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: 50.59 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN--SNDNVLEDFGIMiepvfyPEMSVIDNlk 96
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRdvTQASLRAAIGIV------PQDTVLFN-- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 97 fylklhgkKELYSNI------------ERTLKLVELWESRNRKPKGF-----------SFGMKQRTALAIALVAEPDFLI 153
Cdd:COG5265 446 --------DTIAYNIaygrpdaseeevEAAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPILI 517
|
...
gi 1937413360 154 LDE 156
Cdd:COG5265 518 FDE 520
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
132-190 |
6.23e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 6.23e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 132 SFGmKQRTAL-AIALVAEPDFLILDEPFVGLDPVG---VQKLIDILkkwSSERQISMLISSHQ 190
Cdd:PRK10938 403 SWG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNrqlVRRFVDVL---ISEGETQLLFVSHH 461
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-211 |
6.71e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvledFG----------IMIEPVFYpE 88
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK-------FGltdlrrvlsiIPQSPVLF-S 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 89 MSVIDNLKFYLKlHGKKELYSNIERTlklvELWESRNRKPKG-----------FSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:PLN03232 1324 GTVRFNIDPFSE-HNDADLWEALERA----HIKDVIDRNPFGldaevseggenFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937413360 158 FVGLDpVGVQKLIDilKKWSSE-RQISMLISSHQLGELeALCNRYIYIEGGKLAE 211
Cdd:PLN03232 1399 TASVD-VRTDSLIQ--RTIREEfKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLE 1449
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
3-162 |
8.21e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.47 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 3 KIENLSKKFPGND---FYS---------LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTdinsn 70
Cdd:cd03291 25 KQENNDRKHSSDDnnlFFSnlclvgapvLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 71 dnvledfgIMIEPVFYPEM--SVIDNLKFYLKLHGKKelYSNIERTLKLVE---LWESRNRKPKG-----FSFGMKQRTA 140
Cdd:cd03291 100 --------ISFSSQFSWIMpgTIKENIIFGVSYDEYR--YKSVVKACQLEEditKFPEKDNTVLGeggitLSGGQRARIS 169
|
170 180
....*....|....*....|..
gi 1937413360 141 LAIALVAEPDFLILDEPFVGLD 162
Cdd:cd03291 170 LARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-61 |
1.03e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 1 MLKIENLSKKFpgNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKIS 61
Cdd:PRK10636 312 LLKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG 370
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-162 |
1.47e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA--KSQKPTSGKISYNG-----------------TDINSndnvledfgi 79
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGfpkkqetfarisgyceqNDIHS---------- 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 80 miepvfyPEMSVIDNLKF--YLKLH---GKKELYSNIERTLKLVELWESRNR-----KPKGFSFGMKQRTALAIALVAEP 149
Cdd:PLN03140 966 -------PQVTVRESLIYsaFLRLPkevSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANP 1038
|
170
....*....|...
gi 1937413360 150 DFLILDEPFVGLD 162
Cdd:PLN03140 1039 SIIFMDEPTSGLD 1051
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-167 |
2.84e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 18 SLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTS-------GKISY--------NGTdinSNDNVLedFGIMIE 82
Cdd:PLN03130 632 TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasvvirGTVAYvpqvswifNAT---VRDNIL--FGSPFD 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 83 PVFYPEMSVIDNLKFYLKLHGKKELYSNIERTLKLvelwesrnrkpkgfSFGMKQRTALAIALVAEPDFLILDEPFVGLD 162
Cdd:PLN03130 707 PERYERAIDVTALQHDLDLLPGGDLTEIGERGVNI--------------SGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
....*.
gi 1937413360 163 P-VGVQ 167
Cdd:PLN03130 773 AhVGRQ 778
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-162 |
2.87e-06 |
|
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: 48.79 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 12 PGNDFYsLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGtdINSNDNVLED--FGIMI---EPVFY 86
Cdd:TIGR00957 1296 EDLDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIGLHDlrFKITIipqDPVLF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 87 PemsviDNLKFYLKLHGKkelYSNIE--RTLKLVELWESRNRKPKGFSF-----------GMKQRTALAIALVAEPDFLI 153
Cdd:TIGR00957 1373 S-----GSLRMNLDPFSQ---YSDEEvwWALELAHLKTFVSALPDKLDHecaeggenlsvGQRQLVCLARALLRKTKILV 1444
|
....*....
gi 1937413360 154 LDEPFVGLD 162
Cdd:TIGR00957 1445 LDEATAAVD 1453
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-50 |
2.92e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.51 E-value: 2.92e-06
10 20 30
....*....|....*....|....*....|..
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA 50
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALA 48
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-175 |
3.49e-06 |
|
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: 46.55 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKsqkpTSGKISYNGTdinsndnvledfgimiEPVFYPEMSV-IDNLKF 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLISF----------------LPKFSRNKLIfIDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 98 YLKLhgkkelysNIErTLKLvelwesrNRKPKGFSFGMKQRTALA--IALVAEPDFLILDEPFVGLDPVGVQKLIDILKK 175
Cdd:cd03238 71 LIDV--------GLG-YLTL-------GQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKG 134
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-162 |
8.06e-06 |
|
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: 47.25 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 18 SLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN-------SNDNVLED--FGIMIEPVFYpe 88
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYvpqqawiQNDSLRENilFGKALNEKYY-- 730
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 89 MSVIDNLKFYLKLhgkkELYSNIERTlklvELWEsrnrKPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLD 162
Cdd:TIGR00957 731 QQVLEACALLPDL----EILPSGDRT----EIGE----KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-212 |
8.91e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 46.44 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF--PGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKP----TSGKISYNGTD-------- 66
Cdd:COG4170 3 LLDIRNLTIEIdtPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDllklspre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 67 ----INSNdnvledfgI-MI--EPVFY--PEMSVIDNL-----------KFYLKLHGKKElysnieRTLKLVELWESRNR 126
Cdd:COG4170 83 rrkiIGRE--------IaMIfqEPSSCldPSAKIGDQLieaipswtfkgKWWQRFKWRKK------RAIELLHRVGIKDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 127 K------PKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNR 200
Cdd:COG4170 149 KdimnsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADT 228
|
250
....*....|..
gi 1937413360 201 YIYIEGGKLAES 212
Cdd:COG4170 229 ITVLYCGQTVES 240
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-157 |
9.03e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 6 NLSKKFPGNDfYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAksqkptsgkisynGTDINSNDNVLEDFGIMI---- 81
Cdd:PRK11819 11 RVSKVVPPKK-QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKEFEGEARPAPGIKVgylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 82 -EPVFYPEMSVIDNLKfyLKLHGKK-------ELYSN-----------IERTLKLVELWESRN---------------RK 127
Cdd:PRK11819 77 qEPQLDPEKTVRENVE--EGVAEVKaaldrfnEIYAAyaepdadfdalAAEQGELQEIIDAADawdldsqleiamdalRC 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937413360 128 PKG------FSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:PRK11819 155 PPWdakvtkLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-210 |
9.35e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENL-SKKFPgndfySLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDIN---SNDNVLED 76
Cdd:PRK10982 250 ILEVRNLtSLRQP-----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnANEAINHG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 77 FGIMIEPV----FYPEM-----SVIDNLKFYLklhGKKELYSNieRTLKLVELW--ESRNRKPKG-------FSFGMKQR 138
Cdd:PRK10982 325 FALVTEERrstgIYAYLdigfnSLISNIRNYK---NKVGLLDN--SRMKSDTQWviDSMRVKTPGhrtqigsLSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 139 TALAIALVAEPDFLILDEPFVGLDpVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGKLA 210
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGID-VGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-162 |
1.28e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.40 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 13 GNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSNDNVLEDFGIMIePVFYPEM--- 89
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRY-SVAYAAQkpw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 90 ----SVIDNLKFYLKLHgkKELYSNIERTLKL---VELWESRNRKPKG-----FSFGMKQRTALAIALVAEPDFLILDEP 157
Cdd:cd03290 90 llnaTVEENITFGSPFN--KQRYKAVTDACSLqpdIDLLPFGDQTEIGerginLSGGQRQRICVARALYQNTNIVFLDDP 167
|
....*
gi 1937413360 158 FVGLD 162
Cdd:cd03290 168 FSALD 172
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-212 |
1.42e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.95 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKF--PGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKP----TSGKISYNGTDIN--SNDN 72
Cdd:PRK15093 3 LLDIRNLTIEFktSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLrlSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 73 VLEDFGIMIEPVFYPEMSVID------------------NLKFYLKLHGKKElysnieRTLKLVELWESRNRK------P 128
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDpservgrqlmqnipgwtyKGRWWQRFGWRKR------RAIELLHRVGIKDHKdamrsfP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 129 KGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQLGELEALCNRYIYIEGGK 208
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
....
gi 1937413360 209 LAES 212
Cdd:PRK15093 237 TVET 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-171 |
1.96e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 57 SGKISYNGTDINsnDNVLED----FGIMI-EPVFYpEMSVIDNLKFylklhGKKE-LYSNIERTLKLV---ELWES---- 123
Cdd:PTZ00265 1276 SGKILLDGVDIC--DYNLKDlrnlFSIVSqEPMLF-NMSIYENIKF-----GKEDaTREDVKRACKFAaidEFIESlpnk 1347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 124 --RNRKP--KGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPvGVQKLID 171
Cdd:PTZ00265 1348 ydTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIE 1398
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
140-189 |
5.88e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.15 E-value: 5.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1937413360 140 ALAIALVA--EPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQIsmLISSH 189
Cdd:COG4637 268 ALLAALLSprPPPLLCIEEPENGLHPDLLPALAELLREASERTQV--IVTTH 317
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
138-205 |
7.41e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 7.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 138 RTALAIALVAEPDFLILDEPFVGLDPVGV-QKLIDILKKWSSERQISMLISSHQlGELEALCNRYIYIE 205
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKNFQLIVITHD-EELVDAADHIYRVE 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-191 |
9.16e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKI----SYNGTDIN-----SNDNVLEDfgimiEPVFYPEmSV 91
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindSHNLKDINlkwwrSKIGVVSQ-----DPLLFSN-SI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 92 IDNLKFylKLHGKKEL-------------------------------YSNIERTLKLVELWESRNR-------------- 126
Cdd:PTZ00265 477 KNNIKY--SLYSLKDLealsnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNELIEMRKNyqtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 127 ---------------------KPKGFSFGMKQRTALAIALVAEPDFLILDEPFVGLDPVG---VQKLIDILKkwSSERQI 182
Cdd:PTZ00265 555 kvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylVQKTINNLK--GNENRI 632
|
....*....
gi 1937413360 183 SMLIsSHQL 191
Cdd:PTZ00265 633 TIII-AHRL 640
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
25-189 |
1.91e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 25 EIEKGEIVGLIGKNGAGKSTLMKMMAKS---QKPTSGKISYNGTDINSNDNVLEdfgimiepvfypemsvidnLKFYLKL 101
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITYAlygKTPRYGRQENLRSVFAPGEDTAE-------------------VSFTFQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 102 HGKKelYsNIERTLKL--------VELWESR-----NRKPKGFSFGMKQRTALAIALV----------AEPDFLILDEPF 158
Cdd:cd03279 85 GGKK--Y-RVERSRGLdydqftriVLLPQGEfdrflARPVSTLSGGETFLASLSLALAlsevlqnrggARLEALFIDEGF 161
|
170 180 190
....*....|....*....|....*....|.
gi 1937413360 159 VGLDPVGVQKLIDILKKWSSERQiSMLISSH 189
Cdd:cd03279 162 GTLDPEALEAVATALELIRTENR-MVGVISH 191
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-163 |
1.91e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 19 LSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINSndnvledFGI--------MI--EPVFYpE 88
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA-------YGLrelrrqfsMIpqDPVLF-D 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 89 MSVIDNLKFYLKLhgkkelySNIE--RTLKLVELWESRNRKPKG-----------FSFGMKQRTALAIALVAE-PDFLIL 154
Cdd:PTZ00243 1398 GTVRQNVDPFLEA-------SSAEvwAALELVGLRERVASESEGidsrvleggsnYSVGQRQLMCMARALLKKgSGFILM 1470
|
....*....
gi 1937413360 155 DEPFVGLDP 163
Cdd:PTZ00243 1471 DEATANIDP 1479
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-204 |
2.72e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 123 SRNRKPKGFSFGMKQRTALAIALVAEPDFL--ILDEPFVGLDPVGVQKLIDILKKWSSERQISMLISSHQlgELEALCNR 200
Cdd:PRK00635 469 TPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDE--QMISLADR 546
|
....
gi 1937413360 201 YIYI 204
Cdd:PRK00635 547 IIDI 550
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
129-175 |
4.85e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 4.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1937413360 129 KGFSFGMKQRTALAIAL----VAEPDFLILDEPFVGLDPVGVQKLIDILKK 175
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-190 |
6.06e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 6.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937413360 118 VELWESRNRKPKGFSFGMK-Q-----RTALAIALVAEPDFLILDEPFVGLDPVGVQKLIDILKKWSSERQIsMLISSHQ 190
Cdd:COG4717 546 VDTEDGRTRPVEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQV-IYFTCHE 623
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
68-195 |
9.15e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 68 NSNDNVLEDFGIMIEPVFYPEMSvIDNLKFYLKLHGKKELYSNIERTLKLVELWESRNRKPK----GFSFGMKQRTALAI 143
Cdd:pfam13304 171 LAADLALFPDLKELLQRLVRGLK-LADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGElpafELSDGTKRLLALLA 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937413360 144 ALVA---EPDFLILDEPFVGLDPVGVQKLIDILKKWSSER-QIsmLISSHQLGELE 195
Cdd:pfam13304 250 ALLSalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGaQL--ILTTHSPLLLD 303
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-156 |
9.89e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.50 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 1 MLKIENLSKKFPGNDFYsLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMA--------KSQKPTSGKISY--------NG 64
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYvpqrpymtLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 65 TdinsndnvledfgiMIEPVFYPeMSVIDnlkFYLKLHGKKELysniERTLKLVEL---------WESRNRKPKGFSFGM 135
Cdd:TIGR00954 530 T--------------LRDQIIYP-DSSED---MKRRGLSDKDL----EQILDNVQLthilereggWSAVQDWMDVLSGGE 587
|
170 180
....*....|....*....|.
gi 1937413360 136 KQRTALAIALVAEPDFLILDE 156
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDE 608
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-206 |
1.11e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 21 DVSLEIEKGEIVGLIGKNGAGKSTL-MKMMAKSQ-KPTSGKISYNGTDINSND----------NVLED---FG-IMIEPV 84
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgRNISGTVFKDGKEVDVSTvsdaidaglaYVTEDrkgYGlNLIDDI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 85 FY-------PEMS---VIDNLK-------FYLKLHGKKelySNI-ERTLKLvelwesrnrkpkgfSFGMKQRTALAIALV 146
Cdd:NF040905 358 KRnitlanlGKVSrrgVIDENEeikvaeeYRKKMNIKT---PSVfQKVGNL--------------SGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937413360 147 AEPDFLILDEPFVGLDpVGVQKLI-DILKKWSSERQISMLISShQLGELEALCNRyIYI--EG 206
Cdd:NF040905 421 TDPDVLILDEPTRGID-VGAKYEIyTIINELAAEGKGVIVISS-ELPELLGMCDR-IYVmnEG 480
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-162 |
1.22e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.51 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENLSKKFPGNDFYSLSDVSLEIEKGEIVGLIGKNGAGKSTLMKMMAKSQKPTSGKISYNGTDINS------------ 69
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlplhtlrsrlsi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 70 --NDNVLedFGIMIEPVFYPEMSVIDN-LKFYLKLHGKKELYSNIERTLKLVELWESRNrkpkgFSFGMKQRTALAIALV 146
Cdd:cd03288 100 ilQDPIL--FSGSIRFNLDPECKCTDDrLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN-----FSVGQRQLFCLARAFV 172
|
170
....*....|....*.
gi 1937413360 147 AEPDFLILDEPFVGLD 162
Cdd:cd03288 173 RKSSILIMDEATASID 188
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-189 |
4.26e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.06 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 2 LKIENlskkfpgndFYSLSDVSLEIEKGeIVGLIGKNGAGKSTLMKMMAKSQKPTSG-KIS----YNGTDINSNDNVLE- 75
Cdd:COG3593 6 IKIKN---------FRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrKFDeedfYLGDDPDLPEIEIEl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937413360 76 ----DFGIMIEPVFYPEM----------------SVIDNL-----KFYLKLHGKKEL-----YSNIERTLKLVELWESRN 125
Cdd:COG3593 76 tfgsLLSRLLRLLLKEEDkeeleealeelneelkEALKALnellsEYLKELLDGLDLelelsLDELEDLLKSLSLRIEDG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937413360 126 RKPKGFSFGMKQRTALAIALV---------AEPDFLILDEPFVGLDPVGVQKLIDILKKWSSER-QIsmLISSH 189
Cdd:COG3593 156 KELPLDRLGSGFQRLILLALLsalaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPnQV--IITTH 227
|
|
| |
