|
Name |
Accession |
Description |
Interval |
E-value |
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-224 |
1.68e-131 |
|
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: 369.42 E-value: 1.68e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSIIEEPP 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 82 LYKNLSAYDNMKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGI 161
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 162 QELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYDGSENLEELFNNQIL 224
Cdd:TIGR03740 161 QELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINKSENLEKLFVEVVK 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
3.13e-92 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 270.40 E-value: 3.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRKIGSIIE 78
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKVVTTMLGVSEST----ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEarerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 155 GLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYDG--SENLEELF 219
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDElkARLLEDVF 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-206 |
3.67e-91 |
|
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: 266.78 E-value: 3.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR--RDLRKIGSIIEE 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKniEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDNMKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPI 159
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545668914 160 GIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:cd03268 161 GIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-203 |
1.81e-75 |
|
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: 225.35 E-value: 1.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL---RKIGSIIE 78
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEevkRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKvvttmlgvsestilpllnkvglgdidkrpvkqFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP 158
Cdd:cd03230 81 EPSLYENLTVRENLK--------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545668914 159 IGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:cd03230 129 ESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-219 |
2.21e-70 |
|
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: 215.11 E-value: 2.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRKIGSII 77
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPT 153
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKrieeLIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 154 NGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYD------GSENLEELF 219
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDelreeiGEENLEDAF 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-206 |
1.07e-67 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 209.96 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSIIEEP 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNlsaydnMKVVTTML------GVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:COG4152 81 GLYPK------MKVGEQLVylarlkGLSKAEAKRradeWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 151 EPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-229 |
6.93e-57 |
|
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: 182.59 E-value: 6.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 9 KSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR--RDLRK-IGSIIEEPPLYKN 85
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVRepRKVRRsIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 86 LSAYDNMKVVTTMLGVS----ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGI 161
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPkdeaEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 162 QELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEkeyDGSENLEELFNNQILFEKRR 229
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAE---GTPEELKRRLGKDTLESRPR 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-206 |
1.58e-56 |
|
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: 178.93 E-value: 1.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGkVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD---LRKIGSIIE 78
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqklRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKVVTTMLGVS----ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPskevKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545668914 155 GLDPIGIQELREIIESFkSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:cd03264 160 GLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-205 |
4.23e-55 |
|
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: 175.16 E-value: 4.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSIIEEPP 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 82 LYKNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRrideWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 158 PIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVL 205
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-194 |
4.54e-55 |
|
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: 174.97 E-value: 4.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL---RKIGSII 77
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdyrRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSAYDNMKVVTTMLGV--SESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLraDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 545668914 156 LDPIGIQELREIIESFKSEGMTIMISSHILSEVE-----HLADF 194
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAaarvlDLGDF 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-206 |
3.02e-54 |
|
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: 173.32 E-value: 3.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR--RDLRK-IGSIIEEP 80
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRepREVRRrIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAYDNMKVVTTMLGVSEST----ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGL 156
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAErrerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545668914 157 DPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-227 |
1.70e-52 |
|
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: 169.05 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL----RKIGSI 76
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPplyknlsayDNMKVVTT----------MLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLIN 142
Cdd:COG1122 81 FQNP---------DDQLFAPTveedvafgpeNLGLPREEIRErveeALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDGSenLEELFNNQ 222
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV----ADGT--PREVFSDY 225
|
....*
gi 545668914 223 ILFEK 227
Cdd:COG1122 226 ELLEE 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-206 |
1.97e-50 |
|
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: 163.83 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW---SRRDL----RKIGSI 76
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELyrlrRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMkvvttMLGVSESTILPL----------LNKVGL-GDIDKRPvKQFSLGMKQRLGIAISLINSPK 145
Cdd:cd03261 83 FQSGALFDSLTVFENV-----AFPLREHTRLSEeeireivlekLEAVGLrGAEDLYP-AELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 146 LLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-204 |
2.73e-50 |
|
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: 163.06 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGK--RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE--WSRRDLRK-IGSI 76
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirTDRKAARQsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIkeevELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545668914 153 TNGLDPIGIQELREIIESFKsEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
9.22e-50 |
|
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: 162.46 E-value: 9.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW---SRRDL----RKI 73
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELyelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPPLYKNLSAYDN----MKVVTTMlgvSESTILPL----LNKVGL-GDIDKRPvKQFSLGMKQRLGIAISLINSP 144
Cdd:COG1127 85 GMLFQGGALFDSLTVFENvafpLREHTDL---SEAEIRELvlekLELVGLpGAADKMP-SELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 145 KLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDGSenLEELFNNQ 222
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII----AEGT--PEELLASD 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-206 |
2.56e-49 |
|
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: 160.61 E-value: 2.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYG--KRTI--LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL---RKI 73
Cdd:cd03266 1 MITADALTKRFRdvKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAearRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPPLYKNLSAYDNMKVVTTMLGVSESTILPLLNKV----GLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELadrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-202 |
1.81e-48 |
|
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: 158.01 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 3 KIQNLKKSY--GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGSI 76
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdlTKLSLKELRRkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPplyknlsayDNMKVVTT----------MLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLIN 142
Cdd:cd03225 81 FQNP---------DDQFFGPTveeevafgleNLGLPEEEIEErveeALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGK 202
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-202 |
4.65e-48 |
|
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: 156.19 E-value: 4.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL------RKIGS 75
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelpplrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNmkvvttmlgvsesTILPLlnkvglgdidkrpvkqfSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:cd03229 81 VFQDFALFPHLTVLEN-------------IALGL-----------------SGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 156 LDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGK 202
Cdd:cd03229 131 LDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-202 |
2.13e-47 |
|
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: 153.55 E-value: 2.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 3 KIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKigsiieeppl 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 yknlsaydnmkvvttmlgvsestilpLLNKVGLgdidkrpVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQ 162
Cdd:cd00267 71 --------------------------LRRRIGY-------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 545668914 163 ELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGK 202
Cdd:cd00267 118 RLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-204 |
2.51e-47 |
|
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: 155.74 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY----GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLR----- 71
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 -------------------KIGSIIEEPPL-YKNLSAYDNMKVVttmlgvsestILPLLNKVGLGD--IDKRPVkQFSLG 129
Cdd:cd03257 81 rkeiqmvfqdpmsslnprmTIGEQIAEPLRiHGKLSKKEARKEA----------VLLLLVGVGLPEevLNRYPH-ELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 130 MKQRLGIAISLINSPKLLILDEPTNGLDP-----IgIQELREIIESFkseGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVsvqaqI-LDLLKKLQEEL---GLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
6.54e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 6.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREwSRRDLRKIG------ 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-PRRARRRIGyvpqra 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPPLyknlSAYDnmkVVttMLG-VSESTILPLLNK------------VGLGDIDKRPVKQFSLGMKQRLGIAISLI 141
Cdd:COG1121 85 EVDWDFPI----TVRD---VV--LMGrYGRRGLFRRPSRadreavdealerVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 142 NSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFI-----GFIYEGKIvleKEYDGSENLE 216
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVlllnrGLVAHGPP---EEVLTPENLS 232
|
...
gi 545668914 217 ELF 219
Cdd:COG1121 233 RAY 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-221 |
1.31e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 161.22 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKR-----TILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS------RRD 69
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 70 LRK------------------IGSIIEEPP-LYKNLSAYDNMKVVTTmlgvsestilpLLNKVGLGD--IDKRPvKQFSL 128
Cdd:COG1123 340 LRRrvqmvfqdpysslnprmtVGDIIAEPLrLHGLLSRAERRERVAE-----------LLERVGLPPdlADRYP-HELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 129 GMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVlek 207
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIV--- 484
|
250
....*....|....
gi 545668914 208 eYDGSenLEELFNN 221
Cdd:COG1123 485 -EDGP--TEEVFAN 495
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-204 |
2.41e-46 |
|
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: 152.67 E-value: 2.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRR--DLRKIGSIIEE 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIrarvRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545668914 156 LDPIGIQELR-EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03259 161 LDAKLREELReELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-204 |
2.74e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 152.90 E-value: 2.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS---RRDL----RK 72
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkRREIpylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 IGSIIEEPPLYKNLSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIrrrvREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-204 |
2.29e-45 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 150.79 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV-----SKTSGSIIFEGREWSRRDL------ 70
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKIGSIIEEPPLYkNLSAYDNMKVVTTMLGVSESTILP-----LLNKVGLGDIDKRPVKQFSL--GMKQRLGIAISLINS 143
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDerveeALRKAALWDEVKDRLHALGLsgGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 144 PKLLILDEPTNGLDPIGIQELREIIESFKSEgMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-206 |
3.12e-45 |
|
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: 150.67 E-value: 3.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGS------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 --IIEeppLYKNLSAYDNMkvvttMLGVSEST-------------------ILPLLNKVGLGDIDKRPVKQFSLGMKQRL 134
Cdd:cd03219 81 fqIPR---LFPELTVLENV-----MVAAQARTgsglllararreerearerAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 135 GIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-220 |
4.11e-45 |
|
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: 150.96 E-value: 4.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDL-RKIGSI 76
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaSLSRRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDnmkVVttMLG------------------VSEStilplLNKVGLGDIDKRPVKQFSLGMKQRLGIAI 138
Cdd:COG1120 81 PQEPPAPFGLTVRE---LV--ALGryphlglfgrpsaedreaVEEA-----LERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 139 SLINSPKLLILDEPTNGLDPIGIQELREIIESF-KSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDGS----- 212
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIV----AQGPpeevl 226
|
250
....*....|
gi 545668914 213 --ENLEELFN 220
Cdd:COG1120 227 tpELLEEVYG 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-221 |
3.36e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.22 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE--WSRRDL----RKIG 74
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltDSKKDInklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPPLYKNLSAYDN-----MKVvttmLGVS----ESTILPLLNKVGLGD-IDKRPvKQFSLGMKQRLGIAISLINSP 144
Cdd:COG1126 81 MVFQQFNLFPHLTVLENvtlapIKV----KKMSkaeaEERAMELLERVGLADkADAYP-AQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 145 KLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlEkeyDGSEnlEELFNN 221
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIV-E---EGPP--EEFFEN 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-222 |
5.32e-44 |
|
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: 147.30 E-value: 5.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS-----RRDLRKIGSI 76
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEkleeLLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 153 TNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKeydgseNLEELFNNQ 222
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEG------TPEEIAANE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-193 |
6.06e-44 |
|
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: 146.52 E-value: 6.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 3 KIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREwSRRDLRKIGSI--IEEP 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-LEKERKRIGYVpqRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAYDnmkVVTTML--------GVSEST---ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:cd03235 80 DRDFPISVRD---VVLMGLyghkglfrRLSKADkakVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLAD 193
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFD 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-154 |
8.33e-44 |
|
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: 144.33 E-value: 8.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL----RKIGSIIEEPPLYKNLSAYDNM 92
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkslrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 93 KVVTTMLGVS----ESTILPLLNKVGLGDIDKRPV----KQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:pfam00005 81 RLGLLLKGLSkrekDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-203 |
8.56e-44 |
|
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: 146.48 E-value: 8.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYG----KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDL---- 70
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiskLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 -RKIGSIIEEPPLYKNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPK 145
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERREraeeLLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 146 LLILDEPTNGLDPIGIQELREIIESF-KSEGMTIMISSHILsEVEHLADFIGFIYEGKI 203
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-212 |
6.45e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.20 E-value: 6.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRK---- 72
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 IGSIIEEPPLYKNLSAYDN--------MKVVTTMLG-VSESTI---LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISL 140
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGlFPPEDReraLEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 141 INSPKLLILDEPTNGLDPIGIQE----LREIIEsfkSEGMTIMISSHILSEVEHLAD-FIGfIYEGKIVlekeYDGS 212
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQvmdlLRRIAR---EDGITVVVNLHQVDLARRYADrIIG-LRDGRVV----FDGP 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-206 |
9.50e-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: 144.80 E-value: 9.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGS----- 75
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARlgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 ---IIEeppLYKNLSAYDNMKVV------TTMLGVSESTILP-------------LLNKVGLGDIDKRPVKQFSLGMKQR 133
Cdd:COG0411 84 tfqNPR---LFPELTVLENVLVAaharlgRGLLAALLRLPRArreereareraeeLLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 134 LGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-203 |
2.12e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.65 E-value: 2.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL----RKIGSII 77
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNlSAYDNMKVVTTM--LGVSESTILPLLNKVGLGDID-KRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLreRKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545668914 155 GLDPigiqELREIIES-----FKSEGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:COG4619 160 ALDP----ENTRRVEEllreyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-206 |
2.18e-42 |
|
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: 142.96 E-value: 2.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGSI 76
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTMLGVSEST-----ILPLLNKvgLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKarlerVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 152 PTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFiGFIYE-GKIVLE 206
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADR-AYVLErGRVVLE 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-206 |
2.92e-42 |
|
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: 140.64 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRKIGsiie 78
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEvsfASPRDARRAG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 epplyknlsaydnmkvvttmlgvsestilpllnkVGLgdidkrpVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP 158
Cdd:cd03216 77 ----------------------------------IAM-------VYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 159 IGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-206 |
6.55e-42 |
|
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: 148.51 E-value: 6.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY--GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKT---SGSIIFEGREWSRRDL----R 71
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEalrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 KIGSIIEEPPLYKN-LSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKL 146
Cdd:COG1123 84 RIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEArarvLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 147 LILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-217 |
4.19e-41 |
|
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: 140.40 E-value: 4.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYG-KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLR----KI 73
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdiNKLKGKALRqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPPLYKNLSAYDNmkVVTTMLG-----------VSESTI---LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAIS 139
Cdd:cd03256 81 GMIFQQFNLIERLSVLEN--VLSGRLGrrstwrslfglFPKEEKqraLAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 140 LINSPKLLILDEPTNGLDPIGIQELREIIESF-KSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDG-SENLEE 217
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIV----FDGpPAELTD 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-203 |
7.30e-41 |
|
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: 138.82 E-value: 7.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW--SRRDL----RKIGS 75
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNInelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDN-MKVVTTMLGVS----ESTILPLLNKVGLGD-IDKRPvKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:cd03262 81 VFQQFNLFPHLTVLENiTLAPIKVKGMSkaeaEERALELLEKVGLADkADAYP-AQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-221 |
8.62e-41 |
|
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: 141.73 E-value: 8.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY----GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSK---TSGSIIFEGRE---WSRRDL 70
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllkLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RK----------------------IGSIIEEPPLY-KNLSAYDNMKVVTTMLgvsestilpllNKVGLGD----IDKRPV 123
Cdd:COG0444 81 RKirgreiqmifqdpmtslnpvmtVGDQIAEPLRIhGGLSKAEARERAIELL-----------ERVGLPDperrLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 124 kQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIgIQ-----ELREIIESFkseGMTIMISSHILSEVEHLADFIGFI 198
Cdd:COG0444 150 -ELSGGMRQRVMIARALALEPKLLIADEPTTALDVT-IQaqilnLLKDLQREL---GLAILFITHDLGVVAEIADRVAVM 224
|
250 260
....*....|....*....|...
gi 545668914 199 YEGKIVlekEYDGSenlEELFNN 221
Cdd:COG0444 225 YAGRIV---EEGPV---EELFEN 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-204 |
1.39e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 136.80 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 3 KIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDL-RKIGsiie 78
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaSLSPKELaRKIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 epplyknlsaydnmkvvttmlgvsestILP-LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:cd03214 77 ---------------------------YVPqALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 158 PIGIQELREIIESF-KSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03214 130 IAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-193 |
2.67e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.01 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGS 75
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaagIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNMkvvttMLGvSESTILP-------------LLNKVGLgDID-KRPVKQFSLGMKQRLGIAISLI 141
Cdd:COG1129 84 IHQELNLVPNLSVAENI-----FLG-REPRRGGlidwramrrrareLLARLGL-DIDpDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545668914 142 NSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLAD 193
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIAD 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-206 |
4.30e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 137.47 E-value: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS-----RRDLRKIGS 75
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmhKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREErleeLLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 152 PTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-206 |
8.16e-40 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 137.02 E-value: 8.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS-----RRDLRKIGSI 76
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlpmhERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTMLG-----VSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKdldraEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 152 PTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAE 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-193 |
1.33e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY----GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDlRKIGSI 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-PDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTMLGVS----ESTILPLLNKVGLGD-IDKRPvKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:COG1116 86 FQEPALLPWLTVLDNVALGLELRGVPkaerRERARELLELVGLAGfEDAYP-HQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 545668914 152 PTNGLDPIGIQELREIIES-FKSEGMTIMISSHILSEVEHLAD 193
Cdd:COG1116 165 PFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLAD 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-204 |
5.72e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 5.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYG----KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDL--- 70
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDissLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 --RKIGSIIEEPPLYKNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGD-IDKRPvKQFSLGMKQRLGIAISLINS 143
Cdd:COG1136 84 rrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRErareLLERVGLGDrLDHRP-SQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 144 PKLLILDEPTNGLDPigiQELREIIESFKS----EGMTIMISSHILsEVEHLADFIGFIYEGKIV 204
Cdd:COG1136 163 PKLILADEPTGNLDS---KTGEEVLELLRElnreLGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-193 |
1.52e-38 |
|
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: 132.98 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKR----TILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDlRKIGSII 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-PDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDI-DKRPvKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAEAreraEELLELVGLSGFeNAYP-HQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 545668914 153 TNGLDPIGIQELR-EIIESFKSEGMTIMISSHILSEVEHLAD 193
Cdd:cd03293 159 FSALDALTREQLQeELLDIWRETGKTVLLVTHDIDEAVFLAD 200
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-183 |
2.44e-38 |
|
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: 131.39 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 16 ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE--WSRRDL----RKIGSIIEEPplyknlsay 89
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPldYSRKGLlerrQRVGLVFQDP--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 90 DNMKVVTTM----------LGVSE----STILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:TIGR01166 78 DDQLFAADVdqdvafgplnLGLSEaeveRRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180
....*....|....*....|....*...
gi 545668914 156 LDPIGIQELREIIESFKSEGMTIMISSH 183
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-211 |
5.25e-38 |
|
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: 132.07 E-value: 5.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 8 KKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG-REWSRRD--LRKIGSII-EEPPLY 83
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKkfLRRIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 84 KNLSAYDNMKVVTTMLGVSES----TILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPI 159
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPArfkkRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545668914 160 GIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDG 211
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL----YDG 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-206 |
5.94e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 133.78 E-value: 5.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDLRKIGSIie 78
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpSRARHARQRVGVV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 epPLYKNL----SAYDNMKVVTTMLGVSESTIL----PLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:PRK13537 86 --PQFDNLdpdfTVRENLLVFGRYFGLSAAAARalvpPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 151 EPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-193 |
6.84e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.47 E-value: 6.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRK--IGS 75
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvriRSPRDAIAlgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNMkvvttMLGvSESTILPLLN-------------KVGLgDID-KRPVKQFSLGMKQRLGIAISLI 141
Cdd:COG3845 85 VHQHFMLVPNLTVAENI-----VLG-LEPTKGGRLDrkaararirelseRYGL-DVDpDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545668914 142 NSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLAD 193
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIAD 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-219 |
6.92e-38 |
|
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: 132.13 E-value: 6.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGS--IIFeGRE---WSRRDLRK-IG 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLF-GERrggEDVWELRKrIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 ----SIIEEPPlyKNLSAYDnmkVVTTmlGVSESTILP-------------LLNKVGLGDIDKRPVKQFSLGMKQRLGIA 137
Cdd:COG1119 82 lvspALQLRFP--RDETVLD---VVLS--GFFDSIGLYreptdeqrerareLLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 138 ISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMT--IMISSH---ILSEVEHLADFIgfiyEGKIVlekeYDG- 211
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtlVLVTHHveeIPPGITHVLLLK----DGRVV----AAGp 226
|
250
....*....|....
gi 545668914 212 ------SENLEELF 219
Cdd:COG1119 227 keevltSENLSEAF 240
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-221 |
1.83e-37 |
|
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: 130.39 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYG----KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRK- 72
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 ---IGSIIEEPPLYKNLSAYDNMKVVTTMLGVS----ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPK 145
Cdd:cd03258 81 rrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPkaeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 146 LLILDEPTNGLDPIGIQE----LREIIESFkseGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEydgsenLEELFNN 221
Cdd:cd03258 161 VLLCDEATSALDPETTQSilalLRDINREL---GLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT------VEEVFAN 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-229 |
2.31e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 132.52 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-------------------GKRTI--LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSII 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalkglfrrEYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 60 FEGRE-WSRRD--LRKIGSII-EEPPLYKNLSAYDNMKVVTTMLGVSESTILPLLNKV----GLGDIDKRPVKQFSLGMK 131
Cdd:COG4586 81 VLGYVpFKRRKefARRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELvellDLGELLDTPVRQLSLGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 132 QRLGIAISLINSPKLLILDEPTNGLDPIGIQELRE-IIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYD 210
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREfLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII----YD 236
|
250
....*....|....*....
gi 545668914 211 GSenLEELFNNqilFEKRR 229
Cdd:COG4586 237 GS--LEELKER---FGPYK 250
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-204 |
3.20e-36 |
|
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: 127.80 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGK-RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL----RKIGSI 76
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvelrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDI---DKRPvKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIreraDELLALVGLDPAefaDRYP-HELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-214 |
8.60e-36 |
|
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: 126.64 E-value: 8.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGK-RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRK---- 72
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitkLRGKKLRKlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 IGSIIEEPPLYKNLSAYDN--------MKVVTTMLG-VSESTI---LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISL 140
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENvlhgrlgyKPTWRSLLGrFSEEDKeraLSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 141 INSPKLLILDEPTNGLDP----IGIQELREIIesfKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDGSEN 214
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPktskQVMDYLKRIN---KEDGITVIINLHQVDLAKKYADRIVGLKAGEIV----FDGAPS 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-204 |
1.10e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.06 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRR--DLRKIGSIIE 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNmkvVT---TMLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:COG3842 85 DYALFPHLTVAEN---VAfglRMRGVPKAEIRArvaeLLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545668914 152 PTNGLDPIGIQELR-EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:COG3842 162 PLSALDAKLREEMReELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-206 |
2.58e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 127.64 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 6 NLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRKIGSIIEEPPL 82
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvpaRARLARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 YKNLSAYDNMKVVTTMLGVS----ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP 158
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMStreiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 159 IGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK13536 206 HARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-204 |
2.85e-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: 124.29 E-value: 2.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKRT-ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSIIEEPPL 82
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 YkNL---SAYDNMKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPI 159
Cdd:cd03226 82 Y-QLftdSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545668914 160 GIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-206 |
5.30e-35 |
|
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: 124.32 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGS 75
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNMKvvttmlgvsestiLPLLNKVGLGDIDKRPVKQFSL-----------------GMKQRLGIAI 138
Cdd:COG0410 83 VPEGRRIFPSLTVEENLL-------------LGAYARRDRAEVRADLERVYELfprlkerrrqragtlsgGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 139 SLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-227 |
1.92e-34 |
|
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: 124.10 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGK-----RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR------EWSRRDL 70
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditakkKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 R-KIG--------SIIEEpplyknlSAYDNMKVVTTMLGVSESTIL----PLLNKVGLGD--IDKRPvkqFSL--GMKQR 133
Cdd:TIGR04521 81 RkKVGlvfqfpehQLFEE-------TVYKDIAFGPKNLGLSEEEAEervkEALELVGLDEeyLERSP---FELsgGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 134 LGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESF-KSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLekeyDGS 212
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVL----DGT 226
|
250
....*....|....*
gi 545668914 213 EnlEELFNNQILFEK 227
Cdd:TIGR04521 227 P--REVFSDVDELEK 239
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-204 |
3.23e-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: 122.35 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL--RKIGSIIEE 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPhkRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIkervAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545668914 156 LDPIGIQELR-EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03300 161 LDLKLRKDMQlELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-201 |
9.09e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 126.72 E-value: 9.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFegrewsRRDLRkIGSIIEEPPLY 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------PKGLR-IGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 84 KNLSAYDN--------MKVVTTMLGVS----------------------------ESTILPLLNKVGLGDID-KRPVKQF 126
Cdd:COG0488 74 DDLTVLDTvldgdaelRALEAELEELEaklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEDlDRPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 127 SLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKseGMTIMIS----------SHILseveHLADFIG 196
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP--GTVLVVShdryfldrvaTRIL----ELDRGKL 227
|
....*
gi 545668914 197 FIYEG 201
Cdd:COG0488 228 TLYPG 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-206 |
1.15e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 121.77 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY--GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD-----LRKIG 74
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweiRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPplyknlsayDNMKVVTTM----------LGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISL 140
Cdd:TIGR04520 81 MVFQNP---------DNQFVGATVeddvafglenLGVPREEMRKrvdeALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 141 INSPKLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVeHLADFIGFIYEGKIVLE 206
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEA-VLADRVIVMNKGKIVAE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-202 |
1.25e-33 |
|
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: 118.64 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYG--KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGS 75
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLRKnIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYkNLSAYDNmkvvttmlgvsestILpllnkvglgdidkrpvkqfSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:cd03228 81 VPQDPFLF-SGTIREN--------------IL-------------------SGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545668914 156 LDPIGIQELREIIESFKSEGMTIMIsSHILSEVEHlADFIGFIYEGK 202
Cdd:cd03228 127 LDPETEALILEALRALAKGKTVIVI-AHRLSTIRD-ADRIIVLDDGR 171
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-204 |
2.31e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 122.49 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY----GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLR-- 71
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 --KIGSIIEEPPLYKNLSAYDN----MKVvttmLGVSESTI----LPLLNKVGLGD-IDKRPvKQFSLGMKQRLGIAISL 140
Cdd:COG1135 81 rrKIGMIFQHFNLLSSRTVAENvalpLEI----AGVPKAEIrkrvAELLELVGLSDkADAYP-SQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 141 INSPKLLILDEPTNGLDPIGIQE----LREIIESFkseGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSildlLKDINREL---GLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-221 |
3.28e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.81 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW--SRRDLRKI----G 74
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPPLYKNLSAYDNM-----KVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVmfgplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDGseNLEELFNN 221
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA----EDG--DPQVLIKN 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-204 |
9.74e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 9.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 8 KKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRewsrrdlrkIGSIIE-----EPpl 82
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VSALLElgagfHP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 ykNLSAYDNMKVVTTMLGVSESTILPLLNKV----GLGD-IDkRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:COG1134 102 --ELTGRENIYLNGRLLGLSRKEIDEKFDEIvefaELGDfID-QPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545668914 158 PIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:COG1134 179 AAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
1.08e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.57 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRT-ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR--EWSRR---DLRKIG 74
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPPLYKNLSA--YDNMKVVTTMLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK13636 85 GMVFQDPDNQLFSAsvYQDVSFGAVNLKLPEDEVRKrvdnALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-203 |
1.36e-32 |
|
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: 118.21 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL--RKIGSIIEE 79
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqeRNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDN----MKVVTTMLGVSESTI----LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:cd03296 83 YALFRHMTVFDNvafgLRVKPRSERPPEAEIrakvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545668914 152 PTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-203 |
5.81e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 119.03 E-value: 5.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR---RDlRKIGSIIE 78
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhaRD-RKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKVVTTMLGVSE--------STILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRRErpnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545668914 151 EPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-183 |
1.11e-31 |
|
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: 115.20 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 5 QNLKKSYGKRTI-LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS---RRDL----RKIGSI 76
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrGRAIpylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIrkrvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|.
gi 545668914 153 TNGLDPIGIQELREIIESFKSEGMTIMISSH 183
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-204 |
2.91e-31 |
|
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: 120.71 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRT--ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGS 75
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASLRRqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYkNLSAYDNMKVvtTMLGVSESTILPLLNKVGLGD-IDKRP----------VKQFSLGMKQRLGIAISLINSP 144
Cdd:COG2274 554 VLQDVFLF-SGTIRENITL--GDPDATDEEIIEAARLAGLHDfIEALPmgydtvvgegGSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 145 KLLILDEPTNGLDPigiQELREIIESFKS--EGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:COG2274 631 RILILDEATSALDA---ETEAIILENLRRllKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIV 688
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-204 |
1.12e-30 |
|
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: 112.39 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 26 KGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW--SRRDL------RKIGSIIEEPPLYKNLSAYDNMKVVTT 97
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKInlppqqRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 98 MLGVSESTILP--LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP----IGIQELREIIESF 171
Cdd:cd03297 102 RKRNREDRISVdeLLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRalrlQLLPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|...
gi 545668914 172 KsegMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03297 182 N---IPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-204 |
1.47e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.08 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV-----SKTSGSIIFEGREWSRRDL----RK 72
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVielrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 IGSIIEEPPLYKNLSAYDNMKVVTTMLGVSEST------ILPLLNKVGLGDIDKR----PVKQFSLGMKQRLGIAISLIN 142
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKkelqerVRWALEKAQLWDEVKDrldaPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSEgMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-204 |
2.15e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR---RDlRKIGSII 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlppKD-RNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSAYDNM----KvvttMLGVSESTILPLLNKV----GLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:COG3839 82 QSYALYPHMTVYENIafplK----LRKVPKAEIDRRVREAaellGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 150 DEPTNGLDPigiqELR-----EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:COG3839 158 DEPLSNLDA----KLRvemraEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-204 |
2.39e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.51 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY--GKRTI--LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDL--- 70
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 -RKIGSIIEEPPLYKNLSAYDNMKVVTTMLGVSESTI----LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPK 145
Cdd:PRK11153 81 rRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIkarvTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 146 LLILDEPTNGLDP-----IgIQELREIIESFkseGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK11153 161 VLLCDEATSALDPattrsI-LELLKDINREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-204 |
2.48e-30 |
|
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: 117.56 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY--GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGS 75
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlRDLDEDDLRRrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYkNLSAYDNMKVVTtmLGVSESTILPLLNKVGLGD-IDKRPVK----------QFSLGMKQRLGIAISLINSP 144
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLAR--PDATDEELWAALERVGLGDwLAALPDGldtwlgeggrRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 145 KLLILDEPTNGLDPIGIQE-LREIIESFKseGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:COG4987 491 PILLLDEPTEGLDAATEQAlLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIV 548
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
2.55e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRT-ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE--WSRRDL----RKI 73
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikYDKKSLlevrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEP------PLYKNLSAYDNMKVVTTMLGVsESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLL 147
Cdd:PRK13639 81 GIVFQNPddqlfaPTVEEDVAFGPLNLGLSKEEV-EKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 148 ILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-221 |
4.15e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.05 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV-----SKTSGSIIFEGREWSRRDL------ 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDIYDPDVdvvelr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKIGSIIEEP-PLYKnlSAYDNMKVVTTMLGVSESTILP-----LLNKVGL----GDIDKRPVKQFSLGMKQRLGIAISL 140
Cdd:COG1117 92 RRVGMVFQKPnPFPK--SIYDNVAYGLRLHGIKSKSELDeiveeSLRKAALwdevKDRLKKSALGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 141 INSPKLLILDEPTNGLDPIGIQELREIIESFKSEgMTIMISSHILSEVEHLADFIGFIYEGKIVlekEYDgseNLEELFN 220
Cdd:COG1117 170 AVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV---EFG---PTEQIFT 242
|
.
gi 545668914 221 N 221
Cdd:COG1117 243 N 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-204 |
1.18e-29 |
|
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: 115.17 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGK----RTILNNVNMNIPKGKVYALIGPNGAGKS----TIMKILTGLVSKTSGSIIFEGRE---WSRRD 69
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllgLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 70 LRK-----IGSIIEEP-----PLY---KNLsaydnMKVVTTMLGVS----ESTILPLLNKVGLGDiDKRPVK----QFSL 128
Cdd:COG4172 86 LRRirgnrIAMIFQEPmtslnPLHtigKQI-----AEVLRLHRGLSgaaaRARALELLERVGIPD-PERRLDayphQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 129 GMKQRLGIAISLINSPKLLILDEPTNGLDpIGIQelREIIESFKS----EGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALD-VTVQ--AQILDLLKDlqreLGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-204 |
1.21e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.89 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL--RKIGSIIEE 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIqqRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDNMKVVTTMLGVSESTI-------LPLLNKVGLGDidkRPVKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERkqrvkeaLELVDLAGFED---RYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545668914 153 TNGLDPIGIQELREII-ESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK11432 164 LSNLDANLRRSMREKIrELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-204 |
1.68e-29 |
|
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: 109.27 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDlRKIGSIIE 78
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKD-RDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKVVTTMLGVSESTILPLLNKVG-LGDIDK---RPVKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAeLLQIEHlldRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545668914 155 GLDPIGIQELR-EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03301 160 NLDAKLRVQMRaELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
2.56e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.66 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR---RDLRKIGSI 76
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeniREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVV--TTMLGVSESTIL----PLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQDIAfgPINLGLDEETVAhrvsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 151 EPTNGLDPIGIQELREIIESF-KSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeydGSENLEELFNNQILFEKRR 229
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV------AYGTVEEIFLQPDLLARVH 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-218 |
4.58e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.38 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIfEGR---EWSRRDLRKIgsiIE 78
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTaplAEAREDTRLM---FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKvvttmLGVS---ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:PRK11247 89 DARLLPWKKVIDNVG-----LGLKgqwRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 156 LDPIGIQELREIIES-FKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYD-------GSENLEEL 218
Cdd:PRK11247 164 LDALTRIEMQDLIESlWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDlprprrrGSARLAEL 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-204 |
4.71e-29 |
|
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: 108.39 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRewsrrdlrkIGSIIE-- 78
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------VSSLLGlg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 ---EPplykNLSAYDNMKVVTTMLGVSESTILPLLNKV----GLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:cd03220 93 ggfNP----ELTGRENIYLNGRLLGLSRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545668914 152 PTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-204 |
5.99e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.83 E-value: 5.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS-----RRDLRKIGSI 76
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTMLG--------------VSESTILPLLNKVGlgdidkrpvKQFSLGMKQRLGIAISLIN 142
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDdlsaeqredranelMEEFHIEHLRDSMG---------QSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-204 |
6.01e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.37 E-value: 6.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 14 RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVS------KTSGSIIFEGREWSRRD---LRK-IGSIIEEPPLY 83
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDaikLRKeVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 84 KNLSAYDNMKVVTTMLGVSES-----TILPLLNKVGLG----DIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKreikkIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545668914 155 GLDPIGIQELREIIESFKSEgMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-204 |
1.01e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 112.93 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGSI 76
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlSDLDPASWRRqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKnLSAYDNMkvvttMLG---VSESTILPLLNKVGLGD-IDKRPV----------KQFSLGMKQRLGIAISLIN 142
Cdd:COG4988 417 PQNPYLFA-GTIRENL-----RLGrpdASDEELEAALEAAGLDEfVAALPDgldtplgeggRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFkSEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIV 550
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-191 |
1.35e-28 |
|
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: 106.67 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR-RDL--RKIGSIIE 78
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqRDEphENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP 158
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 545668914 159 IGIQELREIIESFKSEGMTIMISSHI---LSEVEHL 191
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQdlgLVEAREL 196
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-220 |
1.65e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.15 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTIlnNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRR--DLRKIGSIIE 78
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKvvttmLGVS---------ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:COG3840 79 ENNLFPHLTVAQNIG-----LGLRpglkltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDGSenLEELFN 220
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIA----ADGP--TAALLD 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-188 |
2.41e-28 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 107.51 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIfegrewsRRDLRKIGSIieep 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRIGYV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAYDNMKVVTTML---GVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:PRK09544 73 PQKLYLDTTLPLTVNRFLRlrpGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190
....*....|....*....|....*....|..
gi 545668914 158 PIGIQELREIIESFKSE-GMTIMISSHILSEV 188
Cdd:PRK09544 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLV 184
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-206 |
2.52e-28 |
|
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: 106.07 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGL--VSKTSGSIIFEGR-----EWSRRDLRKIG 74
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditdlPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPPlyknlsaydnmkvvtTMLGVsesTILPLLNKVGLGdidkrpvkqFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:cd03217 81 LAFQYPP---------------EIPGV---KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 155 GLDPIGIQELREIIESFKSEGMTIMISSH---ILSEVEhlADFIGFIYEGKIVLE 206
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITHyqrLLDYIK--PDRVHVLYDGRIVKS 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-219 |
2.83e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.14 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 5 QNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL---RKIG------S 75
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIatrRRVGymsqafS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 iieeppLYKNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGD-IDKRPvKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:NF033858 350 ------LYGELTVRQNLELHARLFHLPAAEIAArvaeMLERFDLADvADALP-DSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 151 EPTNGLDPIGIQEL-REIIESFKSEGMTIMISSHILSEVEhLADFIGFIYEGKiVLE-------KEYDGSENLEELF 219
Cdd:NF033858 423 EPTSGVDPVARDMFwRLLIELSREDGVTIFISTHFMNEAE-RCDRISLMHAGR-VLAsdtpaalVAARGAATLEEAF 497
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-183 |
3.23e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 106.50 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR---RDL----RK 72
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknREVpflrRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 IGSIIEEPPLYKNLSAYDNMKVVTTMLGVSESTIL----PLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRrrvsAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFKSEGMTIMISSH 183
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-204 |
4.30e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.64 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG--------REWSRR---- 68
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssRQLARRlall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 69 ----------DLRKIGSIIEEP--PLYKNLSAYDNMKVVTTMlgvsestilpllNKVGLGDIDKRPVKQFSLGMKQRLGI 136
Cdd:PRK11231 82 pqhhltpegiTVRELVAYGRSPwlSLWGRLSAEDNARVNQAM------------EQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 137 AISLINSPKLLILDEPTNGLDpIGIQ-ELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD-INHQvELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-204 |
7.91e-28 |
|
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: 106.57 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 7 LKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLR-----KIGSIIE 78
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaaMSRKELRelrrkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKVVTTMLGVSEST----ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEreerAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545668914 155 GLDPIGIQELR-EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03294 190 ALDPLIRREMQdELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-204 |
1.31e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.15 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGL----VskTSGSIIFEGR---EWS-------- 66
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkyeV--TSGSILLDGEdilELSpderarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 67 ----------------RRDLRKIGSIIEEPPlyknLSAYDNMKVVTTmlgvsestilpLLNKVGLG-DIDKRPVKQ-FSL 128
Cdd:COG0396 79 iflafqypveipgvsvSNFLRTALNARRGEE----LSAREFLKLLKE-----------KMKELGLDeDFLDRYVNEgFSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 129 GMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSH---ILSEVEhlADFIGFIYEGKIV 204
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrILDYIK--PDFVHVLVDGRIV 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-183 |
1.35e-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: 102.53 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIifegrEWSRRdlrkigsiieepp 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----TWGST------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 82 lyknlsaydnmkvvttmlgvsestilpllNKVGLgdidkrpVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGI 161
Cdd:cd03221 63 -----------------------------VKIGY-------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180
....*....|....*....|..
gi 545668914 162 QELREIIESFKSegmTIMISSH 183
Cdd:cd03221 107 EALEEALKEYPG---TVILVSH 125
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-195 |
1.65e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 105.20 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD-----LRKIGS 75
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDeheiaRLGIGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNM--------KVVTTML----GVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINS 143
Cdd:COG4674 90 KFQKPTVFEELTVFENLelalkgdrGVFASLFarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545668914 144 PKLLILDEPTNGLDPigiQELREIIESFKS--EGMTIMIsshilseVEHLADFI 195
Cdd:COG4674 170 PKLLLLDEPVAGMTD---AETERTAELLKSlaGKHSVVV-------VEHDMEFV 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-224 |
2.09e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.86 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGL--VSKTSGSIIFEGREWSRRDLRK-----I 73
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDteragI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPPLYKNLSAYDNMkvvttMLGvseSTILP---------------LLNKVGLgDID-KRPVKQFSLGMKQRLGIA 137
Cdd:PRK13549 85 AIIHQELALVKELSVLENI-----FLG---NEITPggimdydamylraqkLLAQLKL-DINpATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 138 ISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeydGSENLEE 217
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI------GTRPAAG 229
|
....*..
gi 545668914 218 LFNNQIL 224
Cdd:PRK13549 230 MTEDDII 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-206 |
2.47e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.58 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EW-SRRDLRKIGSI 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditDWqTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEE-PPLYKNLSAYDNMkvvtTMLG--VSESTILPLLNKV-----GLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK11614 85 VPEgRRVFSRMTVEENL----AMGGffAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFiGFIYE-GKIVLE 206
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR-GYVLEnGHVVLE 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
4.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 104.69 E-value: 4.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYG--KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLR----KIG 74
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeirkKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPplyknlsayDNMKVVTT------------MLGVSE--STILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISL 140
Cdd:PRK13632 87 IIFQNP---------DNQFIGATveddiafglenkKVPPKKmkDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 141 INSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMIS-SHILSEVEhLADFIGFIYEGKIV 204
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLI 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-204 |
4.59e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.95 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLR-----KIGS 75
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaqlGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNMKV----VTTMLGVS-------ESTILPLLNKVGLG-DIDKRpVKQFSLGMKQRLGIAISLINS 143
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIgrhlTKKVCGVNiidwremRVRAAMMLLRVGLKvDLDEK-VANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 144 PKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-204 |
4.59e-27 |
|
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: 102.96 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 24 IPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL--RKIGSIIEEPPLYKNLSAYDNMKvvttmLGV 101
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPadRPVSMLFQENNLFAHLTVEQNVG-----LGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 102 SES---------TILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREII-ESF 171
Cdd:cd03298 96 SPGlkltaedrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVlDLH 175
|
170 180 190
....*....|....*....|....*....|...
gi 545668914 172 KSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-204 |
8.74e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.38 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV-----SKTSGSIIFEGREWSRRDL------ 70
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVdpievr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKIGSIIEEPPLYKNLSAYDNMKVVTTMLGVSEST------ILPLLNKVGLGDIDKRPVK----QFSLGMKQRLGIAISL 140
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKkelderVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 141 INSPKLLILDEPTNGLDPIGIQELREIIESFKSEgMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
1.30e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.19 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLvSKTSGSIIFEGRE-------WSRR----DL 70
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVeffnqniYERRvnlnRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKIGSIIEEPPLYKNLSAYDNMKVVTTMLGVSESTILPLLNKVGLGDID---------KRPVKQFSLGMKQRLGIAISLI 141
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADlwdeikhkiHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 142 NSPKLLILDEPTNGLDPIGIQELREIIES--FKSEgMTIMISSHILSEVEHLADFIGFIY--EGKIVLEKEYdGSENleE 217
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSE-LTMVIVSHNLHQVSRLSDFTAFFKgnENRIGQLVEF-GLTK--K 242
|
....
gi 545668914 218 LFNN 221
Cdd:PRK14258 243 IFNS 246
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-204 |
1.31e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 106.41 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTS--GSIIFEGREWSRRDLR---KIGS 75
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRdseALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 II--EEPPLYKNLSAYDNM---------KVV---TTMLGVSEstilpLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLI 141
Cdd:NF040905 81 VIihQELALIPYLSIAENIflgnerakrGVIdwnETNRRARE-----LLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 142 NSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-206 |
1.62e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDL----RKI 73
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLytvrKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPPLYKNLSAYDNMKVVT---TML--GVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLrehTQLpaPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-219 |
2.00e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 106.75 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSI-IFEGREWSRRDLRKIGSIIEEPP- 81
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDMADARHRRAVCPRIAYMPq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 82 -----LYKNLSAYDNMKVVTTMLGVS----ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:NF033858 84 glgknLYPTLSVFENLDFFGRLFGQDaaerRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 153 TNGLDPIGIQELREIIESFKSE--GMTIMISSHILSEVEHLaDFIGFIYEGKI--------VLEKEydGSENLEELF 219
Cdd:NF033858 164 TTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVlatgtpaeLLART--GADTLEAAF 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-227 |
2.38e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRT-----ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG-----REWSRRDLR 71
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 KIGSIIEEPPLYKNL--SAYDNMKVVTTMLGVSESTIL----PLLNKVGL---GDIDKRPVkQFSLGMKQRLGIAISLIN 142
Cdd:PRK13637 83 KKVGLVFQYPEYQLFeeTIEKDIAFGPINLGLSEEEIEnrvkRAMNIVGLdyeDYKDKSPF-ELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLekeyDGseNLEELFNN 221
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCEL----QG--TPREVFKE 235
|
....*.
gi 545668914 222 QILFEK 227
Cdd:PRK13637 236 VETLES 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-204 |
3.19e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.15 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD--LRKIGSIIE 78
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPpyQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDN----MKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:PRK11607 99 SYALFPHMTVEQNiafgLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 155 GLDpigiQELR-----EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK11607 179 ALD----KKLRdrmqlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-202 |
3.34e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.99 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSI---- 76
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 -IEEPPLYKNLSAYDNMKVV------TTML-GV--------SESTILPL----LNKVGLGDIDKRPVKQFSLGMKQRLGI 136
Cdd:PRK11300 85 tFQHVRLFREMTVIENLLVAqhqqlkTGLFsGLlktpafrrAESEALDRaatwLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 137 AISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGK 202
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-206 |
4.40e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRT-ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLR----KIGSI 76
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrsKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEP--PLYKNlSAYDNMKVVTTMLGVSESTIL----PLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:PRK13647 85 FQDPddQVFSS-TVWDDVAFGPVNMGLDKDEVErrveEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 151 EPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-188 |
7.06e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 10 SYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIifegrewSRRDLRKIG------SIIEEPPL- 82
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAGGARVAyvpqrsEVPDSLPLt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 ---------------YKNLSAYDNMKVVTTmlgvsestilplLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLL 147
Cdd:NF040873 74 vrdlvamgrwarrglWRRLTRDDRAAVDDA------------LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545668914 148 ILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEV 188
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-206 |
7.97e-26 |
|
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: 98.92 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYG--KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRrdlrkigsiiee 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 ppLYKNLSAYdnMKVVTTMLGVSESTILpllNKVGlgdidkrpvKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPI 159
Cdd:cd03247 69 --LEKALSSL--ISVLNQRPYLFDTTLR---NNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545668914 160 GIQELREIIESFkSEGMTIMISSHILSEVEHlADFIGFIYEGKIVLE 206
Cdd:cd03247 133 TERQLLSLIFEV-LKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-203 |
8.64e-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: 102.88 E-value: 8.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 6 NLKKSYGKRTIlnNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW--SRRDL------RKIGSII 77
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRKGIflppekRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSAYDNM-----KVVTTMLGVSESTILPLLnkvGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:TIGR02142 82 QEARLFPHLSVRGNLrygmkRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545668914 153 TNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-183 |
8.66e-26 |
|
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: 8.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKG-KVyALIGPNGAGKSTIMKILTGLVSKTSGSIifegrewsrrdlrKIGSII-- 77
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGETVki 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 -----EEPPLYKNLSAYDNMKvvTTMLGVSESTILPLLNKVGLG--DIDKrPVKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:COG0488 381 gyfdqHQEELDPDKTVLDELR--DGAPGGTEQEVRGYLGRFLFSgdDAFK-PVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190
....*....|....*....|....*....|...
gi 545668914 151 EPTNGLDPIGIQELREIIESFksEGmTIMISSH 183
Cdd:COG0488 458 EPTNHLDIETLEALEEALDDF--PG-TVLLVSH 487
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-204 |
8.75e-26 |
|
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: 100.10 E-value: 8.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTiLNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRR--DLRKIGSIIEE 79
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDN----MKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:cd03299 80 YALFPHMTVYKNiaygLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545668914 156 LDPIG----IQELREIIESFkseGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:cd03299 160 LDVRTkeklREELKKIRKEF---GVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-206 |
1.39e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 100.65 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY---------GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS----- 66
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 67 -----RRDL--------------RKIGSIIEEPplYKNLSAYDNMKvvttmlgvSESTILPLLNKVGL--GDIDKRPvKQ 125
Cdd:TIGR02769 82 qrrafRRDVqlvfqdspsavnprMTVRQIIGEP--LRHLTSLDESE--------QKARIAELLDMVGLrsEDADKLP-RQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 126 FSLGMKQRLGIAISLINSPKLLILDEPTNGLDPI----GIQELREIIESFkseGMTIMISSHILSEVEHLADFIGFIYEG 201
Cdd:TIGR02769 151 LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVlqavILELLRKLQQAF---GTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
....*
gi 545668914 202 KIVLE 206
Cdd:TIGR02769 228 QIVEE 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-204 |
1.64e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 103.71 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 10 SY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGSIIEEPPLYk 84
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESLRRqIGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 85 NLSAYDNMKvvttmLG---VSESTILPLLNKVGLGD-IDKRP-----------VKqFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:COG1132 427 SGTIRENIR-----YGrpdATDEEVEEAAKAAQAHEfIEALPdgydtvvgergVN-LSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 150 DEPTNGLDPIGIQELREIIESFkSEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:COG1132 501 DEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIV 553
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-206 |
2.59e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.09 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY--GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE------WSRRdlRKI 73
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvWDVR--RQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPplyknlsayDNMKVVTTM----------LGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAIS 139
Cdd:PRK13635 84 GMVFQNP---------DNQFVGATVqddvafglenIGVPREEMVErvdqALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 140 LINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMIS-SHILSEVEHlADFIGFIYEGKIVLE 206
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-224 |
2.68e-25 |
|
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: 102.98 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV--SKTSGSIIFEGREWSRRDLRK-----I 73
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPPLYKNLSAYDNMKV---VTTMLGVSESTIL-----PLLNKVGLGDI-DKRPVKQFSLGMKQRLGIAISLINSP 144
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLgneITLPGGRMAYNAMylrakNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 145 KLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeydGSENLEELFNNQIL 224
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV------ATKDMSTMSEDDII 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-221 |
3.94e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.09 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKI---LTGLVS--KTSGSIIFEGREWSRRDL------ 70
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPgfRVEGKVTFHGKNLYAPDVdpvevr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKIGSIIEEP-PLYKnlSAYDNMKV---VTTMLGVSESTILPLLNKVGLGDIDKRPVKQ----FSLGMKQRLGIAISLIN 142
Cdd:PRK14243 91 RRIGMVFQKPnPFPK--SIYDNIAYgarINGYKGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKsEGMTIMISSHILSEVEHLADFIGF---------IYEGKIVlekEYDGSe 213
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDMTAFfnvelteggGRYGYLV---EFDRT- 243
|
....*...
gi 545668914 214 nlEELFNN 221
Cdd:PRK14243 244 --EKIFNS 249
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-205 |
3.98e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.43 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS----RRDLR----KIGSIIEEPPlyKNLSA 88
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKqirkKVGLVFQFPE--SQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 89 YDNMKVVT---TMLGVS----ESTILPLLNKVGLGD--IDKRPVkQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPI 159
Cdd:PRK13649 101 ETVLKDVAfgpQNFGVSqeeaEALAREKLALVGISEslFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545668914 160 GIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVL 205
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-204 |
4.29e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS---------RRDLR- 71
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpsekaIRLLRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 KIGSIIEEPPLYKNLSAYDN-----MKVvttmLGVSESTIL----PLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLIN 142
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlieapCKV----LGLSKEQARekamKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHilsEVE---HLADFIGFIYEGKIV 204
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTH---EVEfarKVASQVVYMEKGRII 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-204 |
6.01e-25 |
|
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: 98.00 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKR---TILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLR-KIGSI 76
Cdd:cd03249 3 FKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLRWLRsQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYkNLSAYDNMKvvttmLG---VSESTILPLLNKVGLGD-IDKRPVK----------QFSLGMKQRLGIAISLIN 142
Cdd:cd03249 83 SQEPVLF-DGTIAENIR-----YGkpdATDEEVEEAAKKANIHDfIMSLPDGydtlvgergsQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKsEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-204 |
6.78e-25 |
|
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: 96.85 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 8 KKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVS--KTSGSIIFEGREWSRRDLRK-IGSIIEEPPLYK 84
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKiIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 85 NLSAYDNMKVVTTMLGVSestilpllnkvglGdidkrpvkqfslGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQEL 164
Cdd:cd03213 96 TLTVRETLMFAAKLRGLS-------------G------------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545668914 165 REIIESFKSEGMTIMISSHILS-EVEHLADFIGFIYEGKIV 204
Cdd:cd03213 151 MSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-184 |
7.89e-25 |
|
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: 96.79 E-value: 7.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR-RDL--RKIGSIIE 78
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqRDSiaRGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKVVTTMlgVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP 158
Cdd:cd03231 81 APGIKTTLSVLENLRFWHAD--HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*.
gi 545668914 159 IGIQELREIIESFKSEGMTIMISSHI 184
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
9.85e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 9.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRKIGSII 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvatTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 -EEP-----------------PLYK-NLSAYDNMKvvttmlgVSEStilplLNKVGLGDIDKRPVKQFSLGMKQRLGIAI 138
Cdd:COG4604 81 rQENhinsrltvrelvafgrfPYSKgRLTAEDREI-------IDEA-----IAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 139 SLINSPKLLILDEPTNGLDP---IGI-QELREIIESFkseGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDG--- 211
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMkhsVQMmKLLRRLADEL---GKTVVIVLHDINFASCYADHIVAMKDGRVV----AQGtpe 221
|
250
....*....|...
gi 545668914 212 ----SENLEELFN 220
Cdd:COG4604 222 eiitPEVLSDIYD 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-183 |
1.07e-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: 95.75 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYG--KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRK-IGS 75
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqWDPNELGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNlSAYDNMkvvttmlgvsestilpllnkvglgdidkrpvkqFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:cd03246 81 LPQDDELFSG-SIAENI---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180
....*....|....*....|....*...
gi 545668914 156 LDPIGIQELREIIESFKSEGMTIMISSH 183
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-158 |
1.87e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRKIGSII 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 eepPLYKNLSAYDNMKVVTTM------LGVSESTILPL--LNKVGLGDIDKRPVKQFSLGMKQRLGIAISLI------NS 143
Cdd:PRK13548 82 ---PQHSSLSFPFTVEEVVAMgraphgLSRAEDDALVAaaLAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170
....*....|....*
gi 545668914 144 PKLLILDEPTNGLDP 158
Cdd:PRK13548 159 PRWLLLDEPTSALDL 173
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-204 |
2.31e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.39 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR--EWSRRDL----RKIG 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLlalrQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPP---LYKNLSAydNMKVVTTMLGVSESTIL----PLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLL 147
Cdd:PRK13638 81 TVFQDPEqqiFYTDIDS--DIAFSLRNLGVPEAEITrrvdEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 148 ILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-203 |
4.50e-24 |
|
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: 100.09 E-value: 4.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGK--RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR--EWSRRDLRK-IGSIIE 78
Cdd:TIGR01257 931 VKNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdiETNLDAVRQsLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKVVTTMLGVSEST----ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEaqleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545668914 155 GLDPIGIQELREIIESFKSeGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-192 |
4.64e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 99.44 E-value: 4.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 12 GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDL-RKIG-----------SI 76
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADlsqWDREELgRHIGylpqdvelfdgTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEepplykNLSAYDNM---KVVT--TMLGVSEsTILPLLN----KVGLGDIdkrpvkQFSLGMKQRLGIAISLINSPKLL 147
Cdd:COG4618 423 AE------NIARFGDAdpeKVVAaaKLAGVHE-MILRLPDgydtRIGEGGA------RLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 148 ILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSH---ILSEVEHLA 192
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHrpsLLAAVDKLL 537
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-157 |
5.05e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR--RDLRKIGSIIEE 79
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDNMKVVTTMLGVSESTILPL----LNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRvmeaLRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
..
gi 545668914 156 LD 157
Cdd:PRK09452 175 LD 176
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-208 |
6.19e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 98.92 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGS 75
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNM----KVVTTMLGV------SESTilPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPK 145
Cdd:PRK10762 84 IHQELNLIPQLTIAENIflgrEFVNRFGRIdwkkmyAEAD--KLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 146 LLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKE 208
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAERE 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-224 |
7.39e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.97 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGS 75
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKahqlgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNMKVVTTMLGVSESTILPLLNKVGLgdidkrpvkQFSLGMK---------QRLGIAISLINSPKL 146
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGC---------QLDLDSSagslevadrQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 147 LILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLekeydgSENLEELFNNQIL 224
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL------SGKTADLSTDDII 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-221 |
8.55e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.42 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE-------------WSRR 68
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 69 DLR----KIGSIIEEPPLYKNLSAYDN-MKVVTTMLGVSESTI----LPLLNKVGLGDI--DKRPVkQFSLGMKQRLGIA 137
Cdd:PRK10619 86 QLRllrtRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEAreraVKYLAKVGIDERaqGKYPV-HLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 138 ISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIvlekEYDGSEnlEE 217
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI----EEEGAP--EQ 238
|
....
gi 545668914 218 LFNN 221
Cdd:PRK10619 239 LFGN 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-195 |
1.10e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.45 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIgSIIEEPPLYKNLSAYDNMKvvt 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-VVFQNYSLLPWLTVRENIA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 97 tmLGVSEstILPLLNK-------------VGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQE 163
Cdd:TIGR01184 77 --LAVDR--VLPDLSKserraiveehialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|...
gi 545668914 164 LRE-IIESFKSEGMTIMISSHILSEVEHLADFI 195
Cdd:TIGR01184 153 LQEeLMQIWEEHRVTVLMVTHDVDEALLLSDRV 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-219 |
1.21e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.44 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG----REWSRRDLRKIGSII 77
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSA--------YDNMKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:PRK10253 88 QNATTPGDITVqelvargrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 150 DEPTNGLDPIGIQELREIIESF-KSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE---KEYDGSENLEELF 219
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQgapKEIVTAELIERIY 241
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-203 |
1.35e-23 |
|
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: 94.46 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRT---ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD----LRKIG 74
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPPLYKNlSAYDN----------MKVVTTMLGVSESTILPLLNKVGLGDIDKRPvKQFSLGMKQRLGIAISLINSP 144
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNiayglqscsfECVKEAAQKAHAHSFISELASGYDTEVGEKG-SQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 145 KLLILDEPTNGLDpigiQELREIIESFKSEGM---TIMISSHILSEVEHlADFIGFIYEGKI 203
Cdd:cd03248 170 QVLILDEATSALD----AESEQQVQQALYDWPerrTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-204 |
1.45e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.70 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW---------SRRDLR- 71
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsdkAIRELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 KIGSIIEEPPLYKNLSAYDN-----MKVvttmLGVSEST----ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLIN 142
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlieapCRV----LGLSKDQalarAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHilsEVE---HLADFIGFIYEGKIV 204
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH---EVEvarKTASRVVYMENGHIV 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-204 |
1.47e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.82 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSI------IFEGREWSR-----RD 69
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQqkgliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 70 LR-KIGSIIEEPPLYKNLSAYDNM---KVVTTMLGVSESTIL--PLLNKVGL-GDIDKRPvKQFSLGMKQRLGIAISLIN 142
Cdd:PRK11264 83 LRqHVGFVFQNFNLFPHRTVLENIiegPVIVKGEPKEEATARarELLAKVGLaGKETSYP-RRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-206 |
1.94e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.16 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 6 NLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKT-----SGSIIFEGRE-WSRRDL----RKIGS 75
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrySGDVLLGGRSiFNYRDVlefrRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKnLSAYDNMkvvttMLGVSESTILP----------LLNKVGLGDIDKRPVK----QFSLGMKQRLGIAISLI 141
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNV-----LAGVRAHKLVPrkefrgvaqaRLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 142 NSPKLLILDEPTNGLDPIGIQELREIIESFkSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-204 |
1.97e-23 |
|
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: 93.87 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 8 KKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV---SKTSGSIIFEGREWSRRDLRKIGSIIEEPP-LY 83
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQFQKCVAYVRQDDiLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 84 KNLSAYDNMKVVTTMLGVSEST--------ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNG 155
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSdairkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545668914 156 LDPIGIQELREIIESFKSEGMTIMISSHI-LSEVEHLADFIGFIYEGKIV 204
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
2.76e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.03 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRKIGSII 77
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaaWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 eepPLYKNLS-AYDNMKVVttMLGVS---------ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLI------ 141
Cdd:COG4559 81 ---PQHSSLAfPFTVEEVV--ALGRAphgssaaqdRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 142 -NSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDGS-------E 213
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV----AQGTpeevltdE 231
|
....*.
gi 545668914 214 NLEELF 219
Cdd:COG4559 232 LLERVY 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-215 |
3.28e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVS-----KTSGSIIFEGRE-WSRR----DL 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiYSPRtdtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RK-IGSIIEEPPLYKnLSAYDNMKVVTTMLGVSESTIL-----PLLNKVGLGDIDKRPVKQFSLGM----KQRLGIAISL 140
Cdd:PRK14239 85 RKeIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLdeaveKSLKGASIWDEVKDRLHDSALGLsggqQQRVCIARVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 141 INSPKLLILDEPTNGLDPIGIQELREIIESFKSEgMTIMISSHILSEVEHLADFIGFIYEGKIVlekEYDGSENL 215
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI---EYNDTKQM 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
3.87e-23 |
|
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: 96.97 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDLRK-IGSI 76
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVplaDADADSWRDqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYkNLSAYDNMKVVTtmLGVSESTILPLLNKVGLGD------------IDKRPVKqFSLGMKQRLGIAISLINSP 144
Cdd:TIGR02857 402 PQHPFLF-AGTIAENIRLAR--PDASDAEIREALERAGLDEfvaalpqgldtpIGEGGAG-LSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545668914 145 KLLILDEPTNGLDPIGIQELREIIESFkSEGMTIMISSHILsEVEHLADFI 195
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRI 526
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-204 |
3.95e-23 |
|
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: 93.06 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGK--RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGS 75
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASLRRqIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYkNLSAYDNMKVVTTmlGVSESTILPLLNKVGLGD------------IDKRPVKqFSLGMKQRLGIAISLINS 143
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRP--GATREEVEEAARAANAHEfimelpegydtvIGERGVK-LSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 144 PKLLILDEPTNGLDPIGIQELREIIESFkSEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-168 |
4.74e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.61 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKiGSIIEEP 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-GVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAYDNMKVVTTMLGVS----ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGL 156
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEkmqrLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170
....*....|..
gi 545668914 157 DPIGIQELREII 168
Cdd:PRK11248 160 DAFTREQMQTLL 171
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-157 |
7.03e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 92.50 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKR----TILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD------L 70
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 R--KIGSIIEEPPLYKNLSAYDNMkvvttML-----GVSES--TILPLLNKVGLGD-IDKRPvKQFSLGMKQRLGIAISL 140
Cdd:COG4181 88 RarHVGFVFQSFQLLPTLTALENV-----MLplelaGRRDAraRARALLERVGLGHrLDHYP-AQLSGGEQQRVALARAF 161
|
170
....*....|....*..
gi 545668914 141 INSPKLLILDEPTNGLD 157
Cdd:COG4181 162 ATEPAILFADEPTGNLD 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-204 |
7.41e-23 |
|
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: 95.91 E-value: 7.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY-GKRTIL----------NNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSkTSGSIIFEGREW---SR 67
Cdd:COG4172 276 LEARDLKVWFpIKRGLFrrtvghvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLdglSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 68 RDLRK---------------------IGSIIEEPplyknlsaydnMKVVTTMLGVSEST--ILPLLNKVGL--GDIDKRP 122
Cdd:COG4172 355 RALRPlrrrmqvvfqdpfgslsprmtVGQIIAEG-----------LRVHGPGLSAAERRarVAEALEEVGLdpAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 123 vKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDpIGIQelREIIESFKS----EGMTIMISSHILSEVEHLADFIGFI 198
Cdd:COG4172 424 -HEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQ--AQILDLLRDlqreHGLAYLFISHDLAVVRALAHRVMVM 499
|
....*.
gi 545668914 199 YEGKIV 204
Cdd:COG4172 500 KDGKVV 505
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-206 |
1.03e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 93.23 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-----GKRTI-LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE-------WSR 67
Cdd:PRK13633 4 MIKCKNVSYKYesneeSTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 68 RdlRKIGSIIEEPplyknlsayDNMKVVTTM----------LGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQR 133
Cdd:PRK13633 84 R--NKAGMVFQNP---------DNQIVATIVeedvafgpenLGIPPEEIRErvdeSLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 134 LGIAISLINSPKLLILDEPTNGLDPIGIQE-LREIIESFKSEGMTIMISSHILSEVEHlADFIGFIYEGKIVLE 206
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREvVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-217 |
1.41e-22 |
|
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: 91.94 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTG--LVSKTSGSIIFEG----------------- 62
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGqdllelepderaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 63 --------------REWSRRDLRKIGSIIEEPPLyKNLSAYDNMKVVTTMLGVSESTILPLLNkVGlgdidkrpvkqFSL 128
Cdd:TIGR01978 81 lafqypeeipgvsnLEFLRSALNARRSARGEEPL-DLLDFEKLLKEKLALLDMDEEFLNRSVN-EG-----------FSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 129 GMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLA-DFIGFIYEGKIVLEK 207
Cdd:TIGR01978 148 GEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSG 227
|
250
....*....|
gi 545668914 208 EYDGSENLEE 217
Cdd:TIGR01978 228 DVELAKELEA 237
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-204 |
1.49e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY---------GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS----- 66
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 67 -----RRDL--------------RKIGSIIEEPplyknlsaydnMKVVTTMlgvSEST----ILPLLNKVGL--GDIDKR 121
Cdd:PRK10419 83 qrkafRRDIqmvfqdsisavnprKTVREIIREP-----------LRHLLSL---DKAErlarASEMLRAVDLddSVLDKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 122 PvKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPI----GIQELREIIESFkseGMTIMISSHILSEVEHLADFIGF 197
Cdd:PRK10419 149 P-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlqagVIRLLKKLQQQF---GTACLFITHDLRLVERFCQRVMV 224
|
....*..
gi 545668914 198 IYEGKIV 204
Cdd:PRK10419 225 MDNGQIV 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-204 |
1.66e-22 |
|
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: 91.11 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGSIIEEPPLYKNlSAYDNM 92
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADLRRnIGYVPQDVTLFYG-TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 93 kvvttMLGVSEST---ILPLLNKVGLGDIDKRPVKQFSL-----------GMKQRLGIAISLINSPKLLILDEPTNGLDp 158
Cdd:cd03245 99 -----TLGAPLADderILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTSAMD- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 159 igIQELREIIESFKS--EGMTIMISSHILSEVEhLADFIGFIYEGKIV 204
Cdd:cd03245 173 --MNSEERLKERLRQllGDKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-184 |
2.03e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.70 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREwsrrdlrkigsiiEEP 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-------------IDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAY----DNMKVVTTM----------LGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKL 146
Cdd:PRK13539 69 PDVAEACHYlghrNAMKPALTVaenlefwaafLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 545668914 147 LILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHI 184
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
2.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGK---RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE------WSRRdlR 71
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvWDIR--H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 KIGSIIEEPplyknlsayDNMKVVTTM-----LGVsESTILPL----------LNKVGLGDIDKRPVKQFSLGMKQRLGI 136
Cdd:PRK13650 82 KIGMVFQNP---------DNQFVGATVeddvaFGL-ENKGIPHeemkervneaLELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 137 AISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEhLADFIGFIYEGKIvlekeyDGSENL 215
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQV------ESTSTP 224
|
....
gi 545668914 216 EELF 219
Cdd:PRK13650 225 RELF 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-222 |
2.31e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.00 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVS--KTSGS-IIFEGREWSR-----RDLRK 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQRegrlaRDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 ----IGSIIEEPPLYKNLSAYDNmkVVTTMLG--------------VSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRL 134
Cdd:PRK09984 84 sranTGYIFQQFNLVNRLSVLEN--VLIGALGstpfwrtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 135 GIAISLINSPKLLILDEPTNGLDP----IGIQELREIIEsfkSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYD 210
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPesarIVMDTLRDINQ---NDGITVVVTLHQVDYALRYCERIVALRQGHVF----YD 234
|
250
....*....|..
gi 545668914 211 GSenlEELFNNQ 222
Cdd:PRK09984 235 GS---SQQFDNE 243
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-204 |
2.58e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.53 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGS----- 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 -------IIEEPP---LYKNLSAYDN-----MKVVTTMLGVSESTILPLLNKV--GLGDIDKRPvKQFSLGMKQRLGIAI 138
Cdd:PRK11701 86 llrtewgFVHQHPrdgLRMQVSAGGNigerlMAVGARHYGDIRATAGDWLERVeiDAARIDDLP-TTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 139 SLINSPKLLILDEPTNGLDpIGIQE-----LREIIESFkseGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLD-VSVQArlldlLRGLVREL---GLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-203 |
2.97e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.74 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR---RDLRK-IGSIIEEPP----------- 81
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnfEKLRKhIGIVFQNPDnqfvgsivkyd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 82 ----LYKNLSAYDNMKVVttmlgVSEStilplLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:PRK13648 105 vafgLENHAVPYDEMHRR-----VSEA-----LKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545668914 158 PIGIQELREIIESFKSE-GMTIMISSHILSEVEHlADFIGFIYEGKI 203
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-221 |
4.97e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.08 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 18 NNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW------SRRDLRK------------------I 73
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkddEWRAVRSdiqmifqdplaslnprmtI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEP--PLYKNLSAYDNMKVVTTMLgvsestilpllNKVGL--GDIDKRPvKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:PRK15079 118 GEIIAEPlrTYHPKLSRQEVKDRVKAMM-----------LKVGLlpNLINRYP-HEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 150 DEPTNGLDpIGIQ-ELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYDgsenleELFNN 221
Cdd:PRK15079 186 DEPVSALD-VSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD------EVYHN 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
5.76e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRT-----ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSI----IFEGREWSR---- 67
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 68 -----------RDLRKIGSIIEEPP---LYKNLSAYDNMkVVTTMLGVSESTILPL----LNKVGLGD--IDKRPVkQFS 127
Cdd:PRK13631 101 tnpyskkiknfKELRRRVSMVFQFPeyqLFKDTIEKDIM-FGPVALGVKKSEAKKLakfyLNKMGLDDsyLERSPF-GLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 128 LGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLek 207
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK-- 256
|
250 260
....*....|....*....|
gi 545668914 208 eydgSENLEELFNNQILFEK 227
Cdd:PRK13631 257 ----TGTPYEIFTDQHIINS 272
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-204 |
6.29e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 89.98 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 3 KIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGSII 77
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLRSmIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYkNLSAYDNMKvvttmLGVSEST---ILPLLNKVGLGD-IDKRP----------VKQFSLGMKQRLGIAISLINS 143
Cdd:cd03254 84 QDTFLF-SGTIMENIR-----LGRPNATdeeVIEAAKEAGAHDfIMKLPngydtvlgenGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 144 PKLLILDEPTNGLDPIGIQELREIIESFKsEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-206 |
1.08e-21 |
|
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: 89.60 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 6 NLKKSYG-KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGSIIEEP 80
Cdd:cd03253 5 NVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRaIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PL----------YKNLSAYDNMKVVTTMLGVSESTILPLLN----KVGlgdidKRPVKqFSLGMKQRLGIAISLINSPKL 146
Cdd:cd03253 85 VLfndtigynirYGRPDATDEEVIEAAKAAQIHDKIMRFPDgydtIVG-----ERGLK-LSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 147 LILDEPTNGLDPIGIQELREIIESFKSEGMTIMIsSHILSEVEHlADFIGFIYEGKIVLE 206
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVI-AHRLSTIVN-ADKIIVLKDGRIVER 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-204 |
1.78e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.09 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY----GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD------L 70
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalaqL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RK--IGSIIEEPPLYKNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGD-IDKRPvKQFSLGMKQRLGIAISLINS 143
Cdd:PRK10535 84 RRehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLraqeLLQRLGLEDrVEYQP-SQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 144 PKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHIlSEVEHLADFIGFIYEGKIV 204
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-204 |
1.96e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.09 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRT---ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDL-RKIG 74
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplVQYDHHYLhRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPPLY----KNLSAY------DNMKVVTTMLGVSESTILPLLNKVGLgDIDKRPVkQFSLGMKQRLGIAISLINSP 144
Cdd:TIGR00958 559 LVGQEPVLFsgsvRENIAYgltdtpDEEIMAAAKAANAHDFIMEFPNGYDT-EVGEKGS-QLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 145 KLLILDEPTNGLDpigIQELREIIESFKSEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:TIGR00958 637 RVLILDEATSALD---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-224 |
2.31e-21 |
|
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: 90.55 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIqNLKKSYGKRTIlnNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW----SRRDL----RK 72
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIFLpphrRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 IGSIIEEPPLYKNLSAYDN----MKV------------VTTMLGvsestILPLLNkvglgdidkRPVKQFSLGMKQRLGI 136
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNllygRKRapraerrisfdeVVELLG-----IGHLLD---------RRPATLSGGERQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 137 AISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVlekeydGSENL 215
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV------ASGPL 218
|
....*....
gi 545668914 216 EELFNNQIL 224
Cdd:COG4148 219 AEVLSRPDL 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-221 |
2.97e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY--------GKRTI--LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW------ 65
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 66 SRRDLR------------------KIGSIIEEPPLyknlsaydnmkvVTTMLGVSEST--ILPLLNKVGLgdidkRP--- 122
Cdd:PRK11308 86 AQKLLRqkiqivfqnpygslnprkKVGQILEEPLL------------INTSLSAAERRekALAMMAKVGL-----RPehy 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 123 ---VKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD-PIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFI 198
Cdd:PRK11308 149 dryPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
250 260
....*....|....*....|...
gi 545668914 199 YEGKIVlEKeydGSEnlEELFNN 221
Cdd:PRK11308 229 YLGRCV-EK---GTK--EQIFNN 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-218 |
4.93e-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: 91.02 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-----GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFE-GREW--------- 65
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWvdmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 66 -SRRDLRKIGSIIEEPPLYKNLSAYDN---------------MKVVTT--MLGVSESTILPLLNKVglgdidkrpVKQFS 127
Cdd:TIGR03269 359 gRGRAKRYIGILHQEYDLYPHRTVLDNlteaiglelpdelarMKAVITlkMVGFDEEKAEEILDKY---------PDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 128 LGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELRE-IIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVle 206
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV-- 507
|
250
....*....|..
gi 545668914 207 KEYDGSENLEEL 218
Cdd:TIGR03269 508 KIGDPEEIVEEL 519
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-204 |
4.98e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 88.73 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW-------SRRDLRKIGSII---EEPPLYKNl 86
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnkNLKKLRKKVSLVfqfPEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 87 SAYDNMKVVTTMLGVSE----STILPLLNKVGLGD--IDKRPVkQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIG 160
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEdeakEKALKWLKKVGLSEdlISKSPF-ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 545668914 161 IQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-204 |
1.04e-20 |
|
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: 86.77 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 14 RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL----RKIGSIIEEPPLYkNLSAY 89
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawlrRQVGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 90 DNMKV------------VTTMLGVSESTI-LPLlnkvGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGL 156
Cdd:cd03252 94 DNIALadpgmsmervieAAKLAGAHDFISeLPE----GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545668914 157 DpigIQELREIIESFK--SEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:cd03252 170 D---YESEHAIMRNMHdiCAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-205 |
1.16e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.77 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 14 RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR-------RDLR-KIGSIIE--EPPLY 83
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkklKPLRkKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 84 KNLSAYD------NmkvvttmLGVSESTIL----PLLNKVGLGD--IDKRPVkQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:PRK13634 100 EETVEKDicfgpmN-------FGVSEEDAKqkarEMIELVGLPEelLARSPF-ELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 152 PTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVL 205
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-220 |
1.71e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 26 KGKVYALIGPNGAGKSTIMKILTGLVSkTSGSIIFEGR---EWSRRDLRKIGSII---EEPPL------YKNLSAYDNmk 93
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRplsDWSAAELARHRAYLsqqQSPPFampvfqYLALHQPAG-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 94 vvtTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISL------IN-SPKLLILDEPTNGLDpIGIQE-LR 165
Cdd:COG4138 98 ---ASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLD-VAQQAaLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 166 EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYD---GSENLEELFN 220
Cdd:COG4138 174 RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAevmTPENLSEVFG 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-204 |
1.73e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGSI 76
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMkvvttMLG--------VSESTI----LPLLNKVGLgDID-KRPVKQFSLGMKQRLGIAISLINS 143
Cdd:PRK11288 85 YQELHLVPEMTVAENL-----YLGqlphkggiVNRRLLnyeaREQLEHLGV-DIDpDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 144 PKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-202 |
1.98e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 89.17 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 3 KIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV--SKTSGSIIFEGREWSRRDLRKIGSIIEEP 80
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPTKQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAYDNMKVVTTM-----------LGVSESTILPL-LNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PLN03211 150 ILYPHLTVRETLVFCSLLrlpksltkqekILVAESVISELgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFKSEGMTIMISSH-ILSEVEHLADFIGFIYEGK 202
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHqPSSRVYQMFDSVLVLSEGR 284
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-157 |
2.30e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY--GK--RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS------RRDL 70
Cdd:PRK11629 5 LLQCDNLCKRYqeGSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaaKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 R--KIGSIIEEPPLYKNLSAYDNMKVVTTMLGV----SESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSP 144
Cdd:PRK11629 85 RnqKLGFIYQFHHLLPDFTALENVAMPLLIGKKkpaeINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170
....*....|...
gi 545668914 145 KLLILDEPTNGLD 157
Cdd:PRK11629 165 RLVLADEPTGNLD 177
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-195 |
3.64e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.39 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSrrDL----RKIGSIIEE 79
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVppaeRGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDNMKVVTTMLGVSESTILPLLNKVG----LGD-IDKRPvKQFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAevlqLAHlLDRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 545668914 155 GLDP-IGIQELREIIESFKSEGMTIMISSHILSEVEHLADFI 195
Cdd:PRK11000 163 NLDAaLRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKI 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-204 |
3.96e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGK----RTILNNVNMNIPKGKVYALIGPNGAGKS----TIMKIL-TGLVSKTSGSIIFEGR------EW 65
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGEsllhasEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 66 SRRDLR--KIGSIIEEP------------PLYKNLSAYDNMKvvttmLGVSESTILPLLNKVGLGDIDKR----PvKQFS 127
Cdd:PRK15134 85 TLRGVRgnKIAMIFQEPmvslnplhtlekQLYEVLSLHRGMR-----REAARGEILNCLDRVGIRQAAKRltdyP-HQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 128 LGMKQRLGIAISLINSPKLLILDEPTNGLDpIGIQ-ELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VSVQaQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-203 |
4.14e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSIIEEP 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLS-AYDNMKVV-------TTMLGVSEST----ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK09536 83 PQDTSLSfEFDVRQVVemgrtphRSRFDTWTETdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 149 LDEPTNGLDpIG--IQELrEIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:PRK09536 163 LDEPTASLD-INhqVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-204 |
4.98e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRT--ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDLRKIGSI 76
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiaDYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVVTTmlGVSESTILPLLNKVGLGDI--DKRPV--------KQFSLGMKQRLGIAISLINSPKL 146
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAAP--NASDEALIEVLQQVGLEKLleDDKGLnawlgeggRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 147 LILDEPTNGLDPIGIQELREIIESFkSEGMTIMISSHILSEVEHLaDFIGFIYEGKIV 204
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-189 |
5.95e-20 |
|
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: 87.68 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFeGR-------EWSRRDLRKIG 74
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvklayvDQSRDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEpplyknLS-AYDNMKVVTTMlgVSESTILPLLNKVGlGDIDKRpVKQFSLGMKQRLGIAISLINSPKLLILDEPT 153
Cdd:TIGR03719 402 TVWEE------ISgGLDIIKLGKRE--IPSRAYVGRFNFKG-SDQQKK-VGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545668914 154 NGLDPIGIQELREIIESFKSEGMTI--------MISSHIL-----SEVE 189
Cdd:TIGR03719 472 NDLDVETLRALEEALLNFAGCAVVIshdrwfldRIATHILafegdSHVE 520
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-183 |
7.06e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 13 KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEgrewsrrdlrkigsiIEEPPLYKNLSAYDNM 92
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---------------VPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 93 KVVTTMLGVSEstilpLLNKVGLGD--IDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIES 170
Cdd:COG2401 107 GRKGDFKDAVE-----LLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170
....*....|....
gi 545668914 171 F-KSEGMTIMISSH 183
Cdd:COG2401 182 LaRRAGITLVVATH 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-183 |
9.27e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 87.03 E-value: 9.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRKIGSII 77
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSAYDNMKVVTTmlGVSESTILPLLNKVGLGD-IDKRP----------VKQFSLGMKQRLGIAISLINSPKL 146
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRLARP--DATDEELWAALERVGLADwLRALPdgldtvlgegGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 545668914 147 LILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSH 183
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-193 |
9.56e-20 |
|
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: 84.02 E-value: 9.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-----GKRTI--LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFE-GREW------S 66
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWvdlaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 67 RRD---LRK--IG------SIIeePplykNLSAYDnmkVVTTML---GVSEST-------ILPLLNkvglgdIDKR---- 121
Cdd:COG4778 84 PREilaLRRrtIGyvsqflRVI--P----RVSALD---VVAEPLlerGVDREEararareLLARLN------LPERlwdl 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 122 PVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLAD 193
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVAD 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-227 |
1.13e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.85 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 13 KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV---SKTSGSIIFEGRE------WSRRDlrKIGSIIEEPply 83
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITltaktvWDIRE--KVGIVFQNP--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 84 knlsayDNMKVVTTM----------LGVSESTILPL----LNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:PRK13640 94 ------DNQFVGATVgddvafglenRAVPRPEMIKIvrdvLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHlADFIGFIYEGKIVlekeydGSENLEELFNNQILFEK 227
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLL------AQGSPVEIFSKVEMLKE 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-183 |
1.35e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 83.08 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREwSRRDL----RKIGSI 76
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS-IKKDLctyqKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDN----MKVVTTMLGVSEstilpLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:PRK13540 80 GHRSGINPYLTLRENclydIHFSPGAVGITE-----LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 545668914 153 TNGLDPIGIQELREIIESFKSEGMTIMISSH 183
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-221 |
1.47e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.64 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 12 GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSK---TSGSIIFEGREWSRRDLRKIGSIIEEPPLY-KNLS 87
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYVQQDDLFiPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 88 AYDNMkVVTTMLGVSEST--------ILPLLNKVGLGDI------DKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPT 153
Cdd:TIGR00955 116 VREHL-MFQAHLRMPRRVtkkekrerVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 154 NGLDPIGIQELREIIESFKSEGMTIMISSH-ILSEVEHLADFIGFIYEGKIVlekeYDGS-ENLEELFNN 221
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHqPSSELFELFDKIILMAEGRVA----YLGSpDQAVPFFSD 260
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
2.22e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 83.70 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSIIEEP 80
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 P-----------------LYKNLSAYDN-MKVVTTMLGVS----ESTILPLLNKVGLGDI-DKRPVkQFSLGMKQRLGIA 137
Cdd:COG4598 88 RqlqrirtrlgmvfqsfnLWSHMTVLENvIEAPVHVLGRPkaeaIERAEALLAKVGLADKrDAYPA-HLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 138 ISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIvlekEYDGSEnlEE 217
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI----EEQGPP--AE 240
|
....
gi 545668914 218 LFNN 221
Cdd:COG4598 241 VFGN 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-212 |
2.23e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRKIGSII 77
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSAYDNMKVVTTMLG--VSESTILPLLNKVGLGD-IDKRPVKQFSLGMKQRlgiaISLINS----PKLLILD 150
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIFPWQIRNqqPDPAIFLDDLERFALPDtILTKNIAELSGGEKQR----ISLIRNlqfmPKVLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 151 EPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYDGS 212
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINHADKVITLQPHAGEMQEARYELA 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-203 |
2.63e-19 |
|
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: 81.71 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGkrtiLNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGS 75
Cdd:cd03215 4 VLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDairagIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPP---LYKNLSAYDNMkvvttmlgvsestILPLLnkvglgdidkrpvkqFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:cd03215 80 VPEDRKregLVLDLSVAENI-------------ALSSL---------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545668914 153 TNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-208 |
3.16e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRT-ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSR-RDLRKIGS 75
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPlyknLSAYDNMKVVTTMLGVSESTILP----------LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPK 145
Cdd:PRK13644 81 IVFQNP----ETQFVGRTVEEDLAFGPENLCLPpieirkrvdrALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 146 LLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVeHLADFIGFIYEGKIVLEKE 208
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-223 |
4.13e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 27 GKVYALIGPNGAGKSTIMKILTGLVSkTSGSIIFEGR---EWSRRDLRKIGSII--EEPPL-------YKNLSAYDNmkv 94
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQpleAWSAAELARHRAYLsqQQTPPfampvfqYLTLHQPDK--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 95 vtTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISL------IN-SPKLLILDEPTNGLDpIGiQE--LR 165
Cdd:PRK03695 98 --TRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpdINpAGQLLLLDEPMNSLD-VA-QQaaLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 166 EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYD---GSENLEELFNNQI 223
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDevlTPENLAQVFGVNF 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-204 |
4.62e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRT-----ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSI----IFEGREWSRRDLR 71
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 ----KIGSIIEEPP--LYKNlSAYDNMKVVTTMLGVS----ESTILPLLNKVGLGD--IDKRPVkQFSLGMKQRLGIAIS 139
Cdd:PRK13643 81 pvrkKVGVVFQFPEsqLFEE-TVLKDVAFGPQNFGIPkekaEKIAAEKLEMVGLADefWEKSPF-ELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 140 LINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-204 |
5.88e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 84.77 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTI--LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRKIGSI 76
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNMKVvTTMLGVSESTILPLLNKVGLGD-IDKRPV----------KQFSLGMKQRLGIAISLINSPK 145
Cdd:TIGR02203 411 VSQDVVLFNDTIANNIAY-GRTEQADRAEIERALAAAYAQDfVDKLPLgldtpigengVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 146 LLILDEPTNGLDPIGIQELREIIESFKsEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-201 |
7.11e-19 |
|
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: 85.07 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRT--ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE--WSRRDLRK-IGS 75
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSilTNISDVHQnMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLYKNLSAYDNMKVVTTMLGVSESTILPLLN----KVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANwsiqSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545668914 152 PTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEG 201
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-209 |
1.10e-18 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 84.17 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREwsrrDLRKIGSiieepPLYKNLSAYDNMKVVT 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA----ALIAISS-----GLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 97 TMLGVSESTILPLLNKV-GLGDIDK---RPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFK 172
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIiEFADIGKfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFK 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 545668914 173 SEGMTIMISSHILSEVEHLADFIGFIYEGKIvleKEY 209
Cdd:PRK13545 191 EQGKTIFFISHSLSQVKSFCTKALWLHYGQV---KEY 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-202 |
1.68e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.46 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY----GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSK---TSGSIIFEGRE---WSRRDL 70
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREilnLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKIG----SIIEEPPLyKNLSAYdnMKVVTT-----ML--GVSESTI----LPLLNKVGLGDIDKR----PvKQFSLGMK 131
Cdd:PRK09473 92 NKLRaeqiSMIFQDPM-TSLNPY--MRVGEQlmevlMLhkGMSKAEAfeesVRMLDAVKMPEARKRmkmyP-HEFSGGMR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 132 QRLGIAISLINSPKLLILDEPTNGLDpIGIQ-ELREIIESFKSEGMT--IMIsSHILSEVEHLADFIGFIYEGK 202
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALD-VTVQaQIMTLLNELKREFNTaiIMI-THDLGVVAGICDKVLVMYAGR 239
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-210 |
1.77e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.48 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTiMKILTGLVSKTSGSIIFEGREW--SRRDLRKigSIIEE 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWcaNRRALRR--TIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLY----KNLSAYDNMKVVTTMLGVSESTILP----LLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:NF000106 91 RPVR*grrESFSGRENLYMIGR*LDLSRKDARAradeLLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 152 PTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEKEYD 210
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-210 |
1.90e-18 |
|
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: 80.23 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY--GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS---RRDLRKIGSI 76
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkigLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 I-EEPPLY-----KNLSAYDNmkvvttmlgVSESTILPLLNKVGLGD-IDKRPVK----------QFSLGMKQRLGIAIS 139
Cdd:cd03244 83 IpQDPVLFsgtirSNLDPFGE---------YSDEELWQALERVGLKEfVESLPGGldtvveeggeNLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 140 LINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMIsSHILSEVEHlADFIGFIYEGKIVlekEYD 210
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTI-AHRLDTIID-SDRILVLDKGRVV---EFD 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-158 |
2.05e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGK-----RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR------EWSRrd 69
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpEYKR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 70 LRKIGSI-------------IEEpplykNLS-AYDNMKVVTTMLGVSESTI---LPLLNKVGLGdIDKR---PVKQFSLG 129
Cdd:COG1101 79 AKYIGRVfqdpmmgtapsmtIEE-----NLAlAYRRGKRRGLRRGLTKKRRelfRELLATLGLG-LENRldtKVGLLSGG 152
|
170 180
....*....|....*....|....*....
gi 545668914 130 MKQRLGIAISLINSPKLLILDEPTNGLDP 158
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDP 181
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-209 |
3.02e-18 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 80.63 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGrewsrrdlrKIGSIIEEPPLYKNLSAYDNMKVVT 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------EVSVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 97 TMLGVSESTILPLLNKV----GLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFK 172
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIiefsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 545668914 173 SEGMTIMISSHILSEVEHLADFIGFIYEGKIvleKEY 209
Cdd:PRK13546 191 EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL---KDY 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-183 |
3.63e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.46 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSI------IFEGREWSRRDLRKIG 74
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepIRRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 siiEEPPLYKNLSAYDNMKVVTTMLG-VSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPT 153
Cdd:PRK13538 81 ---HQPGIKTELTALENLRFYQRLHGpGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 545668914 154 NGLDPIGIQELREIIESFKSEGMTIMISSH 183
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-183 |
5.89e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.12 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD-LRKIGSIIEE 79
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDNMKVVTTMLGV-SESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP 158
Cdd:PRK13543 91 PGLKADLSTLENLHFLCGLHGRrAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170 180
....*....|....*....|....*
gi 545668914 159 IGIQELREIIESFKSEGMTIMISSH 183
Cdd:PRK13543 171 EGITLVNRMISAHLRGGGAALVTTH 195
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-204 |
8.29e-18 |
|
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: 81.40 E-value: 8.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 10 SY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGSIIEEPPL-- 82
Cdd:COG5265 366 GYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQASLRAaIGIVPQDTVLfn 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 ---YKNLsAYDNmkvvttmLGVSESTI---------------LP--LLNKVGlgdidKRPVKqFSLGMKQRLGIAISLIN 142
Cdd:COG5265 446 dtiAYNI-AYGR-------PDASEEEVeaaaraaqihdfiesLPdgYDTRVG-----ERGLK-LSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 143 SPKLLILDEPTNGLDPI---GIQ-ELREIiesfkSEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:COG5265 512 NPPILIFDEATSALDSRterAIQaALREV-----ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.74 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRT-----ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW-----SRRDLR 71
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 KIGSIIEEPPLYKNLSaydNMKVVTTMLGVS---------ESTILP----------------------LLNKVGLgDIDK 120
Cdd:PRK13651 83 VLEKLVIQKTRFKKIK---KIKEIRRRVGVVfqfaeyqlfEQTIEKdiifgpvsmgvskeeakkraakYIELVGL-DESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 121 RPVKQFSL--GMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFI 198
Cdd:PRK13651 159 LQRSPFELsgGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250 260
....*....|....*....|....*...
gi 545668914 199 YEGKIVlekeYDGsENLEELFNNQILFE 226
Cdd:PRK13651 239 KDGKII----KDG-DTYDILSDNKFLIE 261
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-204 |
1.21e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.95 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNL----KKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSK----TSGSIIFEGREWS------ 66
Cdd:COG4170 3 LLDIRNLtieiDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLklspre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 67 RRDL--RKIGSIIEEPplyknLSAYDNMKVVTTMLgvSES-------------------TILPLLNKVGLGDiDKRPVK- 124
Cdd:COG4170 83 RRKIigREIAMIFQEP-----SSCLDPSAKIGDQL--IEAipswtfkgkwwqrfkwrkkRAIELLHRVGIKD-HKDIMNs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 125 ---QFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIG-IQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYE 200
Cdd:COG4170 155 yphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTqAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYC 234
|
....
gi 545668914 201 GKIV 204
Cdd:COG4170 235 GQTV 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-204 |
1.45e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 12 GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRK-IGSIIEEPPLYkNLS 87
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRnIAVVFQDAGLF-NRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 88 AYDNMKVVTTmlGVSESTILPLLNKVGLGD-IDKRPVK----------QFSLGMKQRLGIAISLINSPKLLILDEPTNGL 156
Cdd:PRK13657 425 IEDNIRVGRP--DATDEEMRAAAERAQAHDfIERKPDGydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 157 DPIGIQELREIIESFkSEGMTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:PRK13657 503 DVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-224 |
1.55e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.54 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 6 NLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREW----SRRDLRKIGSII-EEP 80
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGISMVhQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAYDNM---KVVTTMLGVSESTIL----PLLNKVGLgDIDKR-PVKQFSLGMKQRLGIAISLINSPKLLILDEP 152
Cdd:PRK10982 83 NLVLQRSVMDNMwlgRYPTKGMFVDQDKMYrdtkAIFDELDI-DIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 153 TNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlekeydGSENLEELFNNQIL 224
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI------ATQPLAGLTMDKII 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-213 |
3.33e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLkksyGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLR-----KIGS 75
Cdd:COG1129 256 VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairaGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IieepP-------LYKNLSAYDNMkvvttmlgvsestILPLLNKVG-LGDIDKR----------------------PVKQ 125
Cdd:COG1129 332 V----PedrkgegLVLDLSIRENI-------------TLASLDRLSrGGLLDRRreralaeeyikrlriktpspeqPVGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 126 FSLGMKQRLGIAISLINSPKLLILDEPTNGLDpIG-IQELREIIESFKSEGMTI-MISSHiLSEVEHLADFIGFIYEGKI 203
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VGaKAEIYRLIRELAAEGKAViVISSE-LPELLGLSDRILVMREGRI 472
|
250
....*....|
gi 545668914 204 VleKEYDGSE 213
Cdd:COG1129 473 V--GELDREE 480
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-206 |
3.73e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRT---ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL----RKI 73
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlrRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPP-LYKNLSAYDNMKVVTTMLGVSESTILPLLNK----VGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK13642 84 GMVFQNPDnQFVGATVEDDVAFGMENQGIPREEMIKRVDEallaVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHlADFIGFIYEGKIVLE 206
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-204 |
4.17e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.43 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKkSYGKRTILNNVNMNIPKGKVYALIGPNGAGKS----TIMKILTGLVSKTSGSIIFEGREWSRRDLR--KIGS 75
Cdd:PRK10418 5 IELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRgrKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPlyknlSAYD---NMK--VVTTMLGV----SESTILPLLNKVGLGDiDKRPVK----QFSLGMKQRLGIAISLIN 142
Cdd:PRK10418 84 IMQNPR-----SAFNplhTMHthARETCLALgkpaDDATLTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESF-KSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-204 |
4.60e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.38 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGK-RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDLRKIGSIIEE 79
Cdd:PRK10790 343 IDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsSLSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PPLYKNLSAYDNmkvVTTMLGVSESTILPLLNKVGLGD--------IDKRPVKQ---FSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK10790 423 DPVVLADTFLAN---VTLGRDISEEQVWQALETVQLAElarslpdgLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 149 LDEPTNGLDP---IGIQE-LREIiesfkSEGMTIMISSHILSE-VEhlADFIGFIYEGKIV 204
Cdd:PRK10790 500 LDEATANIDSgteQAIQQaLAAV-----REHTTLVVIAHRLSTiVE--ADTILVLHRGQAV 553
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-204 |
5.22e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.99 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTG--LVSKTSGSIIFEGRewsrrdlrkigSIIE 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE-----------SILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 -EPPLYKNLSAYDNMKVVTTMLGVSESTILPL-----LNKVGLGDID----------------------KRPVKQ-FSLG 129
Cdd:CHL00131 76 lEPEERAHLGIFLAFQYPIEIPGVSNADFLRLaynskRKFQGLPELDplefleiineklklvgmdpsflSRNVNEgFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 130 MKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLA-DFIGFIYEGKIV 204
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKII 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-227 |
5.82e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKRT-----ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR--------RDL 70
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikevKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKIGSIIEEPPLYKNLSAYDNMKVVTTMLGVSEST------ILPLLNKVGLG-DIDKRPVKQFSLGMKQRLGIAISLINS 143
Cdd:PRK13645 89 RKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKqeaykkVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 144 PKLLILDEPTNGLDPIGIQELREIIESF-KSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLEkeydGSENleELFNNQ 222
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI----GSPF--EIFSNQ 242
|
....*
gi 545668914 223 ILFEK 227
Cdd:PRK13645 243 ELLTK 247
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-204 |
8.45e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.15 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR------RDLR--KIGSIIEEPPLYKNLSA 88
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRrkKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 89 YDNMKVVTTMLGVS----ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQEL 164
Cdd:PRK10070 124 LDNTAFGMELAGINaeerREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545668914 165 R-EIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK10070 204 QdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-157 |
1.29e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.59 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYG----KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD------L 70
Cdd:PRK10584 6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 R--KIGSIIEEPPLYKNLSAYDNMKVVTTMLGVSE----STILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSP 144
Cdd:PRK10584 86 RakHVGFVFQSFMLIPTLNALENVELPALLRGESSrqsrNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170
....*....|...
gi 545668914 145 KLLILDEPTNGLD 157
Cdd:PRK10584 166 DVLFADEPTGNLD 178
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-183 |
6.47e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.14 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIifegrewsrrdlrKIGSIIEEPPLY 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------------HCGTKLEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 84 KNLSAYDNMKVVTTMLGVSESTIlpLLNKVG------LGDI---DKR---PVKQFSLGMKQRLGIAISLINSPKLLILDE 151
Cdd:PRK11147 389 QHRAELDPEKTVMDNLAEGKQEV--MVNGRPrhvlgyLQDFlfhPKRamtPVKALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|..
gi 545668914 152 PTNGLDPIGIQELREIIESFKSegmTIMISSH 183
Cdd:PRK11147 467 PTNDLDVETLELLEELLDSYQG---TVLLVSH 495
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-203 |
6.91e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 6.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGSIIEEPP---LYKNLSA 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 89 YDNMKVvttmlgvsesTILPLLNKVGlGDIDKR----------------------PVKQFSLGMKQRLGIAISLINSPKL 146
Cdd:PRK10762 348 KENMSL----------TALRYFSRAG-GSLKHAdeqqavsdfirlfniktpsmeqAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 147 LILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-210 |
1.07e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.22 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVS--KTSGSII----------------FEGR 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 64 E---------------WS-----RRDLRKIGSIIeeppLYKNLSAYDNMKVVTTMLGVSEST----------ILPLLNKV 113
Cdd:TIGR03269 81 PcpvcggtlepeevdfWNlsdklRRRIRKRIAIM----LQRTFALYGDDTVLDNVLEALEEIgyegkeavgrAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 114 GLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELRE-IIESFKSEGMTIMISSHILSEVEHLA 192
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*...
gi 545668914 193 DFIGFIYEGKIVLEKEYD 210
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPD 254
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-204 |
1.39e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.39 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTI----LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSkTSGSIIFEGREWSRRDLRKIGS- 75
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLQRISEk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 ------------IIEEP-----PLYKnlSAYDNMKVVTTMLGVSEST----ILPLLNKVGLGD----IDKRPvKQFSLGM 130
Cdd:PRK11022 82 errnlvgaevamIFQDPmtslnPCYT--VGFQIMEAIKVHQGGNKKTrrqrAIDLLNQVGIPDpasrLDVYP-HQLSGGM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 131 KQRLGIAISLINSPKLLILDEPTNGLD-PIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-212 |
1.75e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTIlnNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRR--DLRKIGSIIE 78
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 79 EPPLYKNLSAYDNMKvvttmLGVS---------ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:PRK10771 79 ENNLFSHLTVAQNIG-----LGLNpglklnaaqREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVlekeYDGS 212
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIA----WDGP 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-181 |
1.89e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.82 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSI-----IFEGR------EWSRRD 69
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgIKLGYfaqhqlEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 70 lrkigsiieEPPLyknlsaydnMKVVTTMLGVSESTILPLLNKVGL-GDIDKRPVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK10636 392 ---------ESPL---------QHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190
....*....|....*....|....*....|...
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFksEGMTIMIS 181
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDF--EGALVVVS 484
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-220 |
1.95e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 15 TILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREwSRRDLRKigSII------EE-----PPLY 83
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQK--NLVayvpqsEEvdwsfPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 84 KN---LSAYDNMKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIG 160
Cdd:PRK15056 98 EDvvmMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 161 IQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIyEGKIVLEKEYDGS---ENLEELFN 220
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTftaENLELAFS 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-218 |
2.68e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.91 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLK-KSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRK--IGS 75
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitgLSPRERRRlgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPP---LYKNLSAYDNMkvvttMLGVSESTIL---PLLNK---------------VGLGDIDkRPVKQFSLGMKQRL 134
Cdd:COG3845 338 IPEDRLgrgLVPDMSVAENL-----ILGRYRRPPFsrgGFLDRkairafaeelieefdVRTPGPD-TPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 135 GIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVleKEYDGSE- 213
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV--GEVPAAEa 489
|
....*
gi 545668914 214 NLEEL 218
Cdd:COG3845 490 TREEI 494
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-203 |
3.08e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 19 NVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL--------------RKIGSIIEEPPLYK 84
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvylpedRQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 85 NLSA--YDNMKVVTTmlGVSESTILP----LLNkVGLGDIDKrPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP 158
Cdd:PRK15439 361 NVCAltHNRRGFWIK--PARENAVLEryrrALN-IKFNHAEQ-AARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545668914 159 IGIQELREIIESFKSEGMTI-MISSHiLSEVEHLADFIGFIYEGKI 203
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVlFISSD-LEEIEQMADRVLVMHQGEI 481
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-210 |
9.94e-15 |
|
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: 72.46 E-value: 9.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYG-KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRKIGSII 77
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKNLSAYDNMkVVTTMLGVSESTILPLLNKVGL-GDIDKRPV----------KQFSLGMKQRLGIAISLINSPKL 146
Cdd:TIGR01193 554 PQEPYIFSGSILENL-LLGAKENVSQDEIWAACEIAEIkDDIENMPLgyqtelseegSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 147 LILDEPTNGLDPigIQELREIIESFKSEGMTIMISSHILSeVEHLADFIGFIYEGKIVLEKEYD 210
Cdd:TIGR01193 633 LILDESTSNLDT--ITEKKIVNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHD 693
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-183 |
1.39e-14 |
|
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: 69.58 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 12 GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGlvSKTSGSIifEGrewsrrDLRKIGSiieepPLYKNL---SA 88
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI--TG------EILINGR-----PLDKNFqrsTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 89 Y-DNMKVVTTMLGVSESTILPLLNKvGLgdidkrpvkqfSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREI 167
Cdd:cd03232 83 YvEQQDVHSPNLTVREALRFSALLR-GL-----------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRF 150
|
170
....*....|....*.
gi 545668914 168 IESFKSEGMTIMISSH 183
Cdd:cd03232 151 LKKLADSGQAILCTIH 166
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-183 |
1.41e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.97 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 10 SYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKT-SGSIIFEGRewsRR-------DL-RKIGsiieep 80
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGR---RRgsgetiwDIkKHIG------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 plYKNLSAYDNMKVVTTMLGVsestILP----------------------LLNKVGLGD-IDKRPVKQFSLGmKQRLG-I 136
Cdd:PRK10938 340 --YVSSSLHLDYRVSTSVRNV----ILSgffdsigiyqavsdrqqklaqqWLDILGIDKrTADAPFHSLSWG-QQRLAlI 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545668914 137 AISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMT--IMISSH 183
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSHH 461
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-157 |
1.48e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 7 LKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSkTSGSIIFEGR---EWSRRDL----RKIGSIIEE 79
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQplhNLNRRQLlpvrHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 80 PplYKNLSAYDNM-KVVTTMLGV---------SESTILPLLNKVGLgDIDKR---PvKQFSLGMKQRLGIAISLINSPKL 146
Cdd:PRK15134 371 P--NSSLNPRLNVlQIIEEGLRVhqptlsaaqREQQVIAVMEEVGL-DPETRhryP-AEFSGGQRQRIAIARALILKPSL 446
|
170
....*....|.
gi 545668914 147 LILDEPTNGLD 157
Cdd:PRK15134 447 IILDEPTSSLD 457
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-229 |
1.63e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 72.12 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG--------REWSRRDLRK 72
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 IGSIIEEPPLYKNLSA-------YDNMKVVTTMLG----VSESTILP----LLNKVGLGDID-KRPVKQFSLGMKQRLGI 136
Cdd:PRK10636 81 LEYVIDGDREYRQLEAqlhdaneRNDGHAIATIHGkldaIDAWTIRSraasLLHGLGFSNEQlERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 137 AISLINSPKLLILDEPTNGLDPIGIQELREIIESFksEGMTIMISshilseveHLADFIGFIYEGKIVLEKeydgsENLE 216
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILIS--------HDRDFLDPIVDKIIHIEQ-----QSLF 225
|
250
....*....|...
gi 545668914 217 ELFNNQILFEKRR 229
Cdd:PRK10636 226 EYTGNYSSFEVQR 238
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-215 |
1.75e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.99 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNL----KKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGlVSK-----TSGSIIFEGREW---SRR 68
Cdd:PRK15093 3 LLDIRNLtiefKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKdnwrvTADRMRFDDIDLlrlSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 69 DLRK-----IGSIIEEPPLYKNLSAYDNMKVVTTMLGVS------------ESTILPLLNKVGLGD---IDKRPVKQFSL 128
Cdd:PRK15093 82 ERRKlvghnVSMIFQEPQSCLDPSERVGRQLMQNIPGWTykgrwwqrfgwrKRRAIELLHRVGIKDhkdAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 129 GMKQRLGIAISLINSPKLLILDEPTNGLDPIG-IQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVlek 207
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTqAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV--- 238
|
....*...
gi 545668914 208 EYDGSENL 215
Cdd:PRK15093 239 ETAPSKEL 246
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-186 |
2.54e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.30 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 5 QNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIifegrewsrrdlrKIGSIIEEPPLYK 84
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-------------KIGETVKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 85 NLSAYDNMKVVTTMlgVSEST-ILpllnKVGLGDIDKR---------------PVKQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:PRK11819 395 SRDALDPNKTVWEE--ISGGLdII----KVGNREIPSRayvgrfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545668914 149 LDEPTNGLDPIGIQELREIIESFKseGMTIMIS----------SHILS 186
Cdd:PRK11819 469 LDEPTNDLDVETLRALEEALLEFP--GCAVVIShdrwfldriaTHILA 514
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-227 |
2.93e-14 |
|
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: 71.48 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY--GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSkTSGSIIFEGREWSRRDL---RKIGSI 76
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLqtwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEP------PLYKNLSAYDNMkvvttmlgvSESTILPLLNKVGLgdidKRPVKQF---------------SLGMKQRLG 135
Cdd:TIGR01271 1297 IPQKvfifsgTFRKNLDPYEQW---------SDEEIWKVAEEVGL----KSVIEQFpdkldfvlvdggyvlSNGHKQLMC 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 136 IAISLINSPKLLILDEPTNGLDPIGIQELREII-ESFKSegMTIMISSHilsEVEHLADFIGF-IYEGKIVleKEYDgse 213
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSN--CTVILSEH---RVEALLECQQFlVIEGSSV--KQYD--- 1433
|
250
....*....|....
gi 545668914 214 NLEELFNNQILFEK 227
Cdd:TIGR01271 1434 SIQKLLNETSLFKQ 1447
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-204 |
3.47e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG---REWSRRDLRKIGSIIEEPPLYKNLSAYDNMK 93
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRNQVALVSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 94 VVTTMLGVSESTI--------LPLLNKV--GLGDIDKRPVKQFSLGMKQRLGIAISLI-NSPkLLILDEPTNGLD---PI 159
Cdd:PRK11176 439 YARTEQYSREQIEeaarmayaMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLrDSP-ILILDEATSALDtesER 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545668914 160 GIQELREIIESFKsegmTIMISSHILSEVEHlADFIGFIYEGKIV 204
Cdd:PRK11176 518 AIQAALDELQKNR----TSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-210 |
3.84e-14 |
|
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: 68.59 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKR--TILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL----RKIGS 75
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLedlrSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLY-----KNLSAYDNM--KVVTTMLGVSEStilpllnkvGLgdidkrpvkQFSLGMKQRLGIAISLINSPKLLI 148
Cdd:cd03369 87 IPQDPTLFsgtirSNLDPFDEYsdEEIYGALRVSEG---------GL---------NLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 149 LDEPTNGLDPIGIQELREII-ESFKseGMTIMISSHILSEVehlADF--IGFIYEGKIvleKEYD 210
Cdd:cd03369 149 LDEATASIDYATDALIQKTIrEEFT--NSTILTIAHRLRTI---IDYdkILVMDAGEV---KEYD 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-157 |
6.23e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.87 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR-----EWSRRDlrkIG 74
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelEPADRD---IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 SIIEEPPLYKNLSAYDNM----KVVttmlGVSESTILPLLNKV----GLGD-IDKRPvKQFSLGMKQR--LGIAIslINS 143
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMayglKIR----GMPKAEIEERVAEAarilELEPlLDRKP-RELSGGQRQRvaMGRAI--VRE 152
|
170
....*....|....
gi 545668914 144 PKLLILDEPTNGLD 157
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-217 |
8.87e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.28 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGL--VSKTSGSIIFEGREW-----SRRDLRKI 73
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLlelspEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 74 GSIIEEPPLYKNLSayDNMKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQ---------------FSLGMKQRLGIAI 138
Cdd:PRK09580 81 FMAFQYPVEIPGVS--NQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgFSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 139 SLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSH---ILSEVEhlADFIGFIYEGKIVLEKEYDGSENL 215
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHyqrILDYIK--PDYVHVLYQGRIVKSGDFTLVKQL 236
|
..
gi 545668914 216 EE 217
Cdd:PRK09580 237 EE 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-206 |
1.29e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.27 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR-------RDLRK-IGSIIE--EPPLYKnl 86
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyiRPVRKrIGMVFQfpESQLFE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 87 sayDNM--------KVVTTMLGVSESTILPLLNKVGLG-DIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:PRK13646 101 ---DTVereiifgpKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545668914 158 PIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-157 |
1.92e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 14 RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR---EWSRRDL-RKIGSiieeppLYKNLSAY 89
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleSWSSKAFaRKVAY------LPQQLPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 90 DNMKVVTTM----------LG---------VSESTILpllnkVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:PRK10575 98 EGMTVRELVaigrypwhgaLGrfgaadrekVEEAISL-----VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
....*..
gi 545668914 151 EPTNGLD 157
Cdd:PRK10575 173 EPTSALD 179
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-204 |
2.14e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTIL---------NNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR-----EWS 66
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 67 RRDLR----------------KIGSIIEEP-PLYKNLSAYDNmkvvttmlgvsESTILPLLNKVGL-GDIDKRPVKQFSL 128
Cdd:PRK15112 84 YRSQRirmifqdpstslnprqRISQILDFPlRLNTDLEPEQR-----------EKQIIETLRQVGLlPDHASYYPHMLAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 129 GMKQRLGIAISLINSPKLLILDEPTNGLD-PIGIQELREIIESFKSEGMT-IMISSHiLSEVEHLADFIGFIYEGKIV 204
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQGISyIYVTQH-LGMMKHISDQVLVMHQGEVV 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-227 |
2.26e-13 |
|
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: 67.57 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSY--GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSkTSGSIIFEGREWSRRDL---RKIGSI 76
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLqkwRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEP------PLYKNLSAYDNMkvvttmlgvSESTILPLLNKVGLgdidKRPVKQF---------------SLGMKQRLG 135
Cdd:cd03289 82 IPQKvfifsgTFRKNLDPYGKW---------SDEEIWKVAEEVGL----KSVIEQFpgqldfvlvdggcvlSHGHKQLMC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 136 IAISLINSPKLLILDEPTNGLDPIGIQELREII-ESFKseGMTIMISSHILSEVEHLADFIgFIYEGKIvleKEYDgseN 214
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFA--DCTVILSEHRIEAMLECQRFL-VIEENKV---RQYD---S 219
|
250
....*....|...
gi 545668914 215 LEELFNNQILFEK 227
Cdd:cd03289 220 IQKLLNEKSHFKQ 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-193 |
2.26e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.38 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---------WSRRDLR 71
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErlgklrqdqFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 72 KIGSII-----------EEPPLYKN--LSAYDNMKV------VTTMLGVS-ESTILPLLNKVGLG-DIDKRPVKQFSLGM 130
Cdd:PRK15064 81 VLDTVImghtelwevkqERDRIYALpeMSEEDGMKVadlevkFAEMDGYTaEARAGELLLGVGIPeEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 131 KQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSegmTIMISSH---ILSEV-EHLAD 193
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS---TMIIISHdrhFLNSVcTHMAD 224
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-204 |
2.44e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.38 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIifegrEWSrrDLRKIG------- 74
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWS--ENANIGyyaqdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 75 -SIIEEPPLYKNLSAY----DNMKVVTTMLGvsestilPLLnkVGLGDIdKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:PRK15064 393 yDFENDLTLFDWMSQWrqegDDEQAVRGTLG-------RLL--FSQDDI-KKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 150 DEPTNGLDPIGIQELREIIESFKSegmTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK15064 463 DEPTNHMDMESIESLNMALEKYEG---TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
2.50e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.33 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLK-KSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTsGSIIFEGREWSRRDL----RKIGSI 76
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPeswrKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNlSAYDNMkvvttMLG---VSESTILPLLNKVGLGDIDKR-------PVKQ----FSLGMKQRLGIAISLIN 142
Cdd:PRK11174 429 GQNPQLPHG-TLRDNV-----LLGnpdASDEQLQQALENAWVSEFLPLlpqgldtPIGDqaagLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 143 SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMIsSHILSEVEHLaDFIGFIYEGKIVLEKEYdgsenlEELFNNQ 222
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMV-THQLEDLAQW-DQIWVMQDGQIVQQGDY------AELSQAG 574
|
...
gi 545668914 223 ILF 225
Cdd:PRK11174 575 GLF 577
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-157 |
4.40e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 4 IQNLKKSY-GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKtsgsiiFEGREWSRRDLrKIGSIIEEPPL 82
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARPQPGI-KVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 YKNLSAYDNMkvvttMLGVSEstILPLLNK-------------------------------VGLGDIDKR---------- 121
Cdd:TIGR03719 80 DPTKTVRENV-----EEGVAE--IKDALDRfneisakyaepdadfdklaaeqaelqeiidaADAWDLDSQleiamdalrc 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545668914 122 -----PVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:TIGR03719 153 ppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-204 |
1.63e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 19 NVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRewsRRDL----------RKIGSIIEEPplYKNL-- 86
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ---RIDTlspgklqalrRDIQFIFQDP--YASLdp 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 87 ------SAYDNMKVVTTMLG-VSESTILPLLNKVGL-GDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD- 157
Cdd:PRK10261 417 rqtvgdSIMEPLRVHGLLPGkAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDv 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545668914 158 PIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-228 |
1.96e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEgrewsrRDL---------- 70
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE------QDLivarlqqdpp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKI-GSI------------------------IEEPPLYKNLSaydNMKVVTTMLGVS-----ESTILPLLNKVGLgDIDK 120
Cdd:PRK11147 77 RNVeGTVydfvaegieeqaeylkryhdishlVETDPSEKNLN---ELAKLQEQLDHHnlwqlENRINEVLAQLGL-DPDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 121 rPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKseGMTIMIsSHILSEVEHLADFIGFIYE 200
Cdd:PRK11147 153 -ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIFI-SHDRSFIRNMATRIVDLDR 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 545668914 201 GKIV----------LEKEydgsENL--EELFNNQilFEKR 228
Cdd:PRK11147 229 GKLVsypgnydqylLEKE----EALrvEELQNAE--FDRK 262
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-183 |
1.99e-12 |
|
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: 62.94 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 14 RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREwsrrdlrkigsiieepplyknlsaydnmk 93
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 94 vvtTMLGVSESTILPLLNkvgLGDIDKRP-VKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPigiQELREIIESFK 172
Cdd:cd03223 65 ---DLLFLPQRPYLPLGT---LREQLIYPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE---ESEDRLYQLLK 135
|
170
....*....|.
gi 545668914 173 SEGMTIMISSH 183
Cdd:cd03223 136 ELGITVISVGH 146
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-224 |
2.56e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.90 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIqNLKKSYGKRTIlnNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDL--------RK 72
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclppekRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 73 IGSIIEEPPLYKNLSAYDNMKvvttmLGVSEST------ILPLLnkvGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKL 146
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLR-----YGMAKSMvaqfdkIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 147 LILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIVLekeydgSENLEELFNNQIL 224
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKA------FGPLEEVWASSAM 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-198 |
4.67e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 21 NMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSIIEEPPLYKN---LSAYDNMKVVTT 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNtdmLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 98 ----MLGVSESTI-LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFK 172
Cdd:PRK10938 103 aeiiQDEVKDPARcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH 182
|
170 180
....*....|....*....|....*.
gi 545668914 173 SEGMTIMIsshILSEVEHLADFIGFI 198
Cdd:PRK10938 183 QSGITLVL---VLNRFDEIPDFVQFA 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-158 |
6.23e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.44 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 14 RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIfegrewsRRDLRKI-----------GSIieeppl 82
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-------RPAGARVlflpqrpylplGTL------ 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 yKNLSAYDNmkvvtTMLGVSESTILPLLNKVGLGDIDKRP------VKQFSLGMKQRLGIAISLINSPKLLILDEPTNGL 156
Cdd:COG4178 443 -REALLYPA-----TAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
..
gi 545668914 157 DP 158
Cdd:COG4178 517 DE 518
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-157 |
8.21e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 5 QNLKKSYG-KRTILNNVNMN-IPKGKVyALIGPNGAGKSTIMKILTGLVSKtsgsiiFEGREWSRRDLrKIGSIIEEPPL 82
Cdd:PRK11819 10 NRVSKVVPpKKQILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKE------FEGEARPAPGI-KVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 YKNLSAYDNMkvvttMLGVSEST-ILPLLNKV----------------------------GLGDIDKR------------ 121
Cdd:PRK11819 82 DPEKTVRENV-----EEGVAEVKaALDRFNEIyaayaepdadfdalaaeqgelqeiidaaDAWDLDSQleiamdalrcpp 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 545668914 122 ---PVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:PRK11819 157 wdaKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-186 |
5.96e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 12 GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSI---------IFEGREWSRRDLRkigsiiEEPPL 82
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLDLS------SNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 83 YknlsaydnmkVVTTMLGVSESTILPLLNKVGL-GDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGI 161
Cdd:PLN03073 594 Y----------MMRCFPGVPEQKLRAHLGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV 663
|
170 180
....*....|....*....|....*..
gi 545668914 162 QELREIIESFksEGMTIMIS--SHILS 186
Cdd:PLN03073 664 EALIQGLVLF--QGGVLMVShdEHLIS 688
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-183 |
7.29e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTI-LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWS---RRDLRK-IGSI 76
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeqPEDYRKlFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 IEEPPLYKNLSAYDNmKVVTTMLGVSESTILPLLNKVGLGDiDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGL 156
Cdd:PRK10522 403 FTDFHLFDQLLGPEG-KPANPALVEKWLERLKMAHKLELED-GRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180
....*....|....*....|....*...
gi 545668914 157 DPIGIQEL-REIIESFKSEGMTIMISSH 183
Cdd:PRK10522 481 DPHFRREFyQVLLPLLQEMGKTIFAISH 508
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-157 |
7.29e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 12 GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKIL-----TGLVskTSGSIIFEGREWSRRDLRKIG-----------S 75
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRSIGyvqqqdlhlptS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEEPPLY-------KNLSAYDNMKVVTTMLGVSESTIL--PLLNKVGLGdidkrpvkqFSLGMKQRLGIAISLINSPKL 146
Cdd:TIGR00956 852 TVRESLRFsaylrqpKSVSKSEKMEYVEEVIKLLEMESYadAVVGVPGEG---------LNVEQRKRLTIGVELVAKPKL 922
|
170
....*....|..
gi 545668914 147 LI-LDEPTNGLD 157
Cdd:TIGR00956 923 LLfLDEPTSGLD 934
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-190 |
1.14e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRT---ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR--------EWSRrdl 70
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlKWWR--- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 71 RKIGSIIEEPPLYKN---------------------------LSAYDNMK---------------VVTTMLG-------- 100
Cdd:PTZ00265 460 SKIGVVSQDPLLFSNsiknnikyslyslkdlealsnyynedgNDSQENKNkrnscrakcagdlndMSNTTDSneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 101 ----VSESTILPLLNKVGLGD-IDKRPVK----------QFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELR 165
Cdd:PTZ00265 540 nyqtIKDSEVVDVSKKVLIHDfVSALPDKyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260
....*....|....*....|....*.
gi 545668914 166 EIIESFK-SEGMTIMISSHILSEVEH 190
Cdd:PTZ00265 620 KTINNLKgNENRITIIIAHRLSTIRY 645
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-206 |
1.59e-10 |
|
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: 58.10 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTImkiltglvsktsgsiIFEGREWSRRDLrkigsiieeppLYKNLSAYDNMKVVt 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---------------VNEGLYASGKAR-----------LISFLPKFSRNKLI- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 97 tMLGVsestiLPLLNKVGLGDID-KRPVKQFSLGMKQRLGIAISLINSPK--LLILDEPTNGLDPIGIQELREIIESFKS 173
Cdd:cd03238 64 -FIDQ-----LQFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLID 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 545668914 174 EGMTIMISSHILsEVEHLADFIGFI------YEGKIVLE 206
Cdd:cd03238 138 LGNTVILIEHNL-DVLSSADWIIDFgpgsgkSGGKVVFS 175
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-204 |
2.50e-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: 58.04 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 8 KKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVS---KTSGSIIFEGREWSRRDLRKIGSII---EEPP 81
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKYPGEIIyvsEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 82 LYKNLSAYDNMKVVTTMLGvsestilpllNKVglgdidkrpVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGI 161
Cdd:cd03233 94 HFPTLTVRETLDFALRCKG----------NEF---------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545668914 162 QELREIIESF-KSEGMTIMISSHILS-EVEHLADFIGFIYEGKIV 204
Cdd:cd03233 155 LEILKCIRTMaDVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-157 |
5.34e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTiLNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR-----EWSRRD------ 69
Cdd:PRK13409 340 LVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpQYIKPDydgtve 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 70 --LRKIGSIIEEPPLYknlsaydnmkvvttmlgvSEstilpLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLL 147
Cdd:PRK13409 419 dlLRSITDDLGSSYYK------------------SE-----IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170
....*....|
gi 545668914 148 ILDEPTNGLD 157
Cdd:PRK13409 476 LLDEPSAHLD 485
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-199 |
7.68e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 24 IPK-GKVYALIGPNGAGKSTIMKILTG-----------------LVSKTSGSII---FEG-REWSRRDLRKIGSIIEEPP 81
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdeVLKRFRGTELqnyFKKlYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 82 LYKNlsaydnmKVVTTMLGVSESTIL-PLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDpIG 160
Cdd:PRK13409 175 VFKG-------KVRELLKKVDERGKLdEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-IR 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545668914 161 --------IQELreiiesfkSEGMTIMISSHILSEVEHLADFIGFIY 199
Cdd:PRK13409 247 qrlnvarlIREL--------AEGKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-204 |
9.85e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 19 NVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSI-------------IFEGREWSRRDLRK-----IGSIIEEP 80
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHvrgadMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 ------------------PLYKNLSAYDNMKVVTTMLG---VSES-TILpllnkvglgdidKRPVKQFSLGMKQRLGIAI 138
Cdd:PRK10261 114 mtslnpvftvgeqiaesiRLHQGASREEAMVEAKRMLDqvrIPEAqTIL------------SRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 139 SLINSPKLLILDEPTNGLDpIGIQ-ELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALD-VTIQaQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-215 |
1.06e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 25 PKGKVyALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR---RDLRKIGSIIEEPPLYKNLSAYDNMKVVTTMlgv 101
Cdd:PLN03232 1261 PSEKV-GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfglTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEH--- 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 102 SESTILPLLNKVGLGD-IDKRPV----------KQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDpIGIQEL--REII 168
Cdd:PLN03232 1337 NDADLWEALERAHIKDvIDRNPFgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVD-VRTDSLiqRTIR 1415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545668914 169 ESFKSegMTIMISSHILSEVEHlADFIGFIYEGKIVlekEYDGSENL 215
Cdd:PLN03232 1416 EEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVL---EYDSPQEL 1456
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
51-189 |
1.15e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 51 VSKTSGSIIFEGR---EWSRRDLRKIGSIIEEPPLYKNLSAYDNMKV------------VTTMLGVSEsTILPLLNKVgl 115
Cdd:PTZ00265 1272 VFKNSGKILLDGVdicDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFgkedatredvkrACKFAAIDE-FIESLPNKY-- 1348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545668914 116 gDIDKRPV-KQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEG-MTIMISSHILSEVE 189
Cdd:PTZ00265 1349 -DTNVGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIK 1423
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-203 |
1.22e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 13 KRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLV-SKTSGSIIFEGREWSRRDL--------------RKIGSII 77
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNPaqairagiamvpedRKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKN--LSAYDNMKVVTTM-----LGVSESTILPLLNKVGLGDIdkrPVKQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:TIGR02633 352 PILGVGKNitLSVLKSFCFKMRIdaaaeLQIIGSAIQRLKVKTASPFL---PIGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545668914 151 EPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-199 |
1.83e-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: 57.10 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 24 IPK-GKVYALIGPNGAGKSTIMKILTGL-----------------VSKTSGSIIFEgrewsrrDLRKI--GSI------- 76
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswdevLKRFRGTELQD-------YFKKLanGEIkvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 77 -IEEPPLYKN------LSAYDNMKVVTTmlgvsestilpLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLIL 149
Cdd:COG1245 168 yVDLIPKVFKgtvrelLEKVDERGKLDE-----------LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545668914 150 DEPTNGLDpIGiQELR--EIIESFKSEGMTIMISSHILSEVEHLADFIGFIY 199
Cdd:COG1245 237 DEPSSYLD-IY-QRLNvaRLIRELAEEGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-186 |
3.33e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 14 RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR---RDLRKIGSIIEEPPLYKNLSAYD 90
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqlDSWRSRLAVVSQTPFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 91 NMKvvttmLGVSEST----------------ILPL----LNKVGlgdidKRPVkQFSLGMKQRLGIAISLINSPKLLILD 150
Cdd:PRK10789 408 NIA-----LGRPDATqqeiehvarlasvhddILRLpqgyDTEVG-----ERGV-MLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190
....*....|....*....|....*....|....*...
gi 545668914 151 EPTNGLDpiGIQElREIIESFKS--EGMTIMISSHILS 186
Cdd:PRK10789 477 DALSAVD--GRTE-HQILHNLRQwgEGRTVIISAHRLS 511
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-215 |
4.04e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 16 ILNNVNMNI-PKGKVyALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSR---RDLRKIGSIIEEPP-LYK-----N 85
Cdd:PLN03130 1254 VLHGLSFEIsPSEKV-GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglMDLRKVLGIIPQAPvLFSgtvrfN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 86 LSAYDNMkvvttmlgvSESTILPLLNKVGLGDIDKRPVK-----------QFSLGMKQRLGIAISLINSPKLLILDEPTN 154
Cdd:PLN03130 1333 LDPFNEH---------NDADLWESLERAHLKDVIRRNSLgldaevseageNFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 155 GLDpIGIQEL--REIIESFKSegMTIMISSHILSEVEHlADFIGFIYEGKIVlekEYDGSENL 215
Cdd:PLN03130 1404 AVD-VRTDALiqKTIREEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVV---EFDTPENL 1459
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
122-203 |
5.06e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 122 PVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMT-IMISSHiLSEVEHLADFIGFIYE 200
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAiIVISSE-LPEVLGLSDRVLVMHE 480
|
...
gi 545668914 201 GKI 203
Cdd:PRK13549 481 GKL 483
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-63 |
5.22e-09 |
|
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: 54.40 E-value: 5.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 545668914 16 ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR 63
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-189 |
8.42e-09 |
|
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: 54.62 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKsygkrtiLNNVNMNIPKGKVyALIGPNGAGKSTIMKILTgLVSKTSGSIIFEGREWSRRD------------ 69
Cdd:COG3593 6 IKIKNFRS-------IKDLSIELSDDLT-VLVGENNSGKSSILEALR-LLLGPSSSRKFDEEDFYLGDdpdlpeieielt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 70 ----LRKIGSIIEEPPLYKNLSA------------------------YDNMKVVTTMLGVSESTILPLLN--KVGLGDID 119
Cdd:COG3593 77 fgslLSRLLRLLLKEEDKEELEEaleelneelkealkalnellseylKELLDGLDLELELSLDELEDLLKslSLRIEDGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 120 KRPVKQFSLGMKQRLGIAISLI-------NSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSH---ILSEVE 189
Cdd:COG3593 157 ELPLDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHsphLLSEVP 236
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-199 |
1.34e-08 |
|
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: 53.52 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 24 IPK-GKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGrEWSR--RDLRkiGSIIE---EPPLYKNLSAYDNMKVVTT 97
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPP-DWDEilDEFR--GSELQnyfTKLLEGDVKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 98 MLGVSESTILPLLNKV-------------GLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDpIGiQEL 164
Cdd:cd03236 99 IPKAVKGKVGELLKKKdergkldelvdqlELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD-IK-QRL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 545668914 165 R--EIIESFKSEGMTIMISSHILSEVEHLADFIGFIY 199
Cdd:cd03236 177 NaaRLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-202 |
1.85e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.18 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 23 NIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIifegrEWSRRDLRKIGSIIEepPLYKnLSAYDNMKVVTTMLGVS 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDTVSYKPQYIK--ADYE-GTVRDLLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 103 ESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP----IGIQELREIIESFKSegmTI 178
Cdd:cd03237 93 PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAENNEK---TA 169
|
170 180
....*....|....*....|....
gi 545668914 179 MISSHILSEVEHLADFIgFIYEGK 202
Cdd:cd03237 170 FVVEHDIIMIDYLADRL-IVFEGE 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-157 |
2.09e-08 |
|
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: 54.02 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 24 IPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRewsrrdlrkigsiIEEPPLYknLSAYDNMKVVTTMLGVSE 103
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------ISYKPQY--ISPDYDGTVEEFLRSANT 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 104 STI------LPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:COG1245 428 DDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-204 |
5.65e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVS--------KTSGSIIFEGREWSRRD--- 69
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDapr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 70 ---LRKIGSIIEEPPLYKN------LSAYDNMKVVTTMLGVSESTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISL 140
Cdd:PRK13547 81 larLRAVLPQAAQPAFAFSareivlLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668914 141 ---------INSPKLLILDEPTNGLDPIGIQELREIIESFKSE-GMTIMISSHILSEVEHLADFIGFIYEGKIV 204
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-195 |
8.72e-08 |
|
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: 51.18 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIF-------EGREWSRRDLRKIGSIIEEPPLYKNLSAY 89
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesePSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 90 DNM-----------KVVTTMLGVS-ESTILPLLNKVGLGDidkRPVkQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:cd03290 97 ENItfgspfnkqryKAVTDACSLQpDIDLLPFGDQTEIGE---RGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 545668914 158 PIGIQELRE--IIESFKSEGMTIMISSHILSEVEHlADFI 195
Cdd:cd03290 173 IHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWI 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-227 |
9.60e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 10 SYGKRTILNNVNMNIPKGKVYALIGPNGAGK-STIMKILTGLVSKTSGSIIFEGR-------EW----SRRDLRKIGSII 77
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGTvayvpqvSWifnaTVRDNILFGSPF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 78 EEPPLYKnlsAYDnmkvVTTMlgvseSTILPLLNKVGLGDIDKRPVkQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:PLN03130 706 DPERYER---AID----VTAL-----QHDLDLLPGGDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 158 P-IGIQELREIIESFKSEGMTIMISS--HILSEVehlaDFIGFIYEGKIVLEKEYdgsenlEELFNNQILFEK 227
Cdd:PLN03130 773 AhVGRQVFDKCIKDELRGKTRVLVTNqlHFLSQV----DRIILVHEGMIKEEGTY------EELSNNGPLFQK 835
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-200 |
1.07e-07 |
|
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: 50.68 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 31 ALIGPNGAGKSTIMK----ILTGLVSKTSgsiifEGREWSRRDLRKiGSIIEEPPLYKNLSAYDNMKVVTTMlGVSESTI 106
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyALTGELPPNS-----KGGAHDPKLIRE-GEVRAQVKLAFENANGKKYTITRSL-AILENVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 107 LpllnkVGLGDIDK---RPVKQFSLGMKQ------RLGIAISLINSPKLLILDEPTNGLDPIGIQE-LREIIESFKSEGM 176
Cdd:cd03240 99 F-----CHQGESNWpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKN 173
|
170 180
....*....|....*....|....
gi 545668914 177 TIMIsshILSEVEHLADFIGFIYE 200
Cdd:cd03240 174 FQLI---VITHDEELVDAADHIYR 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-224 |
1.72e-07 |
|
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: 51.45 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 16 ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKI--GSIIEEPPLYKNLSAYDNMK 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWImpGTIKDNIIFGLSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 94 VVTTMLGVSESTILPLLNKVGLGDIDkrpvKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDpigIQELREIIESFKS 173
Cdd:TIGR01271 521 VIKACQLEEDIALFPEKDKTVLGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFTHLD---VVTEKEIFESCLC 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545668914 174 EGMTIMISSHILSEVEHL--ADFIGFIYEGKIVLEKEYDGSENLEELFNNQIL 224
Cdd:TIGR01271 594 KLMSNKTRILVTSKLEHLkkADKILLLHEGVCYFYGTFSELQAKRPDFSSLLL 646
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-203 |
1.88e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.94 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRtiLNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRD----LRK-IGS 75
Cdd:PRK09700 265 VFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldaVKKgMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIE---EPPLYKNLSAYDNMKVVTTMLGVSESTILPLLN-----KVGLGDIDKRPVK---------QFSLGMKQRLGIAI 138
Cdd:PRK09700 343 ITEsrrDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHevdeqRTAENQRELLALKchsvnqnitELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 139 SLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKI 203
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-185 |
6.81e-07 |
|
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: 47.37 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 26 KGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFegrewsrrdlrkigsiieepplyknlsaydnmkvvttmlgVSEST 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------------------------------IDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 106 ILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHIL 185
Cdd:smart00382 41 ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
32-188 |
1.33e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 48.04 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 32 LIGPNGAGKSTIMKILTGLVSktSGSIIF--------EGREWSRRDLRKIGSIIEepPLYKNLSAYDNMKVVTTMLGVSE 103
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLLLQ--SNFIYLpaersgpaRLYPSLVRELSDLGSRGE--YTADFLAELENLEILDDKSKELL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 104 STILPLLNKVGLGDI-------------------DKRPVKQFSLGMKQRLGIAISLINSPK---LLILDEPTNGLDPIGI 161
Cdd:COG4938 101 EQVEEWLEKIFPGKVevdassdlvrlvfrpsgngKRIPLSNVGSGVSELLPILLALLSAAKpgsLLIIEEPEAHLHPKAQ 180
|
170 180 190
....*....|....*....|....*....|
gi 545668914 162 QELREIIESFKSEGMTIMI---SSHILSEV 188
Cdd:COG4938 181 SALAELLAELANSGVQVIIethSDYILNGL 210
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-63 |
1.44e-06 |
|
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: 48.26 E-value: 1.44e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 545668914 20 VNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGR 63
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ 394
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-195 |
1.49e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 1.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668914 121 RPVKQFSLGMKQRLGIAISLINS---PKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEhLADFI 195
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYV 881
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-158 |
1.58e-06 |
|
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: 48.21 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 16 ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGL-------VSKTSGSIIF---EGREWSRRDLRKigSIIeepplYKN 85
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrLTKPAKGKLFyvpQRPYMTLGTLRD--QII-----YPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 86 LSayDNMKvvttMLGVSESTILPLLNKVGLGDIDKRPV---------KQFSLGMKQRLGIAISLINSPKLLILDEPTNGL 156
Cdd:TIGR00954 540 SS--EDMK----RRGLSDKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
..
gi 545668914 157 DP 158
Cdd:TIGR00954 614 SV 615
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-203 |
1.69e-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: 48.40 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEG-------REWSRRD-LRK---IGSIIEEPPLYKN 85
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsvayvpqQAWIQNDsLREnilFGKALNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 86 LSAydnmkvvttmlgvseSTILPLLNKVGLGD---IDKRPVkQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDP-IGI 161
Cdd:TIGR00957 734 LEA---------------CALLPDLEILPSGDrteIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545668914 162 QELREIIesfKSEGM----TIMISSHILSEVEHLaDFIGFIYEGKI 203
Cdd:TIGR00957 798 HIFEHVI---GPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-157 |
2.89e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 27 GKVYALIGPNGAGKSTIMKILTGlvSKTSGSIifEG----------REWSRR--------DLRKIGSIIEEPPLY----- 83
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGdirisgfpkkQETFARisgyceqnDIHSPQVTVRESLIYsaflr 981
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 84 --KNLSAYDNMKVVTTMLGVSEstILPLLNK-VGLGDIDKRPVKQfslgmKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:PLN03140 982 lpKEVSKEEKMMFVDEVMELVE--LDNLKDAiVGLPGVTGLSTEQ-----RKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
116-189 |
4.57e-06 |
|
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: 46.61 E-value: 4.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668914 116 GDIDKRPVKQFSLGMKQRLGIAISLI---NSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVE 189
Cdd:pfam13304 227 GGGGELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-158 |
4.94e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 16 ILNNVNMNI-PKGKVyALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGRE---WSRRDLRKIGSIIEEPPLYKNLSAYDN 91
Cdd:PTZ00243 1325 VLRGVSFRIaPREKV-GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigaYGLRELRRQFSMIPQDPVLFDGTVRQN 1403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545668914 92 mkvVTTMLGVSESTILPLLNKVGL--------GDIDKRPVK---QFSLGMKQRLGIAISLINSPKLLIL-DEPTNGLDP 158
Cdd:PTZ00243 1404 ---VDPFLEASSAEVWAALELVGLrervasesEGIDSRVLEggsNYSVGQRQLMCMARALLKKGSGFILmDEATANIDP 1479
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
5.83e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLKKSYGKRTILNNVNMNIPKGKVYaLIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKIGSIIEEP 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSITFLPSAITY-IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAYDNMKVVTTMLGVSEsTILPLLNKVGLGDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDPIG 160
Cdd:PRK13541 80 GLKLEMTVFENLKFWSEIYNSAE-TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180
....*....|....*....|....*...
gi 545668914 161 IQELREIIESFKSEGMTIMISSHILSEV 188
Cdd:PRK13541 159 RDLLNNLIVMKANSGGIVLLSSHLESSI 186
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
12-193 |
8.34e-06 |
|
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: 44.66 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 12 GKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMK----ILTGLVSKTsgsiifegrewSRRDLRKIGSIieepplyknlS 87
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiglALGGAQSAT-----------RRRSGVKAGCI----------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 88 AYDNMKVVTTMLGVS--ESTILPLLNKVGLGDIDKRPvkqfslgmkqrlgiaislinspkLLILDEPTNGLDPIGIQELR 165
Cdd:cd03227 65 AAVSAELIFTRLQLSggEKELSALALILALASLKPRP-----------------------LYILDEIDRGLDPRDGQALA 121
|
170 180
....*....|....*....|....*...
gi 545668914 166 EIIESFKSEGMTIMISSHiLSEVEHLAD 193
Cdd:cd03227 122 EAILEHLVKGAQVIVITH-LPELAELAD 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-157 |
1.31e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMK---------------------------------ILT 48
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqevvgddttalqcVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 49 GLVSKT-----SGSIIFEGREWSRRDLRKIGSI-----IEEPP-------LYKNLSAYD----NMKVVTTMLGVSESTil 107
Cdd:PLN03073 258 TDIERTqlleeEAQLVAQQRELEFETETGKGKGankdgVDKDAvsqrleeIYKRLELIDaytaEARAASILAGLSFTP-- 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545668914 108 pllnkvglgDIDKRPVKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLD 157
Cdd:PLN03073 336 ---------EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
107-195 |
2.42e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 107 LPLLNKVGLGDID-KRPVKQFSLGMKQRLGIAISL---INSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISS 182
Cdd:TIGR00630 810 LQTLCDVGLGYIRlGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIE 889
|
90
....*....|...
gi 545668914 183 HILsEVEHLADFI 195
Cdd:TIGR00630 890 HNL-DVIKTADYI 901
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-195 |
3.82e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 17 LNNVNMNIPKGKVYALIGPNGAGKSTI--------------------------------MKILTGLvsktSGSIIFEGRE 64
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayarqflgqmdkpdVDSIEGL----SPAIAIDQKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 65 WSRRDLRKIGSIIEepplyknlsAYDNMKVVTTMLGVSEStiLPLLNKVGLGDID-KRPVKQFSLGMKQRLGIAiSLINS 143
Cdd:cd03270 87 TSRNPRSTVGTVTE---------IYDYLRLLFARVGIRER--LGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLA-TQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 144 P---KLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHlADFI 195
Cdd:cd03270 155 GltgVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-201 |
6.01e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.92 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 16 ILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRKI--GSIIEEPPLYKNLSAYDNMK 93
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWImpGTIKENIIFGVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 94 VVTTMLGVSESTILPLLNKVGLGDIDkrpvKQFSLGMKQRLGIAISLINSPKLLILDEPTNGLDpigIQELREIIESFKS 173
Cdd:cd03291 132 VVKACQLEEDITKFPEKDNTVLGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFGYLD---VFTEKEIFESCVC 204
|
170 180 190
....*....|....*....|....*....|
gi 545668914 174 EGMTIMISSHILSEVEHL--ADFIGFIYEG 201
Cdd:cd03291 205 KLMANKTRILVTSKMEHLkkADKILILHEG 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-216 |
1.08e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 1 MLKIQNLkkSYGKRTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIIFEGREWSRRDLRK-----IGS 75
Cdd:PRK10982 250 ILEVRNL--TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 76 IIEE---PPLYKNLSAYDNMKVvttmlgvseSTILPLLNKVGLGD-----------IDKRPVK---------QFSLGMKQ 132
Cdd:PRK10982 328 VTEErrsTGIYAYLDIGFNSLI---------SNIRNYKNKVGLLDnsrmksdtqwvIDSMRVKtpghrtqigSLSGGNQQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 133 RLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGK---IVLEKEY 209
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKTT 478
|
....*..
gi 545668914 210 DGSENLE 216
Cdd:PRK10982 479 TQNEILR 485
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
145-206 |
1.08e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668914 145 KLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHILSEVEHLADFIGFIYEGKIVLE 206
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
2-213 |
1.84e-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: 41.10 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKkSYGKRTILNNVNMNipKGKVYALIGPNGAGKSTIMKILT-GLVSKTSGsiifEGREWSRRDLRKIGsiieEP 80
Cdd:cd03279 6 LELKNFG-PFREEQVIDFTGLD--NNGLFLICGPTGAGKSTILDAITyALYGKTPR----YGRQENLRSVFAPG----ED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 81 PLYKNLSAYDNMKV--VTTMLGVSEST-----ILPLlnkvglGDIDK---RPVKQFSLG--MKQRLGIAISLIN------ 142
Cdd:cd03279 75 TAEVSFTFQLGGKKyrVERSRGLDYDQftrivLLPQ------GEFDRflaRPVSTLSGGetFLASLSLALALSEvlqnrg 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545668914 143 --SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISSHilseVEHLADFIGfiyeGKIVLEKEYDGSE 213
Cdd:cd03279 149 gaRLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH----VEELKERIP----QRLEVIKTPGGSR 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
144-206 |
2.85e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 2.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 144 PKLLILDEPTNGLDpIGIQ-ELREIIESFKSEGMT-IMISSHiLSEVEHLADFIGFIYEGKIVLE 206
Cdd:NF040905 423 PDVLILDEPTRGID-VGAKyEIYTIINELAAEGKGvIVISSE-LPELLGMCDRIYVMNEGRITGE 485
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-68 |
3.31e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 3.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 545668914 14 RTILNNVNMNIPKGKVYALIGPNGAGKSTIMKILTGLVSktsgsiIFEGREWSRR 68
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE------ISEGRVWAER 721
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-202 |
5.02e-04 |
|
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: 39.48 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 24 IPKGKVYALIGPNGAGKSTIMKILTGLVSKTSGSIifegrEWSRrdlrkigSIIEEPPLYKNLSAydnmkvvttmlgvse 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-----EWDG-------ITPVYKPQYIDLSG--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 104 stilpllnkvglgdidkrpvkqfslGMKQRLGIAISLINSPKLLILDEPTNGLDPIGIQELREIIESFKSEGM-TIMISS 182
Cdd:cd03222 75 -------------------------GELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVE 129
|
170 180
....*....|....*....|
gi 545668914 183 HILSEVEHLADFIgFIYEGK 202
Cdd:cd03222 130 HDLAVLDYLSDRI-HVFEGE 148
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
107-195 |
9.92e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 107 LPLLNKVGLGDID-KRPVKQFSLGMKQRLGIAISLIN---SPKLLILDEPTNGLDPIGIQELREIIESFKSEGMTIMISS 182
Cdd:cd03271 150 LQTLCDVGLGYIKlGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIE 229
|
90
....*....|...
gi 545668914 183 HILsEVEHLADFI 195
Cdd:cd03271 230 HNL-DVIKCADWI 241
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
120-211 |
1.35e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.14 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 120 KRPVK--QFSLGMKQRLGIAISLI--NSPKLLILDEPTNGLDPIGIQELREIIESFkSEGMTIMISSH---ILSEVEhlA 192
Cdd:COG4637 251 DRPFParELSDGTLRFLALLAALLspRPPPLLCIEEPENGLHPDLLPALAELLREA-SERTQVIVTTHspaLLDALE--P 327
|
90
....*....|....*....
gi 545668914 193 DFIgfiyegkIVLEKEYDG 211
Cdd:COG4637 328 EEV-------LVLEREDDG 339
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-185 |
1.99e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 2 LKIQNLKKSYGKRTIlnnvnmNIPKGkVYALIGPNGAGKSTIM---------------KILTGLVSK--TSGSIIFE--- 61
Cdd:COG0419 5 LRLENFRSYRDTETI------DFDDG-LNLIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVgsEEASVELEfeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668914 62 -GREW--SRRDLRKIGSIIEEPPLYK-------NLSAYDNMKVVTTMLG------VSESTILPLLNKVGLGDIDK-RPVK 124
Cdd:COG0419 78 gGKRYriERRQGEFAEFLEAKPSERKealkrllGLEIYEELKERLKELEealesaLEELAELQKLKQEILAQLSGlDPIE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545668914 125 QFSLGMKQRLGIAISLinspkLLILDepTNGLDPIGIQELREIIESfksegmtIMISSHIL 185
Cdd:COG0419 158 TLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEE-------LAIITHVI 204
|
|
| |
